<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE targets SYSTEM "http://targetdb.pdb.org/target.dtd">
<targets>

<target>
<id>YBL082C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MEGEQSPQGEKSLQRKQFVRPPLDLWQDLKDGVRYVIFDCRANLIVMPLLILFESMLCKI
IIKKVAYTEIDYKAYMEQIEMIQLDGMLDYSQVSGGTGPLVYPAGHVLIYKMMYWLTEGM
DHVERGQVFFRYLYLLTLALQMACYYLLHLPPWCVVLACLSKRLHSIYVLRLFNDCFTTL
FMVVTVLGAIVASRCHQRPKLKKSLALVISATYSMAVSIKMNALLYFPAMMISLFILNDA
NVILTLLDLVAMIAWQVAVAVPFLRSFPQQYLHCAFNFGRKFMYQWSINWQMMDEEAFND
KRFHLALLISHLIALTTLFVTRYPRILPDLWSSLCHPLRKNAVLNANPAKTIPFVLIASN
FIGVLFSRSLHYQFLSWYHWTLPILIFWSGMPFFVGPIWYVLHEWCWNSYPPNSQASTLL
LALNTVLLLLLALTQLSGSVALAKSHLRTTSSMEKKLN
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000178</url>
<remark>Standard Name: ALG3</remark>
<remark>
Dolichol-P-Man dependent alpha(1-3) mannosyltransferase, involved in the synthesis of dolichol-linked oligosaccharide donor for N-linked glycosylation of proteins
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_009471.1</databaseId>
</databaseRef>
</target>

<target>
<id>YBR085W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MSSDAKQQETNFAINFLMGGVSAAIAKTAASPIERVKILIQNQDEMIKQGTLDKKYSGIV
DCFKRTAKQEGLISFWRGNTANVIRYFPTQALNFAFKDKIKLMFGFKKEEGYGKWFAGNL
ASGGAAGALSLLFVYSLDFARTRLAADAKSSKKGGARQFNGLTDVYKKTLKSDGIAGLYR
GFMPSVVGIVVYRGLYFGMFDSLKPLVLTGSLDGSFLASFLLGWVVTTGASTCSYPLDTV
RRRMMMTSGQAVKYNGAIDCLKKIVASEGVGSLFKGCGANILRSVAGAGVISMYDQLQMI
LFGKKFK
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>ADP/ATP carrier</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000289</url>
<remark>Standard Name: AAC3</remark>
<remark>
Mitochondrial inner membrane ADP/ATP translocator, exchanges cytosolic ADP for mitochondrially synthesized ATP; expressed under anaerobic conditions; similar to Pet9p and Aac1p; has roles in maintenance of viability and in respiration
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_009642.1</databaseId>
</databaseRef>
</target>

<target>
<id>YBR243C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MLRLFSLALITCLIYYSKNQGPSALVAAVGFGIAGYLATDMLIPRVGKSFIKIGLFGKDL
SKPGRPVLPETIGAIPAAVYLFVMFIYIPFIFYKYMVITTSGGGHRDVSVVEDNGMNSNI
FPHDKLSEYLSAILCLESTVLLGIADDLFDLRWRHKFFLPAIAAIPLLMVYYVDFGVTHV
LIPGFMERWLKKTSVDLGLWYYVYMASMAIFCPNSINILAGVNGLEVGQCIVLAILALLN
DLLYFSMGPLATRDSHRFSAVLIIPFLGVSLALWKWNRWPATVFVGDTYCYFAGMVFAVV
GILGHFSKTMLLLFIPQIVNFIYSCPQLFKLVPCPRHRLPKFNEKDGLMYPSRANLKEEP
PKSIFKPILKLLYCLHLIDLEFDENNEIISTSNMTLINLTLVWFGPMREDKLCNTILKLQ
FCIGILALLGRHAIGAIIFGHDNLWTVR
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>UDP-N-acetyl-glucosamine-1-P transferase (GPT)</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000447</url>
<remark>Standard Name: ALG7</remark>
<remark>
UDP-N-acetyl-glucosamine-1-P transferase, transfers Glc-Nac-P from UDP-GlcNac to Dol-P in the ER in the first step of the dolichol pathway of protein asparagine-linked glycosylation; inhibited by tunicamycin
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_009802.1</databaseId>
</databaseRef>
</target>

<target>
<id>YCR011C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MGSHRRYLYYSILSFLLLSCSVVLAKQDKTPFFEGTSSKNSRLTAQDKGNDTCPPCFNCM
LPIFECKQFSECNSYTGRCECIEGFAGDDCSLPLCGGLSPDESGNKDRPIRAQNDTCHCD
NGWGGINCDVCQEDFVCDAFMPDPSIKGTCYKNGMIVDKVFSGCNVTNEKILQILNGKIP
QITFACDKPNQECNFQFWIDQLESFYCGLSDCAFEYDLEQNTSHYKCNDVQCKCVPDTVL
CGAKGSIDISDFLTETIKGPGDFSCDLETRQCKFSEPSMNDLILTVFGDPYITLKCESGE
CVHYSEIPGYKSPSKDPTVSWQGKLVLALTAVMVLALFTFATFYISKSPLFRNGLGSSKS
PIRLPDEDAVNNFLQNEDDTLATLSFENITYSVPSINSDGVEETVLNEISGIVKPGQILA
IMGGSGAGKTTLLDILAMKRKTGHVSGSIKVNGISMDRKSFSKIIGFVDQDDFLLPTLTV
FETVLNSALLRLPKALSFEAKKARVYKVLEELRIIDIKDRIIGNEFDRGISGGEKRRVSI
ACELVTSPLVLFLDEPTSGLDASNANNVIECLVRLSSDYNRTLVLSIHQPRSNIFYLFDK
LVLLSKGEMVYSGNAKKVSEFLRNEGYICPDNYNIADYLIDITFEAGPQGKRRRIRNISD
LEAGTDTNDIDNTIHQTTFTSSDGTTQREWAHLAAHRDEIRSLLRDEEDVEGTDGRRGAT
EIDLNTKLLHDKYKDSVYYAELSQEIEEVLSEGDEESNVLNGDLPTGQQSAGFLQQLSIL
NSRSFKNMYRNPKLLLGNYLLTILLSLFLGTLYYNVSNDISGFQNRMGLFFFILTYFGFV
TFTGLSSFALERIIFIKERSNNYYSPLAYYISKIMSEVVPLRVVPPILLSLIVYPMTGLN
MKDNAFFKCIGILILFNLGISLEILTIGIIFEDLNNSIILSVLVLLGSLLFSGLFINTKN
ITNVAFKYLKNFSVFYYAYESLLINEVKTLMLKERKYGLNIEVPGATILSTFGFVVQNLV
FDIKILALFNVVFLIMGYLALKWIVVEQK
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000604</url>
<remark>Standard Name: ADP1</remark>
<remark>
Putative ATP-dependent permease of the ABC transporter family of proteins
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_009937.2</databaseId>
</databaseRef>
</target>

<target>
<id>YCR021C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MNDTLSSFLNRNEALGLNPPHGLDMHITKRGSDWLWAVFAVFGFILLCYVVMFFIAENKG
SRLTRYALAPAFLITFFEFFAFFTYASDLGWTGVQAEFNHVKVSKSITGEVPGIRQIFYS
KYIAWFLSWPCLLFLIELAASTTGENDDISALDMVHSLLIQIVGTLFWVVSLLVGSLIKS
TYKWGYYTIGAVAMLVTQGVICQRQFFNLKTRGFNALMLCTCMVIVWLYFICWGLSDGGN
RIQPDGEAIFYGVLDLCVFAIYPCYLLIAVSRDGKLPRLSLTGGFSHHHATDDVEDAAPE
TKEAVPESPRASGETAIHEPEPEAEQAVEDTA
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000615</url>
<remark>Standard Name: HSP30</remark>
<remark>
Hydrophobic plasma membrane localized, stress-responsive protein that negatively regulates the H(+)-ATPase Pma1p; induced by heat shock, ethanol treatment, weak organic acid, glucose limitation, and entry into stationary phase
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_009950.1</databaseId>
</databaseRef>
</target>

<target>
<id>YDL015C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MPITIKSRSKGLRDTEIDLSKKPTLDDVLKKISANNHNISKYRIRLTYKKESKQVPVISE
SFFQEEADDSMEFFIKDLGPQISWRLVFFCEYLGPVLVHSLFYYLSTIPTVVDRWHSASS
DYNPFLNRVAYFLILGHYGKRLFETLFVHQFSLATMPIFNLFKNCFHYWVLSGLISFGYF
GYGFPFGNAKLFKYYSYLKLDDLSTLIGLFVLSELWNFYCHIKLRLWGDYQKKHGNAKIR
VPLNQGIFNLFVAPNYTFEVWSWIWFTFVFKFNLFAVLFLTVSTAQMYAWAQKKNKKYHT
RRAFLIPFVF
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>enoyl reductase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002173</url>
<remark>Standard Name: TSC13</remark>
<remark>
Enoyl reductase that catalyzes the last step in each cycle of very long chain fatty acid elongation, localizes to the ER, highly enriched in a structure marking nuclear-vacuolar junctions, coimmunoprecipitates with elongases Fen1p and Sur4p
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010269.1</databaseId>
</databaseRef>
</target>

<target>
<id>YDL035C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MITEGFPPNLNALKGSSLLEKRVDSLRQLNTTTVNQLLGLPGMTSTFTAPQLLQLRIIAI
TASAVSLIAGCLGMFFLSKMDKRRKVFRHDLIAFLIICDFLKAFILMIYPMIILINNSVY
ATPAFFNTLGWFTAFAIEGADMAIMIFAIHFAILIFKPNWKWRNKRSGNMEGGLYKKRSY
IWPITALVPAILASLAFINYNKLNDDSDTTIILDNNNYNFPDSPRQGGYKPWSAWCYLPP
KPYWYKIVLSWGPRYFIIIFIFAVYLSIYIFITSESKRIKAQIGDFNHNVLEEEKEKKKL
FGLGHWGKAKWYFRSYFKLPLLHLLRNLKNFFTISFIDPNEETDDSGSSNGTFNFGESSN
EIPTLFRKTNTGSDENVSASGGVRLLDYNSAKPLDMSKYAMSEQPDLERNNPFDCENDIT
LNPSELVSKQKEHKVTFSVENEGLDTRKSSMLGHQTFSCQNSLESPLAMYDNKNDNSDIT
SNIKEKGGIINNNSNNDDDDNNNNNDNDNDNNNSNNNNNNNNNNNNNNNNNNNNNNNNNN
NNNNSNNIKNNVDNNNTNPADNIPTLSNEAFTPSQQFSQERVNNNADRCENSSFTNVQQH
FQAQTYKQMKKRRAQIQKNLRAIFIYPLSYIGIWLFPIIADALQYNHEIKHGPTMWVTYI
DTCVRPLSCLVDVIVYLFKEKPWNYSWAKTESKYLIEKYILKGELGEKEILKFCHSNWGK
RGWYYRGKWKKRKCWKYSTNPLKRILWFVERFFKQLFELKLHFSFYDNCDDFEYWENYYS
AKDSNDNKRTESDETKTNSSDRSLPSNSLELQAMLNNITAEEVEVPLFWRIIHHIPMLGG
IDLDELNRLLKIRYNNDHFSLPGLKFALNQNKSHDKHQDVSTNSMVKSSFFSSNIVTNDD
ENSIEEDKNLRYSDASASENYLVKPTIPGTTPDPIIEAQNDNDSSDSSGIDLIAFLRNGP
L
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>G protein coupled receptor (GPCR)</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002193</url>
<remark>Standard Name: GPR1</remark>
<remark>
Plasma membrane G protein coupled receptor (GPCR) that interacts with the heterotrimeric G protein alpha subunit, Gpa2p, and with Plc1p; sensor that integrates nutritional signals with the modulation of cell fate via PKA and cAMP synthesis
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010249.1</databaseId>
</databaseRef>
</target>

<target>
<id>YDL093W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MNKEHLLKVDPIPDVTIKRGPLRSFLITKPCDNLSSLRTVTSSKEKLLVGCLLIFTAIVR
LHNISLPNSVVFGENEVGTFVSQYVNNIFFTDVHPPLVAMLYATVSSVFGYKGLFNYGNI
GTEYTANVPYVAMRFFSATLGIVSVLVLYLTLRVSGVKIAVAAICAVCFAIENSFVTLSR
FTLIEGPFVFFMACAVYFFRRSELYLPNSCKANKSLLAASIALGFAVSSKWAGLFTIAWA
GIIVLWRVWFMIGDLSRPIGSSIKYMAFQFTCLLAIPAFIYFLIFSVHIKTLNVNGISSS
FFPAEFRKTLKYNNVIKETVAEVAVGSAVSLNHVGTAGGYLHSHLHNYPAGSMQQQVTLY
PHIDQNNKWIIELAEHPNENVTSFQNLTDGTIIKLRQLKNGCRLHSHDHKPPVSQNADWQ
KEVSCYGYEGFEGDINDDWIIEIDKKRSEPGPAQEHIRAIETKFRLKHYLTGCYLFSHPE
KLPEWGFGQQEVTCAYFAREDLTSWYIEENENEISLPNPEKVSYKKMSFWQKFVAIHKFM
FYLNNYMDTSHAYSSEPKTWPLMLRGIDFWNENGREVYFLGNAVLWWSVTAFICTFIIGV
AVELLAWKLGVNILRDKHIINFHYQVFQYLLGFAAHYFPYFFVGQKLFLYDYLPAYYFGI
LAFGHALDLISTYISNKRNNTGYIVVAIFMVVCFYFFSEHSPLIYATGWSSNLCKRSKWL
GSWDFYCNSLLLSDSHYELNAES
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>dolichyl phosphate-D-mannose:protein O-D-mannosyltransferase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002251</url>
<remark>Standard Name: PMT5</remark>
<remark>
Protein O-mannosyltransferase, transfers mannose residues from dolichyl phosphate-D-mannose to protein serine/threonine residues; acts in a complex with Pmt3p, can instead interact with Pmt2p in some conditions; target for new antifungals
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010190.1</databaseId>
</databaseRef>
</target>

<target>
<id>YDL095W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSEEKTYKRVEQDDPVPELDIKQGPVRPFIVTDPSAELASLRTMVTLKEKLLVACLAVFT
AVIRLHGLAWPDSVVFDEVHFGGFASQYIRGTYFMDVHPPLAKMLYAGVASLGGFQGDFD
FENIGDSFPSTTPYVLMRFFSASLGALTVILMYMTLRYSGVRMWVALMSAICFAVENSYV
TISRYILLDAPLMFFIAAAVYSFKKYEMYPANSLNAYKSLLATGIALGMASSSKWVGLFT
VTWVGLLCIWRLWFMIGDLTKSSKSIFKVAFAKLAFLLGVPFALYLVFFYIHFQSLTLDG
DGASFFSPEFRSTLKNNKIPQNVVADVGIGSIISLRHLSTMGGYLHSHSHNYPAGSEQQQ
STLYPHMDANNDWLLELYNAPGESLTTFQNLTDGTKVRLFHTVTRCRLHSHDHKPPVSES
SDWQKEVSCYGYSGFDGDANDDWVVEIDKKNSAPGVAQERVIALDTKFRLRHAMTGCYLF
SHEVKLPAWGFEQQEVTCASSGRHDLTLWYVENNSNPLLPEDTKRISYKPASFISKFIES
HKKMWHINKNLVEPHVYESQPTSWPFLLRGISYWGENNRNVYLLGNAIVWWAVTAFIGIF
GLIVITELFSWQLGKPILKDSKVVNFHVQVIHYLLGFAVHYAPSFLMQRQMFLHHYLPAY
YFGILALGHALDIIVSYVFRSKRQMGYAVVITFLAASVYFFKSFSPIIYGTPWTQELCQK
SQWLSGWDYNCNTYFSSLEEYKNQTLTKRESQPAATSTVEEITIEGDGPSYEDLMNEDGK
KIFKDTEGNELDPEVVKKMLEEEGANILKVEKRAVLE
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>dolichyl phosphate-D-mannose:protein O-D-mannosyltransferase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002253</url>
<remark>Standard Name: PMT1</remark>
<remark>
Protein O-mannosyltransferase, transfers mannose residues from dolichyl phosphate-D-mannose to protein serine/threonine residues; acts in a complex with Pmt2p, can instead interact with Pmt3p in some conditions; target for new antifungals
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010188.1</databaseId>
</databaseRef>
</target>

<target>
<id>YDL212W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MFSYSDFCSIGTAMILSATTFLMGVFFSNMPYDYHLLFNPNSTQEHFDLALRHYQILHET
PLPVIVTLCVVAGIGLVGGTIKVFKPNPELQMFEYCSLGLYVLAICVFLTNVKTGIDCSV
SHNWGEVTENQGLAVIASSNIILLVMFAGVIILQIGLWYSNWDLQKRLKEFYAQEEREAA
NAGKKTEKVDNAKKNDNKSKGAQKRKNAKK
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002371</url>
<remark>Standard Name: SHR3</remark>
<remark>
Endoplasmic reticulum packaging chaperone, required for incorporation of amino acid permeases into COPII coated vesicles for transport to the cell surface
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010069.1</databaseId>
</databaseRef>
</target>

<target>
<id>YDR038C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MSEGTVKENNNEEFNAYHTLTTEEAAEFIGTSLTEGLTQDESLRRLKAVGENTLGDDTKI
DYKAMVLHQVCNAMIMVLVISMAISFAVRDWITGGVISFVIAVNVLIGLVQEYKATKTMN
SLKNLSSPNAHVIRNGKSETINSKDVVPGDICLVKVGDTIPADLRLIETKNFDTDESLLT
GESLPVSKDANLVFGKEEETSVGDRLNLAFSSSAVVKGRAKGIVIKTALNSEIGKIAKSL
QGDSGLISRDPSKSWLQNTWISTKKVTGAFLGTNVGTPLHRKLSKLAVLLFWIAVLFAII
VMASQKFDVDKRVAIYAICVALSMIPSSLVVVLTITMSVGAAVMVSRNVIVRKLDSLEAL
GAVNDICSDKTGTLTQGKMLARQIWIPRFGTITISNSDDPFNPNEGNVSLIPRFSPYEYS
HNEDGDVGILQNFKDRLYEKDLPEDIDMDLFQKWLETATLANIATVFKDDATDCWKAHGD
PTEIAIQVFATKMDLPHNALTGEKSTNQSNENDQSSLSQHNEKPGSAQFEHIAEFPFDST
VKRMSSVYYNNHNETYNIYGKGAFESIISCCSSWYGKDGVKITPLTDCDVETIRKNVYSL
SNEGLRVLGFASKSFTKDQVNDDQLKNITSNRATAESDLVFLGLIGIYDPPRNETAGAVK
KFHQAGINVHMLTGDFVGTAKAIAQEVGILPTNLYHYSQEIVDSMVMTGSQFDGLSEEEV
DDLPVLPLVIARCSPQTKVRMIEALHRRKKFCAMTGDGVNDSPSLKMANVGIAMGINGSD
VSKEASDIVLSDDNFASILNAVEEGRRMTDNIQKFVLQLLAENVAQALYLIIGLVFRDEN
GKSVFPLSPVEVLWIIVVTSCFPAMGLGLEKAAPDLMDRPPNDSEVGIFTWEVIIDTFAY
GIIMTGSCMASFTGSLYGINSGRLGHDCDGTYNSSCRDVYRSRSAAFATMTWCALILAWE
VVDMRRSFFRMHPDTDSPVKEFFRSIWGNQFLFWSIIFGFVSAFPVVYIPVINDKVFLHK
PIGAEWGLAIAFTIAFWIGAELYKCGKRRYFKTQRAHNSENDLERSSKHDPFEAYSTSTT
LQSEINISVKH
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>Na+ ATPase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002445</url>
<remark>Standard Name: ENA5</remark>
<remark>
Protein with similarity to P-type ATPase sodium pumps
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010323.1</databaseId>
</databaseRef>
</target>

<target>
<id>YDR135C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MAGNLVSWACKLCRSPEGFGPISFYGDFTQCFIDGVILNLSAIFMITFGIRDLVNLCKKK
HSGIKYRRNWIIVSRMALVLLEIAFVSLASLNISKEEAENFTIVSQYASTMLSLFVALAL
HWIEYDRSVVANTVLLFYWLFETFGNFAKLINILIRHTYEGIWYSGQTGFILTLFQVITC
ASILLLEALPKKPLMPHQHIHQTLTRRKPNPYDSANIFSRITFSWMSGLMKTGYEKYLVE
ADLYKLPRNFSSEELSQKLEKNWENELKQKSNPSLSWAICRTFGSKMLLAAFFKAIHDVL
AFTQPQLLRILIKFVTDYNSERQDDHSSLQGFENNHPQKLPIVRGFLIAFAMFLVGFTQT
SVLHQYFLNVFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLT
QWLNLIWSGPFQIIICLYSLYKLLGNSMWVGVIILVIMMPLNSFLMRIQKKLQKSQMKYK
DERTRVISEILNNIKSLKLYAWEKPYREKLEEVRNNKELKNLTKLGCYMAVTSFQFNIVP
FLVSCCTFAVFVYTEDRALTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRLFT
FFTNEELQPDSVQRLPKVKNIGDVAINIGDDATFLWQRKPEYKVALKNINFQAKKGNLTC
IVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSQVPWIMNGTVKENILFGHRYDAE
FYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPL
AAVDEHVARHLIEHVLGPNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEI
TKDADSPLWKLLNNYGKKNNGKSNEFGDSSESSVRESSIPVEGELEQLQKLNDLDFGNSD
AISLRRASDATLGSIDFGDDENIAKREHREQGKVKWNIYLEYAKACNPKSVCVFILFIVI
SMFLSVMGNVWLKHWSEVNSRYGSNPNAARYLAIYFALGIGSALATLIQTIVLWVFCTIH
ASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTF
TITVICATTWQFIFIIIPLSVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLA
TVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILGAATLSVFRLK
QGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYADLKSEAPLIVEGH
RPPKEWPSQGDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALF
RMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENIDPINQYTDEAIWR
ALELSHLKEHVLSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDEATAAV
DVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNKS
LFYSLCMEAGLVNEN
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002542</url>
<remark>Standard Name: YCF1</remark>
<remark>
Vacuolar glutathione S-conjugate transporter of the ATP-binding cassette family, has a role in detoxifying metals such as cadmium, mercury, and arsenite; also transports unconjugated bilirubin; similar to human cystic fibrosis protein CFTR
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010419.1</databaseId>
</databaseRef>
</target>

<target>
<id>YDR276C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MDSAKIINIILSLFLPPVAVFLARGWGTDCIVDIILTILAWFPGMLYALYIVLQD
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002684</url>
<remark>Standard Name: PMP3</remark>
<remark>
Small plasma membrane protein related to a family of plant polypeptides that are overexpressed under high salt concentration or low temperature, not essential for viability, deletion causes hyperpolarization of the plasma membrane potential
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010562.1</databaseId>
</databaseRef>
</target>

<target>
<id>YDR284C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MNRVSFIKTPFNIGAKWRLEDVFLLIIMILLNYPVYYQQPFERQFYINDLTISHPYATTE
RVNNNMLFVYSFVVPSLTILIIGSILADRRHLIFILYTSLLGLSLAWFSTSFFTNFIKNW
IGRLRPDFLDRCQPVEGLPLDTLFTAKDVCTTKNHERLLDGFRTTPSGHSSESFAGLGYL
YFWLCGQLLTESPLMPLWRKMVAFLPLLGAALIALSRTQDYRHHFVDVILGSMLGYIMAH
FFYRRIFPPIDDPLPFKPLMDDSDVTLEEAVTHQRIPDEELHPLSDEGM
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>diacylglycerol pyrophosphate phosphatase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002692</url>
<remark>Standard Name: DPP1</remark>
<remark>
Diacylglycerol pyrophosphate (DGPP) phosphatase, zinc-regulated vacuolar membrane-associated lipid phosphatase, dephosphorylates DGPP to phosphatidate (PA) and Pi, then PA to diacylglycerol; involved in lipid signaling and cell metabolism
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010570.1</databaseId>
</databaseRef>
</target>

<target>
<id>YDR503C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MISVMADEKHKEYFKLYYFQYMIIGLCTILFLYSEISLVPRGQNIEFSLDDPSISKRYVP
NELVGPLECLILSVGLSNMVVFWTCMFDKDLLKKNRVKRLRERPDGISNDFHFMHTSILC
LMLIISINAALTGALKLIIGNLRPDFVDRCIPDLQKMSDSDSLVFGLDICKQTNKWILYE
GLKSTPSGHSSFIVSTMGFTYLWQRVFTTRNTRSCIWCPLLALVVMVSRVIDHRHHWYDV
VSGAVLAFLVIYCCWKWTFTNLAKRDILPSPVSV
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>lipid phosphate phosphatase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002911</url>
<remark>Standard Name: LPP1</remark>
<remark>
Lipid phosphate phosphatase, catalyzes Mg(2+)-independent dephosphorylation of phosphatidic acid (PA), lysophosphatidic acid, and diacylglycerol pyrophosphate; involved in control of the cellular levels of phosphatidylinositol and PA
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010791.1</databaseId>
</databaseRef>
</target>

<target>
<id>YER018C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MASIDAFSDLERRMDGFQKDVAQVLARQQNHARQQLQQFQAEMRQLHNQHQHLIDELQRL
ATQRTALQQQIHAAQQATNTTREQWRSYHERESELSRRQSTLAAQSRELDSLLQQRGKEC
VQLRARWAAQSGNDAAEVALYERLLQLRVLPGASDVHDVRFVFGDDSRCWIEVAMHGDHV
IGNSHPALDPKSRATLEHVLTVQGDLAAFLVVARDMLLASL
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>spindle pole component</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000820</url>
<remark>Standard Name: SPC25</remark>
<remark>
Component of the evolutionarily conserved kinetochore-associated Ndc80 complex (Ndc80p-Nuf2p-Spc24p-Spc25p); involved in chromosome segregation, spindle checkpoint activity and kinetochore clustering
</remark>
<remark>PDB entries 2FV4 and 2FTX are related partial structures</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010934.1</databaseId>
</databaseRef>
</target>

<target>
<id>YER026C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MVESDEDFAPQEFPHTDTDVIVNEHRDENDGYASDEVGGTLSRRASSIFSINTTPLAPPN
ATDIQKFTSDEHHFSMMRNLHMADYITMLNGFSGFYSIVSCLRFTLTGKPHYVQRAHFFI
LLGMCFDFLDGRVARLRNRSSLMGQELDSLADLVSFGVAPAAIAFAIGFQTTFDVMILSF
FVLCGLARLARFNVTVAQLPKDSSTGKSKYFEGLPMPTTLALVLGMAYCVRKGLIFDNIP
FGIFREDQILEFHPIILVFFIHGCGMISKSLKIPKP
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>phosphatidylserine synthase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000828</url>
<remark>Standard Name: CHO1</remark>
<remark>
Phosphatidylserine synthase, functions in phospholipid biosynthesis; catalyzes the reaction CDP-diaclyglycerol + L-serine = CMP + L-1-phosphatidylserine, transcriptionally repressed by myo-inositol and choline
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010943.1</databaseId>
</databaseRef>
</target>

<target>
<id>YER072W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSSAPLLQRTPGKKIALPTRVEPKVFFANERTFLSWLNFTVMLGGLGVGLLNFGDKIGRV
SAGLFTFVAMGTMIYALVTYHWRAAAIRRRGSGPYDDRLGPTLLCFFLLVAVIINFILRL
KYNDANTKL
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000874</url>
<remark>Standard Name: VTC1</remark>
<remark>
Vacuolar transporter chaperon (VTC) involved in distributing V-ATPase and other membrane proteins; together with other VTC proteins, forms a heterotetrameric complex that associates with the SNARE Nyv1p and the V0 sector of the V-ATPase
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_010995.1</databaseId>
</databaseRef>
</target>

<target>
<id>YER118C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MSISSKIRPTPRKPSRMATDHSFKMKKFYADPFAISSISLAIVSWVIAIGGSISSASTNE
SFPRFTWWGIVYQFLIICSLMLFYCFDLVDHYRIFITTSIAVAFVYNTNSATNLVYADGP
KKAAASAGVILLSIINLIWILYYGGDNASPTNRWIDSFSIKGIRPSPLENSLHRARRRGN
RNTTPYQNNVYNDAIRDSGYATQFDGYPQQQPSHTNYVSSTALAGFENTQPNTSEAVNLH
LNTLQQRINSASNAKETNDNSNNQTNTNIGNTFDTDFSNGNTETTMGDTLGLYSDIGDDN
FIYKAKALYPYDADDDDAYEISFEQNEILQVSDIEGRWWKARRANGETGIIPSNYVQLID
GPEEMHR
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>transmembrane osmosensor</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000920</url>
<remark>Standard Name: SHO1</remark>
<remark>
Transmembrane osmosensor, participates in activation of both the Cdc42p- and MAP kinase-dependent filamentous growth pathway and the high-osmolarity glycerol response pathway
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_011043.1</databaseId>
</databaseRef>
</target>

<target>
<id>YFL026W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MSDAAPSLSNLFYDPTYNPGQSTINYTSIYGNGSTITFDELQGLVNSTVTQAIMFGVRCG
AAALTLIVMWMTSRSRKTPIFIINQVSLFLIILHSALYFKYLLSNYSSVTYALTGFPQFI
SRGDVHVYGATNIIQVLLVASIETSLVFQIKVIFTGDNFKRIGLMLTSISFTLGIATVTM
YFVSAVKGMIVTYNDVSATQDKYFNASTILLASSINFMSFVLVVKLILAIRSRRFLGLKQ
FDSFHILLIMSCQSLLVPSIIFILAYSLEPNQGTDVLTTVATLLAVLSLPLSSMWATAAN
NASKTNTITSDFTTSTDRFYPGTLSSFQTDSINNDAKSSLRSRLYDLYPRRKETTSDKHS
ERTFVSETADDIEKNQFYQLPTPTSSKNTRIGPFADASYKEGEVEPVDMYTPDTAADEEA
RKFWTEDNNNL
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>G protein coupled receptor (GPCR)|alpha-factor pheromone receptor</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001868</url>
<remark>Standard Name: STE2</remark>
<remark>
Receptor for alpha-factor pheromone; seven transmembrane-domain GPCR that interacts with both pheromone and a heterotrimeric G protein to initiate the signaling response that leads to mating between haploid a and alpha cells
</remark>
<remark>PDB entry 1PJD is a related partial structure</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_116627.1</databaseId>
</databaseRef>
</target>

<target>
<id>YGL006W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSRQDENSALLANNENNKPSYTGNENGVYDNFKLSKSQLSDLHNPKSIRSFVRLFGYESN
SLFKYLKTDKNAGISLPEISNYRKTNRYKNYGDNSLPERIPKSFLQLVWAAFNDKTMQLL
TVAAVVSFVLGLYELWMQPPQYDPEGNKIKQVDWIEGVAIMIAVFVVVLVSAANDYQKEL
QFAKLNKKKENRKIIVIRNDQEILISIHHVLVGDVISLQTGDVVPADCVMISGKCEADES
SITGESNTIQKFPVDNSLRDFKKFNSIDSHNHSKPLDIGDVNEDGNKIADCMLISGSRIL
SGLGRGVITSVGINSVYGQTMTSLNAEPESTPLQLHLSQLADNISVYGCVSAIILFLVLF
TRYLFYIIPEDGRFHDLDPAQKGSKFMNIFITSITVIVVAVPEGLPLAVTLALAFATTRM
TKDGNLVRVLRSCETMGSATAVCSDKTGTLTENVMTVVRGFPGNSKFDDSKSLPVSEQRK
LNSKKVFEENCSSSLRNDLLANIVLNSTAFENRDYKKNDKNTNGSKNMSKNLSFLDKCKS
RLSFFKKGNREDDEDQLFKNVNKGRQEPFIGSKTETALLSLARLSLGLQPGELQYLRDQP
MEKFNIEKVVQTIPFESSRKWAGLVVKYKEGKNKKPFYRFFIKGAAEIVSKNCSYKRNSD
DTLEEINEDNKKETDDEIKNLASDALRAISVAHKDFCECDSWPPEQLRDKDSPNIAALDL
LFNSQKGLILDGLLGIQDPLRAGVRESVQQCQRAGVTVRMVTGDNILTAKAIARNCAILS
TDISSEAYSAMEGTEFRKLTKNERIRILPNLRVLARSSPEDKRLLVETLKGMGDVVAVTG
DGTNDAPALKLADVGFSMGISGTEVAREASDIILMTDDFSAIVNAIKWGRCVSVSIKKFI
QFQLIVNITAVILTFVSSVASSDETSVLTAVQLLWINLIMDTLAALALATDKPDPNIMDR
KPRGRSTSLISVSTWKMILSQATLQLIVTFILHFYGPELFFKKHEDEITSHQQQQLNAMT
FNTFVWLQFFTMLVSRKLDEGDGISNWRGRISAANLNFFQDLGRNYYFLTIMAIIGSCQV
LIMFFGGAPFSIARQTKSMWITAVLCGMLSLIMGVLVRICPDEVAVKVFPAAFVQRFKYV
FGLEFLRKNHTGKHDDEEALLEESDSPESTAFY
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002974</url>
<remark>Standard Name: PMC1</remark>
<remark>
Vacuolar Ca2+ ATPase involved in depleting cytosol of Ca2+ ions; prevents growth inhibition by activation of calcineurin in the presence of elevated concentrations of calcium; similar to mammalian PMCA1a
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_011509.1</databaseId>
</databaseRef>
</target>

<target>
<id>YGL008C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MTDTSSSSSSSSASSVSAHQPTQEKPAKTYDDAASESSDDDDIDALIEELQSNHGVDDED
SDNDGPVAAGEARPVPEEYLQTDPSYGLTSDEVLKRRKKYGLNQMADEKESLVVKFVMFF
VGPIQFVMEAAAILAAGLSDWVDFGVICGLLMLNAGVGFVQEFQAGSIVDELKKTLANTA
VVIRDGQLVEIPANEVVPGDILQLEDGTVIPTDGRIVTEDCFLQIDQSAITGESLAVDKH
YGDQTFSSSTVKRGEGFMVVTATGDNTFVGRAAALVNKAAGGQGHFTEVLNGIGIILLVL
VIATLLLVWTACFYRTNGIVRILRYTLGITIIGVPVGLPAVVTTTMAVGAAYLAKKQAIV
QKLSAIESLAGVEILCSDKTGTLTKNKLSLHEPYTVEGVSPDDLMLTACLAASRKKKGLD
AIDKAFLKSLKQYPKAKDALTKYKVLEFHPFDPVSKKVTAVVESPEGERIVCVKGAPLFV
LKTVEEDHPIPEDVHENYENKVAELASRGFRALGVARKRGEGHWEILGVMPCMDPPRDDT
AQTVSEARHLGLRVKMLTGDAVGIAKETCRQLGLGTNIYNAERLGLGGGGDMPGSELADF
VENADGFAEVFPQHKYRVVEILQNRGYLVAMTGDGVNDAPSLKKADTGIAVEGATDAARS
AADIVFLAPGLSAIIDALKTSRQIFHRMYSYVVYRIALSLHLEIFLGLWIAILDNSLDID
LIVFIAIFADVATLAIAYDNAPYSPKPVKWNLPRLWGMSIILGIVLAIGSWITLTTMFLP
KGGIIQNFGAMNGIMFLQISLTENWLIFITRAAGPFWSSIPSWQLAGAVFAVDIIATMFT
LFGWWSENWTDIVTVVRVWIWSIGIFCVLGGFYYEMSTSEAFDRLMNGKPMKEKKSTRSV
EDFMAAMQRVSTQHEKET
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>plasma membrane H+-ATPase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002976</url>
<remark>Standard Name: PMA1</remark>
<remark>
Plasma membrane H+-ATPase, pumps protons out of the cell; major regulator of cytoplasmic pH and plasma membrane potential; part of the P2 subgroup of cation-transporting ATPases
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_011507.1</databaseId>
</databaseRef>
</target>

<target>
<id>YGL054C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MGAWLFILAVVVNCINLFGQVHFTILYADLEADYINPIELCSKVNKLITPEAALHGALSL
LFLLNGYWFVFLLNLPVLAYNLNKIYNKVQLLDATEIFRTLGKHKRESFLKLGFHLLMFF
FYLYRMIMALIAESGDDF
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003022</url>
<remark>Standard Name: ERV14</remark>
<remark>
Protein localized to COPII-coated vesicles, involved in vesicle formation and incorporation of specific secretory cargo; required for the delivery of bud-site selection protein Axl2p to cell surface; related to Drosophila cornichon
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_011461.1</databaseId>
</databaseRef>
</target>

<target>
<id>YGL167C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSDNPFNASLLDEDSNREREILDATAEALSKPSPSLEYCTLSVDEALEKLDTDKNGGLRS
SNEANNRRSLYGPNEITVEDDESLFKKFLSNFIEDRMILLLIGSAVVSLFMGNIDDAVSI
TLAIFIVVTVGFVQEYRSEKSLEALNKLVPAECHLMRCGQESHVLASTLVPGDLVHFRIG
DRIPADIRIIEAIDLSIDESNLTGENEPVHKTSQTIEKSSFNDQPNSIVPISERSCIAYM
GTLVKEGHGKGIVVGTGTNTSFGAVFEMMNNIEKPKTPLQLTMDKLGKDLSLVSFIVIGM
ICLVGIIQGRSWLEMFQISVSLAVAAIPEGLPIIVTVTLALGVLRMAKRKAIVRRLPSVE
TLGSVNVICSDKTGTLTSNHMTVSKLWCLDSMSNKLNVLSLDKNKKTKNSNGNLKNYLTE
DVRETLTIGNLCNNASFSQEHAIFLGNPTDVALLEQLANFEMPDIRNTVQKVQELPFNSK
RKLMATKILNPVDNKCTVYVKGAFERILEYSTSYLKSKGKKTEKLTEAQKATINECANSM
ASEGLRVFGFAKLTLSDSSTPLTEDLIKDLTFTGLIGMNDPPRPNVKFAIEQLLQGGVHI
IMITGDSENTAVNIAKQIGIPVIDPKLSVLSGDKLDEMSDDQLANVIDHVNIFARATPEH
KLNIVRALRKRGDVVAMTGDGVNDAPALKLSDIGVSMGRIGTDVAKEASDMVLTDDDFST
ILTAIEEGKGIFNNIQNFLTFQLSTSVAALSLVALSTAFKLPNPLNAMQILWINILMDGP
PAQSLGVEPVDHEVMKKPPRKRTDKILTHDVMKRLLTTAACIIVGTVYIFVKEMAEDGKV
TARDTTMTFTCFVFFDMFNALACRHNTKSIFEIGFFTNKMFNYAVGLSLLGQMCAIYIPF
FQSIFKTEKLGISDILLLLLISSSVFIVDELRKLWTRKKNEEDSTYFSNV
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>Ca2+-translocating ATPase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003135</url>
<remark>Standard Name: PMR1</remark>
<remark>
High affinity Ca2+/Mn2+ P-type ATPase required for Ca2+ and Mn2+ transport into Golgi; involved in Ca2+ dependent protein sorting and processing; mutations in human homolog ATP2C1 cause acantholytic skin condition Hailey-Hailey disease
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_011348.1</databaseId>
</databaseRef>
</target>

<target>
<id>YGR049W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MQVSPAIVKGIAVSSLGLYAGILTSSTVISITTPINVLTQHLKNVLCTLGCWSTVLGGLA
TGAFGLSYYLAAPGERPNYLLCGLGVAPLSAAYLYLVSLFNHKLAPKCTRDQNDLEKQKD
EKLPQHHPEVKDGEAACPFSKMNNAKTLKPESERSVKCHSYMSLHMSIVTGITIFTFGKC
ILDGFKA
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003281</url>
<remark>Standard Name: SCM4</remark>
<remark>
Potential regulatory effector of CDC4 function, suppresses a temperature-sensitive allele of CDC4, tripartite protein structure in which a charged region separates two uncharged domains, not essential for mitosis or meiosis
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_011563.1</databaseId>
</databaseRef>
</target>

<target>
<id>YGR172C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSFYNTSNNANNGGGFYQPSAQFAVPQGSMSFQNTVGSSNTGNDNNLGVAPDPLPVGILH
ALSTKGYPHEPPLLEEIGINFDHIITKTKMVLIPIRFGSGVPQEILNDSDLAGPLIFFLL
FGLFLLMAGKVHFGYIYGVALFGTISLHNLSKLMSNNDTSTQTNLQFFNTASILGYCFLP
LCFLSLLGIFHGLNNTTGYVVSVLFVIWSTWTSSGFLNSLLQLQNARLLIAYPLLIFYSV
FALMVIFV
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003404</url>
<remark>Standard Name: YIP1</remark>
<remark>
Integral membrane protein required for the biogenesis of ER-derived COPII transport vesicles; interacts with Yif1p and Yos1p; localizes to the Golgi, the ER, and COPII vesicles
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_011688.1</databaseId>
</databaseRef>
</target>

<target>
<id>YGR175C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSAVNVAPELINADNTITYDAIVIGAGVIGPCVATGLARKGKKVLIVERDWAMPDRIVGE
LMQPGGVRALRSLGMIQSINNIEAYPVTGYTVFFNGEQVDIPYPYKADIPKVEKLKDLVK
DGNDKVLEDSTIHIKDYEDDERERGVAFVHGRFLNNLRNITAQEPNVTRVQGNCIEILKD
EKNEVVGAKVDIDGRGKVEFKAHLTFICDGIFSRFRKELHPDHVPTVGSSFVGMSLFNAK
NPAPMHGHVILGSDHMPILVYQISPEETRILCAYNSPKVPADIKSWMIKDVQPFIPKSLR
PSFDEAVSQGKFRAMPNSYLPARQNDVTGMCVIGDALNMRHPLTGGGMTVGLHDVVLLIK
KIGDLDFSDREKVLDELLDYHFERKSYDSVINVLSVALYSLFAADSDNLKALQKGCFKYF
QRGGDCVNKPVEFLSGVLPKPLQLTRVFFAVAFYTIYLNMEERGFLGLPMALLEGIMILI
TAIRVFTPFLFGELIG
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>squalene monooxygenase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003407</url>
<remark>Standard Name: ERG1</remark>
<remark>
Squalene epoxidase, catalyzes the epoxidation of squalene to 2,3-oxidosqualene; plays an essential role in the ergosterol-biosynthesis pathway and is the specific target of the antifungal drug terbinafine
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_011691.1</databaseId>
</databaseRef>
</target>

<target>
<id>YHR005C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MGCTVSTQTIGDESDPFLQNKRANDVIEQSLQLEKQRDKNEIKLLLLGAGESGKSTVLKQ
LKLLHQGGFSHQERLQYAQVIWADAIQSMKILIIQARKLGIQLDCDDPINNKDLFACKRI
LLKAKALDYINASVAGGSDFLNDYVLKYSERYETRRRVQSTGRAKAAFDEDGNISNVKSD
TDRDAETVTQNEDADRNNSSRINLQDICKDLNQEGDDQMFVRKTSREIQGQNRRNLIHED
IAKAIKQLWNNDKGIKQCFARSNEFQLEGSAAYYFDNIEKFASPNYVCTDEDILKGRIKT
TGITETEFNIGSSKFKVLDAGGQRSERKKWIHCFEGITAVLFVLAMSEYDQMLFEDERVN
RMHESIMLFDTLLNSKWFKDTPFILFLNKIDLFEEKVKSMPIRKYFPDYQGRVGDAEAGL
KYFEKIFLSLNKTNKPIYVKRTCATDTQTMKFVLSAVTDLIIQQNLKKIGII
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>G protein alpha subunit</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001047</url>
<remark>Standard Name: GPA1</remark>
<remark>
GTP-binding alpha subunit of the heterotrimeric G protein that couples to pheromone receptors; negatively regulates the mating pathway by sequestering G(beta)gamma and by triggering an adaptive response; activates Vps34p at the endosome
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_011868.1</databaseId>
</databaseRef>
</target>

<target>
<id>YHR123W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MGYFVPDSHIENLKSYKYQSEDRSLVSKYFLKPFWQRFCHIFPTWMAPNIITLSGFAFIV
INVLTVFYYDPNLNTDTPRWTYFSYALGVFLYQTFDGCDGVHARRINQSGPLGELFDHSI
DAINSTLSIFIFASETGMGFSYNLMLSQFAMLTNFYLSTWEEYHTHTLYLSEFSGPVEGI
LIVCVSLILTGIYGKQVIWHTYLFTITVGDKVIDVDTLDIVFSLAVFGLVMNALSAKRNV
DKYYRNSTSSANNITQIEQDSAIKGLLPFFAYYASIALLVWMQPSFITLSFILSVGFTGA
FTVGRIIVCHLTKQSFPMFNAPMLIPLCQIVLYKICLSLWGIESNKIVFALSWLGFGLSL
GVHIMFMNDIIHEFTEYLDVYALSIKRSKLT
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>sn-1,2-diacylglycerol ethanolamine- and cholinephosphotranferase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001165</url>
<remark>Standard Name: EPT1</remark>
<remark>
sn-1,2-diacylglycerol ethanolamine- and cholinephosphotranferase; not essential for viability
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_011991.1</databaseId>
</databaseRef>
</target>

<target>
<id>YIL114C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MALRFFNDISRDVNGLFNRDFFHTNPLSLNISTTTENGVNFTLKAKQGVTEGPIQTSVEG
RFYDRKEGVSLSQSWSNQNRLNTRIEFSKIAPGWKGDVNAFLTPQSIKNAKFNLSYAQKS
FAARTSIDILQPKDFVGSVTLGHRGFVGGTDIAYDTAAGLCARYAMSIGYLAREYSFILS
TNNRQCATASFFQNVNRYLQVGTKATLQSKTSSNMNIEFVTRYVPDSISQVKAKIADSGL
TTLSYKRNLNKDISLGVGMSFNALQLTEPVHKFGWSLSFSP
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>voltage dependent anion channel (YVDAC2)</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001376</url>
<remark>Standard Name: POR2</remark>
<remark>
Putative mitochondrial porin (voltage-dependent anion channel), related to Por1p but not required for mitochondrial membrane permeability or mitochondrial osmotic stability
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012152.1</databaseId>
</databaseRef>
</target>

<target>
<id>YJL004C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MVSIRRYLRVPNELKPSQIFKQDSLSPSKIGLQIVLLQIFYYTTAIVLFYCWAKLAGYDL
NIKEWLFSWENIDFTNAYGLSISLLWLLDSLICVFFLTVIVGRSKLAWDFAITIHAINFI
VVFLYTRKFPSFSWFFLQILSSLILIFLGTWTTRWRELRDTFFEGLVDPNEGEVGLVTPS
QQHSNHSELEQSPIQLKDLESQI
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003541</url>
<remark>Standard Name: SYS1</remark>
<remark>
Integral membrane protein of the Golgi required for targeting of the Arf-like GTPase Arl3p to the Golgi; multicopy suppressor of ypt6 null mutation
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012530.1</databaseId>
</databaseRef>
</target>

<target>
<id>YJL129C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MHFRRTMSRVPTLASLEIRYKKSFGHKFRDFIALCGHYFAPVKKYIFPSFIAVHYFYTIS
LTLITSILLYPIKNTRYIDTLFLAAGAVTQGGLNTVDINNLSLYQQIVLYIVCCISTPIA
VHSCLAFVRLYWFERYFDGIRDSSRRNFKMRRTKTILERELTARTMTKNRTGTQRTSYPR
KQAKTDDFQEKLFSGEMVNRDEQDSVHSDQNSHDISRDSSNNNTNHNGSSGSLDDFVKED
ETDDNGEYQENNSYSTVGSSSNTVADESLNQKPKPSSLRFDEPHSKQRPARVPSEKFAKR
RGSRDISPADMYRSIMMLQGKHEATAEDEGPPLVIGSPADGTRYKSNVNKLKKATGINGN
KIKIRDKGNESNTDQNSVSSEANSTASVSDESSLHTNFGNKVPSLRTNTHRSNSGPIAIT
DNAETDKKHGPSIQFDITKPPRKISKRVSTFDDLNPKSSVLYRKKASKKYLMKHFPKARR
IRQQIKRRLSTGSIEKNSSNNVSDRKPITDMDDDDDDDDNDGDNNEEYFADNESGDEDER
VQQSEPHSDSELKSHQQQQEKHQLQQNLHRMYKTKSFDDNRSRAVPMERSRTIDMAEAKD
LNELARTPDFQKMVYQNWKAHHRKKPNFRKRGWNNKIFEHGPYASDSDRNYPDNSNTGNS
ILHYAESILHHDGSHKNGSEEASSDSNENIYSTNGGSDHNGLNNYPTYNDDEEGYYGLHF
DTDYDLDPRHDLSKGSGKTYLSWQPTIGRNSNFLGLTRAQKDELGGVEYRAIKLLCTILV
VYYVGWHIVAFVMLVPWIILKKHYSEVVRDDGVSPTWWGFWTAMSAFNDLGLTLTPNSMM
SFNKAVYPLIVMIWFIIIGNTGFPILLRCIIWIMFKISPDLSQMRESLGFLLDHPRRCFT
LLFPKAATWWLLLTLAGLNITDWILFIILDFGSTVVKSLSKGYRVLVGLFQSVSTRTAGF
SVVDLSQLHPSIQVSYMLMMYVSVLPLAISIRRTNVYEEQSLGLYGDMGGEPEDTDTEDD
GNDEDDDEENESHEGQSSQRSSSNNNNNNNRKKKKKKKTENPNEISTKSFIGAHLRKQLS
FDLWFLFLGLFIICICEGDKIKDVQEPNFNIFAILFEIVSAYGTVGLSLGYPDTNQSFSR
QFTTLSKLVIIAMLIRGKNRGLPYSLDRAIILPSDRLEHIDHLEGMKLKRQARTNTEDPM
TEHFKRSFTDVKHRWGALKRKTTHSRNPKRSSTTL
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>180 kDa high affinity potassium transporter</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003665</url>
<remark>Standard Name: TRK1</remark>
<remark>
Component of the Trk1p-Trk2p potassium transport system; 180 kDa high affinity potassium transporter; phosphorylated in vivo and interacts physically with the phosphatase Ppz1p, suggesting Trk1p acitivy is regulated by phosphorylation
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012406.1</databaseId>
</databaseRef>
</target>

<target>
<id>YJL143W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSADHSRDPCPIVILNDFGGAFAMGAIGGVVWHGIKGFRNSPLGERGSGAMSAIKARAPV
LGGNFGVWGGLFSTFDCAVKAVRKREDPWNAIIAGFFTGGALAVRGGWRHTRNSSITCAC
LLGVIEGVGLMFQRYAAWQAKPMAPPLPEAPSSQPLQA
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003679</url>
<remark>Standard Name: TIM17</remark>
<remark>
Essential constituent of the mitochondrial inner membrane presequence translocase; interacts with Pam18p to recruit the presequence translocase-associated motor (PAM complex) and also required for protein sorting during import
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012392.1</databaseId>
</databaseRef>
</target>

<target>
<id>YJR073C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MKESVQEIIQQLIHSVDLQSSKFQLAIVCTMFNPIFWNIVARMEYHKHSLTKMCGGARKG
CYMLAATIFSLGIVRDMVYESALREQPTCSLITGENWTKLGVALFGLGQVLVLSSMYKLG
ITGTYLGDYFGILMDERVTGFPFNVSNNPMYQGSTLSFLGIALYKGKPAGLVVSAVVYFM
YKIALRWEEPFTAMIYANRDKAKKNM
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>unsaturated phospholipid N-methyltransferase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003834</url>
<remark>Standard Name: OPI3</remark>
<remark>
Phospholipid methyltransferase (methylene-fatty-acyl-phospholipid synthase), catalyzes the last two steps in phosphatidylcholine biosynthesis
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012607.1</databaseId>
</databaseRef>
</target>

<target>
<id>YJR086W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MTSVQNSPRLQQPQEQQQQQQQLSLKIKQLKLKRINELNNKLRKELSRERITASNACLTI
INYTSNTKDYTLPELWGYPVAGSNHFIEGLKNAQKNSQMSNSNSVCCTLM
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>G protein gamma subunit</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003846</url>
<remark>Standard Name: STE18</remark>
<remark>
G protein gamma subunit, forms a dimer with Ste4p to activate the mating signaling pathway, forms a heterotrimer with Gpa1p and Ste4p to dampen signaling; C-terminus is palmitoylated and farnesylated, which are required for normal signaling
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012619.1</databaseId>
</databaseRef>
</target>

<target>
<id>YJR117W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<status>Soluble</status>
<status>Purified</status>
<status>Crystallized</status>
<sequence>
MFDLKTILDHPNIPWKLIISGFSIAQFSFESYLTYRQYQKLSETKLPPVLEDEIDDETFH
KSRNYSRAKAKFSIFGDVYNLAQKLVFIKYDLFPKIWHMAVSLLNAVLPVRFHMVSTVAQ
SLCFLGLLSSLSTLVDLPLSYYSHFVLEEKFGFNKLTVQLWITDMIKSLTLAYAIGGPIL
YLFLKIFDKFPTDFLWYIMVFLFVVQILAMTIIPVFIMPMFNKFTPLEDGELKKSIESLA
DRVGFPLDKIFVIDGSKRSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIG
HWQKNHIVNMVIFSQLHTFLIFSLFTSIYRNTSFYNTFGFFLEKSTGSFVDPVITKEFPI
IIGFMLFNDLLTPLECAMQFVMSLISRTHEYQADAYAKKLGYKQNLCRALIDLQIKNLST
MNVDPLYSSYHYSHPTLAERLTALDYVSEKKKN
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>zinc metallo-protease</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003878</url>
<remark>Standard Name: STE24</remark>
<remark>
Highly conserved zinc metalloprotease that functions in two steps of a-factor maturation, C-terminal CAAX proteolysis and the first step of N-terminal proteolytic processing; contains multiple transmembrane spans
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012651.1</databaseId>
</databaseRef>
</target>

<target>
<id>YJR118C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MAQALNSTNIAFFRVAFLFTIAFFCLKNVNSILQNTYFIVLTQAMNLPQLTLSRYSGQLG
LFALLFTLNGVHDLIPLLENNVKYFQSVVPVRLLIFFILTSISYLWESNFYVHNNSVFIY
CFAEVWINFLLYNAIREEKNEEFKRLNQFMVNDEDIEEPQPFTVKTETTEIIEIINDEEN
DDEDGKDNDDNNEKGNDDSDAKK
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003879</url>
<remark>Standard Name: ILM1</remark>
<remark>
Protein of unknown function; may be involved in mitochondrial DNA maintenance; required for slowed DNA synthesis-induced filamentous growth
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012652.1</databaseId>
</databaseRef>
</target>

<target>
<id>YKL119C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MFEIKLNDRITEFLRKFKNSAKSNEGIDEDIDLFLKRHAIPMQSLLFYVKEYRKDSDLQC
SIKELLKPLEFEFKPKAVRGLHYSEDFKKKLEFLKYQEQELEYQSMVKRSKSVFSLQEDD
ELTPSQINKQIKEQVTTVFNVLVSVISVVVAIWYWTGSSTNFPVHVRLLLCLFFGILVLV
ADVVVYNSYLKKLEEAKVKEKTKVEKKKVLSKITL
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001602</url>
<remark>Standard Name: VPH2</remark>
<remark>
Integral membrane protein required for vacuolar H+-ATPase (V-ATPase) function, although not an actual component of the V-ATPase complex; functions in the assembly of the V-ATPase; localized to the endoplasmic reticulum (ER)
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012803.1</databaseId>
</databaseRef>
</target>

<target>
<id>YKL178C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MSYKSAIIGLCLLAVILLAPPLAWHSHTKNIPAIILITWLLTMNLTCIVDAAIWSDDDFL
TRWDGKGWCDIVIKLQVGANIGISCAVTNIIYNLHTILKADSVLPDLSSWTKIVKDLVIS
LFTPVMVMGFSYLLQVFRYGIARYNGCQNLLSPTWITTVLYTMWMLIWSFVGAVYATLVL
FVFYKKRKDVRDILHCTNSGLNLTRFARLLIFCFIIILVMFPFSVYTFVQDLQQVEGHYT
FKNTHSSTIWNTIIKFDPGRPIYNIWLYVLMSYLVFLIFGLGSDALHMYSKFLRSIKLGF
VLDMWKRFIDKNKEKRVGILLNKLSSRKESRNPFSTDSENYISTCTENYSPCVGTPISQA
HFYVDYRIPDDPRKSQNKSKKYLFADKETDDILDEIDLKESRHIPYVTQGQSFDDEISLG
GFSKVTLDYSEKLHNSASSNFEGESLCYSPASKEENSSSNEHSSENTAGP
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>G protein coupled receptor (GPCR)|a-factor receptor</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001661</url>
<remark>Standard Name: STE3</remark>
<remark>
Receptor for a factor receptor, transcribed in alpha cells and required for mating by alpha cells, couples to MAP kinase cascade to mediate pheromone response; ligand bound receptors are endocytosed and recycled to the plasma membrane; GPCR
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012743.1</databaseId>
</databaseRef>
</target>

<target>
<id>YKL212W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MTGPIVYVQNADGIFFKLAEGKGTNDAVIHLANQDQGVRVLGAEEFPVQGEVVKIASLMG
FIKLKLNRYAIIANTVEETGRFNGHVFYRVLQHSIVSTKFNSRIDSEEAEYIKLLELHLK
NSTFYFSYTYDLTNSLQRNEKVGPAASWKTADERFFWNHYLTEDLRNFAHQDPRIDSFIQ
PVIYGYAKTVDAVLNATPIVLGLITRRSIFRAGTRYFRRGVDKDGNVGNFNETEQILLAE
NPESEKIHVFSFLQTRGSVPIYWAEINNLKYKPNLVLGENSLDATKKHFDQQKELYGDNY
LVNLVNQKGHELPVKEGYESVVHALNDPKIHYVYFDFHHECRKMQWHRVKLLIDHLEKLG
LSNEDFFHKVIDSNGNTVEIVNEQHSVVRTNCMDCLDRTNVVQSVLAQWVLQKEFESADV
VATGSTWEDNAPLLTSYQNLWADNADAVSVAYSGTGALKTDFTRTGKRTRLGAFNDFLNS
ASRYYQNNWTDGPRQDSYDLFLGGFRPHTASIKSPFPDRRPVYIQLIPMIICAALTVLGA
TIFFPKDRFTSSKNLLYFAGASIVLALSTKFMFKNGIQFVNWPKLVDVGFLVVHQTHDKE
QQFKGLKYAQSPKFSKPDPLKRD
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>phosphoinositide phosphatase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001695</url>
<remark>Standard Name: SAC1</remark>
<remark>
Lipid phosphoinositide phosphatase of the ER and Golgi, involved in protein trafficking and secretion
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012710.1</databaseId>
</databaseRef>
</target>

<target>
<id>YKR050W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MPTAKRTSSRASLALPFQLRLVHKKSWGHRLRDFISGFLKSCRPIAKYVFPNFIVVHYIY
LITLSIIGSILLYPCKNTAFIDVLFLAAGASTQGGLATKSTNDFNLYQQIVVYVITLLST
PILIHGFLAFVRLYWFERYFDNIRDISKQNFKLRRTMTLQQRELSGSSGNAARSRSFKDN
LFRGKFVSREDPRQSASDVPMDSPDTSALSSISPLNVSSSKEESSDTQSSPPNFSSKRQP
SDVDPRDIYKSIMMLQKQQEKSNANSTDSFSSETNGPAFIVQERHERRAPHCSLKRHSVL
PSSQELNKLAQTKSFQKLLGLRRDEGDHDYFDGAPHKYMVTKKKKISRTQSCNIPTYTAS
PSPKTSGQVVENHRNLAKSAPSSFVDEEMSFSPQESLNLQFQAHPPKPKRREGDIGHPFT
RTMSTNYLSWQPTFGRNSVFIGLTKQQKEELGGVEYRALRLLCCILMVYYIGFNILAFVT
IVPWACTRHHYSEIIRRNGVSPTWWGFFTAMSAFSNLGLSLTADSMVSFDTAPYPLIFMM
FFIIIGNTGFPIMLRFIIWIMFKTSRDLSQFKESLGFLLDHPRRCFTLLFPSGPTWWLFT
TLVVLNATDWILFIILDFNSAVVRQVAKGYRALMGLFQSVCTRTAGFNVVDLSKLHPSIQ
VSYMLMMYVSVLPLAISIRRTNVYEEQSLGLYDSGQDDENITHEDDIKETDHDGESEERD
TVSTKSKPKKQSPKSFVGAHLRRQLSFDLWYLFLGLFIICICEGRKIEDVNKPDFNVFAI
LFEVVSAYGTVGLSLGYPNTNTSLSAQFTVLSKLVIIAMLIRGRNRGLPYTLDRAIMLPS
DKLEQIDRLQDMKAKGKLLAKVGEDPMTTYVKKRSHKLKKIATKFWGKH
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>low affinity potassium transport</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001758</url>
<remark>Standard Name: TRK2</remark>
<remark>
Component of the Trk1p-Trk2p potassium transport system
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012976.1</databaseId>
</databaseRef>
</target>

<target>
<id>YKR067W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSAPAADHNAAKPIPHVPQASRRYKNSYNGFVYNIHTWLYDVSVFLFNILFTIFFREIKV
RGAYNVPEVGVPTILVCAPHANQFIDPALVMSQTRLLKTSAGKSRSRMPCFVTAESSFKK
RFISFFGHAMGGIPVPRIQDNLKPVDENLEIYAPDLKNHPEIIKGRSKNPQTTPVNFTKR
FSAKSLLGLPDYLSNAQIKEIPDDETIILSSPFRTSKSKVVELLTNGTNFKYAEKIDNTE
TFQSVFDHLHTKGCVGIFPEGGSHDRPSLLPIKAGVAIMALGAVAADPTMKVAVVPCGLH
YFHRNKFRSRAVLEYGEPIVVDGKYGEMYKDSPRETVSKLLKKITNSLFSVTENAPDYDT
LMVIQAARRLYQPVKVRLPLPAIVEINRRLLFGYSKFKDDPRIIHLKKLVYDYNRKLDSV
GLKDHQVMQLKTTKLEALRCFVTLIVRLIKFSVFAILSLPGSILFTPIFIICRVYSEKKA
KEGLKKSLVKIKGTDLLATWKLIVALILAPILYVTYSILLIILARKQHYCRIWVPSNNAF
IQFVYFYALLVFTTYSSLKTGEIGVDLFKSLRPLFVSIVYPGKKIEEIQTTRKNLSLELT
AVCNDLGPLVFPDYDKLATEIFSKRDGYDVSSDAESSISRMSVQSRSRSSSIHSIGSLAS
NALSRVNSRGSLTDIPIFSDAKQGQWKSEGETSEDEDEFDEKNPAIVQTARSSDLNKENS
RNTNISSKIASLVRQKREHEKKE
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>glycerol 3-phosphate/dihydroxyacetone phosphate dual substrate-specific sn-1 acyltransferase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001775</url>
<remark>Standard Name: GPT2</remark>
<remark>
Glycerol-3-phosphate acyltransferase located in both lipid particles and the ER; involved in the stepwise acylation of glycerol-3-phosphate and dihydroxyacetone, which are intermediate steps in lipid biosynthesis
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_012993.1</databaseId>
</databaseRef>
</target>

<target>
<id>YLR411W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MNMGGSSSTAAKKATCKISMLWNWYTIDTCFIARSWRNDTKGKFAGSCIGCFALVVVAQW
LTRFSRQFDVELLKRQKIKHLASYSPEEYVVKCGEEDAKSDIEELQGFYNEPSWKTTLIS
LQKSFIYSFYVWGPRRLNEPEDDLLKKVLSCCTLITPVDLYPTFLDHMIRVTIFVLQWGL
SYIIMLLFMYYNGYIIISCLIGAIVGRFIFCYEPLGSLGANGSAQGTVSYDKESDDRKCC
L
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>copper transporter</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004403</url>
<remark>Standard Name: CTR3</remark>
<remark>
High-affinity copper transporter of the plasma membrane, acts as a trimer; gene is disrupted by a Ty2 transposon insertion in many laboratory strains of S. cerevisiae
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_013515.1</databaseId>
</databaseRef>
</target>

<target>
<id>YML019W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MKWCSTYIIIWLAIIFHKFQKSTATASHNIDDILQLKDDTGVITVTADNYPLLSRGVPGY
FNILYITMRGTNSNGMSCQLCHDFEKTYHAVADVIRSQAPQSLNLFFTVDVNEVPQLVKD
LKLQNVPHLVVYPPAESNKQSQFEWKTSPFYQYSLVPENAENTLQFGDFLAKILNISITV
PQAFNVQEFVYYFVACMVVFIFIKKVILPKVTNKWKLFSMILSLGILLPSITGYKFVEMN
AIPFIARDAKNRIMYFSGGSGWQFGIEIFSVSLMYIVMSALSVLLIYVPKISCVSEKMRG
LLSSFLACVLFYFFSYFISCYLIKNPGYPIVF
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004481</url>
<remark>Standard Name: OST6</remark>
<remark>
Subunit of the oligosaccharyltransferase complex of the ER lumen, which catalyzes asparagine-linked glycosylation of newly synthesized proteins; similar to and partially functionally redundant with Ost3p
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_013693.1</databaseId>
</databaseRef>
</target>

<target>
<id>YML052W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MVKVWNIVLRLVVLLFLAGNTLLLILMIISGATDHYPVNRFYWVQGNTTGIPNAGDETRW
TFWGACLQDKDGSDTCTSNLAPAYPISPVDNFNTHINVPHQFISKRDAFYYLTRFSFCFF
WIALAFVGVSFILYVLTWCSKMLSEMVLILMSFGFVFNTAAVVLQTAASAMAKNAFHDDH
RSAQLGASMMGMAWASVFLCIVEFILLVFWSVRARLASTYSIDNSRYRTSSRWNPFHREK
EQATDPILTATGPEDMQQSASIVGPSSNANPVTATAATENQPKGINFFTIRKSHERPDDV
SV
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004516</url>
<remark>Standard Name: SUR7</remark>
<remark>
Putative integral membrane protein; component of eisosomes; associated with endocytosis, along with Pil1p and Lsp1p; sporulation and plasma membrane sphingolipid content are altered in mutants
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_013660.1</databaseId>
</databaseRef>
</target>

<target>
<id>YML055W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSSAKPINVYSIPELNQALDEALPSVFARLNYERSYALLDAKLYIGYSIAVVAGLSFFLD
KKFERDQIVTYQKLLVGAYFVLSLLFWYFSRFIEKGTVYVGKRRGTKEEIYVKTKFEKNE
PLYLVELVQKKKGENSKKELKAKLEVNKVFNESGYLQNDAYFKWFSEQHNVLDTKKNE
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>signal peptidase complex subunit</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004519</url>
<remark>Standard Name: SPC2</remark>
<remark>
Subunit of signal peptidase complex (Spc1p, Spc2p, Spc3p, Sec11p), which catalyzes cleavage of N-terminal signal sequences of proteins targeted to the secretory pathway; homologous to mammalian SPC25
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_013657.1</databaseId>
</databaseRef>
</target>

<target>
<id>YMR056C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MSHTETQTQQSHFGVDFLMGGVSAAIAKTGAAPIERVKLLMQNQEEMLKQGSLDTRYKGI
LDCFKRTATHEGIVSFWRGNTANVLRYFPTQALNFAFKDKIKSLLSYDRERDGYAKWFAG
NLFSGGAAGGLSLLFVYSLDYARTRLAADARGSKSTSQRQFNGLLDVYKKTLKTDGLLGL
YRGFVPSVLGIIVYRGLYFGLYDSFKPVLLTGALEGSFVASFLLGWVITMGASTASYPLD
TVRRRMMMTSGQTIKYDGALDCLRKIVQKEGAYSLFKGCGANIFRGVAAAGVISLYDQLQ
LIMFGKKFK
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>ADP/ATP carrier</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004660</url>
<remark>Standard Name: AAC1</remark>
<remark>
Mitochondrial inner membrane ADP/ATP translocator, exchanges cytosolic ADP for mitochondrially synthesized ATP; Aac1p is a minor isoform while Pet9p is the major ADP/ATP translocator
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_013772.1</databaseId>
</databaseRef>
</target>

<target>
<id>YMR101C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MKMPSIIQIQFVALKRLLVETKEQMCFAVKSIFQRVFAWVMSLSLFSWFYVNLQNILIKA
LRVGPVPEHVSFIMDGNRRYAKSRRLPVKKGHEAGGLTLLTLLYICKRLGVKCVSAYAFS
IENFNRPKEEVDTLMNLFTVKLDEFAKRAKDYKDPLYGSKIRIVGDQSLLSPEMRKKIKK
VEEITQDGDDFTLFICFPYTSRNDMLHTIRDSVEDHLENKSPRINIRKFTNKMYMGFHSN
KCELLIRTSGHRRLSDYMLWQVHENATIEFSDTLWPNFSFFAMYLMILKWSFFSTIQKYN
EKNHSLFEKIHESVPSIFKKKKTAMSLYNFPNPPISVSVTGDE
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>cis-prenyltransferase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004707</url>
<remark>Standard Name: SRT1</remark>
<remark>
Cis-prenyltransferase involved in synthesis of long-chain dolichols (19-22 isoprene units; as opposed to Rer2p which synthesizes shorter-chain dolichols); localizes to lipid bodies; transcription is induced during stationary phase
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_013819.1</databaseId>
</databaseRef>
</target>

<target>
<id>YMR123W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MANFFVRLWESVFEPGTSPQLIIATHVSFVALLLTLIWLIYATNGNIHFYALFCISLLLW
ITVIWFINELSHVKLKDNDELDKDANKKDDSAIKEDSEDKQESGKSTSTARRTQAQSRSR
KA
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>V-ATPase Assembly Factor</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004730</url>
<remark>Standard Name: PKR1</remark>
<remark>
V-ATPase assembly factor, functions with other V-ATPase assembly factors in the ER to efficiently assemble the V-ATPase membrane sector (V&lt;sub&gt;0&lt;/sub&gt;); overproduction confers resistance to Pichia farinosa killer toxin
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_013842.1</databaseId>
</databaseRef>
</target>

<target>
<id>YMR149W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MQFFKTLAALVSCISFVLAYVAQDVHVSFPSTAGKSRVMIGKVEPRIGIDETVPTTITVE
DPNEVIQVNFAIESTNKPFQNTLLIGLPNKNLEMAFEPEIKDNGKLSMYKYRIDLAKLDA
ALLQEASRSPEPIKATLILASSTAKPKENLFREILQLNLNFDVDHSDSSLVDKFGIKPEI
HHIFHAEPKRVAKPIAVIFVLIIFITILSLIVTWLNSCAAAFNNIPTGVTAVYFLGFIAT
IVGFEVIFARYYLGTSIFETLFSSLYLGAPGLLTSTKFLRSFGQTI
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>oligosaccharyl transferase glycoprotein complex, delta subunit</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004757</url>
<remark>Standard Name: SWP1</remark>
<remark>
Delta subunit of the oligosaccharyl transferase glycoprotein complex, which is required for N-linked glycosylation of proteins in the endoplasmic reticulum
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_013869.1</databaseId>
</databaseRef>
</target>

<target>
<id>YMR274C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MLQFSTFLVLLYISISYVLPLYATSQPEGSKRDNPRTIKSRMQKLTIMLISNLFLVPFLQ
SQLSSTTSHISFKDAFLGLGIIPGYYAALPNPWQFSQFVKDLTKCVAMLLTLYCGPVLDF
VLYHLLNPKSSILEDFYHEFLNIWSFRNFIFAPITEEIFYTSMLLTTYLNLIPHSQLSYQ
QLFWQPSLFFGLAHAHHAYEQLQEGSMTTVSILLTTCFQILYTTLFGGLTKFVFVRTGGN
LWCCIILHALCNIMGFPGPSRLNLHFTVVDKKAGRISKLVSIWNKCYFALLVLGLISLKD
TLQTLVGTPGYRITL
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>protease</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004887</url>
<remark>Standard Name: RCE1</remark>
<remark>
Type II CAAX prenyl protease involved in the proteolysis and maturation of Ras and the a-factor mating pheromone
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_014001.1</databaseId>
</databaseRef>
</target>

<target>
<id>YNL044W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MNQLGALAQVSRFTQNFSMENIKSEFQSLQSKLATLRTPQEFFNFKKISKPQNFGEVQSR
VAYNLKYFSSNYGLIIGCLSIYTLLTNLLLLFVIVLVVAGIVGINKLKGEELVTPFGSFK
TNQLYTGLVCVAVPIGFLASPISTLLWLIGASAVSVFGHASLMEKPIETVFDEETV
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004989</url>
<remark>Standard Name: YIP3</remark>
<remark>
Protein localized to COPII vesicles, proposed to be involved in ER to Golgi transport; interacts with members of the Rab GTPase family and Yip1p; also interacts with Rtn1p
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_014354.2</databaseId>
</databaseRef>
</target>

<target>
<id>YNL055C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSPPVYSDISRNINDLLNKDFYHATPAAFDVQTTTANGIKFSLKAKQPVKDGPLSTNVEA
KLNDKQTGLGLTQGWSNTNNLQTKLEFANLTPGLKNELITSLTPGVAKSAVLNTTFTQPF
FTARGAFDLCLKSPTFVGDLTMAHEGIVGGAEFGYDISAGSISRYAMALSYFAKDYSLGA
TLNNEQITTVDFFQNVNAFLQVGAKATMNCKLPNSNVNIEFATRYLPDASSQVKAKVSDS
GIVTLAYKQLLRPGVTLGVGSSFDALKLSEPVHKLGWSLSFDA
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>porin|voltage-dependent anion channel (VDAC)</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005000</url>
<remark>Standard Name: POR1</remark>
<remark>
Mitochondrial porin (voltage-dependent anion channel), outer membrane protein required for the maintenance of mitochondrial osmotic stability and mitochondrial membrane permeability
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_014343.1</databaseId>
</databaseRef>
</target>

<target>
<id>YNL275W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<status>Soluble</status>
<status>Purified</status>
<sequence>
MSNESTRVTVSRGCTASDECAQALERTNDELDRESSVSESRSDEESHEKLSRRRFPTLGI
GIWLDLKDRIPYYKSDWVDAFNYRVIPSIVDTYFNNLLPAIAFAQDMFDRTDNSYGVNEV
LLSSAMAGIVFGVLGGQPLCIVGVTGPISIFNYTVYEIIKPLNTSYFGFMFWICMWSMIF
HLVLAFTNAVCLLQYVTTFPCDIFGLFINVVYIQKGIQILTRQFSAKSGEKSVQDGFASV
VVALVMTAFGLFFKLFHYYPLFSHRIRTFISDYSTALSVLFWSSFTHFGGYLHDVKFKKL
PITKAFFPTSKVNRPQNTWLAYEPIPVKDVFIALPFGIFLTILFYFDHNVSSLMAQRHQY
KLKKPSSFHYDFALLGLTTCISGVLGIPAPNGLIPQAPLHTETLLVRDSNQKVISCVEQR
FTNTFQGLMILGTMTRPLLVCLGEIPQAVLSGLFFIMGINGLMTNSIIQRLVFLFSDPNR
RDNTSPLMKVSKKSMLIFLSFSLTGFAGEFAITNTIAAIGFPLVLLLSVLVSFSFAYIFP
TEELKILDTNVAQKFTIKNLLLENIRDAKFCDKHED
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>boron transporter</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005219</url>
<remark>Standard Name: BOR1</remark>
<remark>
Boron efflux transporter of the plasma membrane; binds HCO3-, I-, Br-, NO3- and Cl- ; has similarity to the characterized boron efflux transporter A. thaliana BOR1
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_014124.1</databaseId>
</databaseRef>
</target>

<target>
<id>YOR212W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MAAHQMDSITYSNNVTQQYIQPQSLQDISAVEDEIQNKIEAARQESKQLHAQINKAKHKI
QDASLFQMANKVTSLTKNKINLKPNIVLKGHNNKISDFRWSRDSKRILSASQDGFMLIWD
SASGLKQNAIPLDSQWVLSCAISPSSTLVASAGLNNNCTIYRVSKENRVAQNVASIFKGH
TCYISDIEFTDNAHILTASGDMTCALWDIPKAKRVREYSDHLGDVLALAIPEEPNSENSS
NTFASCGSDGYTYIWDSRSPSAVQSFYVNDSDINALRFFKDGMSIVAGSDNGAINMYDLR
SDCSIATFSLFRGYEERTPTPTYMAANMEYNTAQSPQTLKSTSSSYLDNQGVVSLDFSAS
GRLMYSCYTDIGCVVWDVLKGEIVGKLEGHGGRVTGVRSSPDGLAVCTGSWDSTMKIWSP
GYQ
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>G protein beta subunit</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005738</url>
<remark>Standard Name: STE4</remark>
<remark>
G protein beta subunit, forms a dimer with Ste18p to activate the mating signaling pathway, forms a heterotrimer with Gpa1p and Ste18p to dampen signaling; may recruit Rho1p to the polarized growth site during mating; contains WD40 repeats
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_014855.1</databaseId>
</databaseRef>
</target>

<target>
<id>YOR245C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSGTFNDIRRRKKEEGSPTAGITERHENKSLSSIDKREQTLKPQLESCCPLATPFERRLQ
TLAVAWHTSSFVLFSIFTLFAISTPALWVLAIPYMIYFFFDRSPATGEVVNRYSLRFRSL
PIWKWYCDYFPISLIKTVNLKPTFTLSKNKRVNEKNYKIRLWPTKYSINLKSNSTIDYRN
QECTGPTYLFGYHPHGIGALGAFGAFATEGCNYSKIFPGIPISLMTLVTQFHIPLYRDYL
LALGISSVSRKNALRTLSKNQSICIVVGGARESLLSSTNGTQLILNKRKGFIKLAIQTGN
INLVPVFAFGEVDCYNVLSTKKDSVLGKMQLWFKENFGFTIPIFYARGLFNYDFGLLPFR
APINVVVGRPIYVEKKITNPPDDVVNHFHDLYIAELKRLYYENREKYGVPDAELKIVG
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>Acyl-CoA : diacylglycerol acyltransferase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005771</url>
<remark>Standard Name: DGA1</remark>
<remark>
Diacylglycerol acyltransferase, catalyzes the terminal step of triacylglycerol (TAG) formation, acylates diacylglycerol using acyl-CoA as an acyl donor, localized to lipid particles
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_014888.1</databaseId>
</databaseRef>
</target>

<target>
<id>YOR328W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MLQAPSSSNSGLNQGNAAPDGPPNETQPYEGLDAAAQEEIKELARTLTSQSSLLSQEKRI
TGTGDPNTLTAASSSSLSRSIFASDIKGVNPILLDVNDPDYDETLDPRSENFSSVRWVRN
MAQICENDSDFYKPFSLGCAWKDLSASGDSADITYQGTFGNMPIKYLKMSWRCISRRLFH
RTHGKSEDNDSGFQILKPMDGCINPGELLVVLGRPGAGCTTLLKSISVNTHGFKISPDTI
ITYNGFSNKEIKNHYRGEVVYNAESDIHIPHLTVFQTLYTVARLKTPRNRIKGVDRDTFA
KHMTEVAMATYGLSHTADTKVGNDFVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLD
SATALEFIKALKTQATITKSAATVAIYQCSKDAYDLFDKVCVLYDGYQIFFGPSKQAKKY
FQRMGYVCPERQTTADYLTSITSPSERIKDKDMVKHGIMIPQTAYEMNQYWIQSEEYKQL
QVQVNKHLDTDSSQQREQIKNAHIAKQSKRARPSSPYTVSFFLQVKYILIRDIWRIKNDP
SIQLFTVLSHAAMALILGSMFYEVMLSTTTTTFYYRGAAIFFAILFNAFSSLLEIFSLYE
TRPITEKHKTYSLYRPSADAFASTFSDVPTKLATAVTFNIPYYFLINLKRDAGAFFFYFL
INIITVFAMSHLFRCIGSVSKTLPQAMVPASVLLLAFAMYTGFAIPRVQMLGWSKWISYI
NPLSYLFESLMINEFHGRNFPCAQYIPSGPNYVNATGDEVTCSALGSIPGNNYVSGDDFI
QTNYGYRHKNKWRSVGIGLAYIIFFLFLYLFFCEYNEGAKQNGEMLVFPHSVVKKMKKKG
IVSEKKKKNQPTLSTSDAEKDVEMNNNSSATDSRFLRDSDAAIMGNDKTVAKEHYSSPSS
SASQSNSFSKSDDIELSKSQAIFHWKNLCYDIPIKNGKRRILDNVDGWVKPGTLTALIGA
SGAGKTTLLDCLAERTTMGLITGDVFVDGRPRDQSFPRSIGYCQQQDLHLKTATVRESLR
FSAYLRQADDVSIEEKDKYVEEVIEVLEMKLYADAIVGVPGEGLNVEQRKRLTIGVELAA
KPKLLVFLDEPTSGLDSQTAWSTCQLMKKLASRGQAILCTIHQPSALLMQEFDRLLFLQE
GGQTVYFGELGKGCKTMINYFEAHGAHKCPPDANPAEWMLEIVGAAPGTHASQDYFAIWR
DSEEYREMQKELDWMERELPKRTEGSSNEEQKEFATSTLYQIKLVSYRLFHQYWRTPFYL
WSKFFSTIVSELFIGFTFFKANTSLQGLQNQMLAIFMFTVVFNPILQQYLPLFVQQRELY
EARERPSRTFSWKAFIVSQILVEIPWNLLAGTIAFFVYYYPVGFYRNASYANQLHERGAL
FWLFACAFYVYISSMGVLVISCIEIAENAANLASLFFIMSLSFCGVLATPNILPRFWIFM
YRVSPLTYLIDALLSVGLANASVVCSSNELLKIVPPSGMTCSEYMEPYMQSTGTGYLLDG
SSETECHFCQFSSTNDYLATVSSSYSRRWMNYGIFSAYIVFDYCAAIFLYWLVRVPKKSK
KLKK
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005855</url>
<remark>Standard Name: PDR10</remark>
<remark>
ABC (ATP-binding cassette) membrane pump involved in the pleiotropic drug resistance network, regulated by Pdr1p and Pdr3p, similar to Pdr5p
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_014973.1</databaseId>
</databaseRef>
</target>

<target>
<id>YPL036W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSSTEAKQYKEKPSKEYLHASDGDDPANNSAASSSSSSSTSTSASSSAAAVPRKAAAASA
ADDSDSDEDIDQLIDELQSNYGEGDESGEEEVRTDGVHAGQRVVPEKDLSTDPAYGLTSD
EVARRRKKYGLNQMAEENESLIVKFLMFFVGPIQFVMEAAAILAAGLSDWVDVGVICALL
LLNASVGFIQEFQAGSIVDELKKTLANTATVIRDGQLIEIPANEVVPGEILQLESGTIAP
ADGRIVTEDCFLQIDQSAITGESLAAEKHYGDEVFSSSTVKTGEAFMVVTATGDNTFVGR
AAALVGQASGVEGHFTEVLNGIGIILLVLVIATLLLVWTACFYRTVGIVSILRYTLGITI
IGVPVGLPAVVTTTMAVGAAYLAKKQAIVQKLSAIESLAGVEILCSDKTGTLTKNKLSLH
EPYTVEGVSPDDLMLTACLAASRKKKGLDAIDKAFLKSLIEYPKAKDALTKYKVLEFHPF
DPVSKKVTAVVESPEGERIVCVKGAPLFVLKTVEEDHPIPEDVHENYENKVAELASRGFR
ALGVARKRGEGHWEILGVMPCMDPPRDDTAQTINEARNLGLRIKMLTGDAVGIAKETCRQ
LGLGTNIYNAERLGLGGGGDMPGSELADFVENADGFAEVFPQHKYRVVEILQNRGYLVAM
TGDGVNDAPSLKKADTGIAVEGATDAARSAADIVFLAPGLSAIIDALKTSRQIFHRMYSY
VVYRIALSLHLEIFLGLWIAILNNSLDINLIVFIAIFADVATLTIAYDNAPYAPEPVKWN
LPRLWGMSIILGIVLAIGSWITLTTMFLPNGGIIQNFGAMNGVMFLQISLTENWLIFVTR
AAGPFWSSIPSWQLAGAVFAVDIIATMFTLFGWWSENWTDIVSVVRVWIWSIGIFCVLGG
FYYIMSTSQAFDRLMNGKSLKEKKSTRSVEDFMAAMQRVSTQHEKSS
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>plasma membrane ATPase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005957</url>
<remark>Standard Name: PMA2</remark>
<remark>
Plasma membrane H+-ATPase, isoform of Pma1p, involved in pumping protons out of the cell; regulator of cytoplasmic pH and plasma membrane potential
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_015289.1</databaseId>
</databaseRef>
</target>

<target>
<id>YPL087W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MLFSWPYPEAPIEGYWGKPTSLIDWCEENYVVSPYIAEWSNTITNSIFLMTAFYSTYSAW
RNKLETRYILIGMGFSLVGIGSWLFHMTLQYRYQLLDELPMLYATIIPSWSIFAETQEIL
IKDEKKRKESSFRIQMVISFIMCGIVTILTWIYVVVQKPAIFQVLYGILTLLVVVLSGWL
TYYHVHDSFAKKNLFITMVMGMIPFVIGFICWQLDIHLCSFWIYIRRTYLALPLGVLLEL
HAWWHLLTGTGVYIFVVYLQYLRILTHGNPNDFLFIWRWGFFPELVRKGLPIGTSYSLEY
LGPIVNTQVDDETKKNN
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>alkaline dihydroceramidase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006008</url>
<remark>Standard Name: YDC1</remark>
<remark>
Alkaline dihydroceramidase, involved in sphingolipid metabolism; preferentially hydrolyzes dihydroceramide to a free fatty acid and dihydrosphingosine; has a minor reverse activity
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_015238.1</databaseId>
</databaseRef>
</target>

<target>
<id>YPL094C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSAVGPGSNAGASVNGGSATAIATLLRNHKELKQRQGLFQAKQTDFFRYKRFVRALHSEE
YANKSARQPEIYPTIPSNKIEDQLKSREIFIQLIKAQMVIPVKKLHSQECKEHGLKPSKD
FPHLIVSNKAQLEADEYFVWNYNPRTYMDYLIVIGVVSIILALVCYPLWPRSMRRGSYYV
SLGAFGILAGFFAVAILRLILYVLSLIVYKDVGGFWIFPNLFEDCGVLESFKPLYGFGEK
DTYSYKKKLKRMKKKQAKRESNKKKAINEKAEQN
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>ER protein translocation apparatus membrane component</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006015</url>
<remark>Standard Name: SEC62</remark>
<remark>
Essential subunit of Sec63 complex (Sec63p, Sec62p, Sec66p and Sec72p); with Sec61 complex, Kar2p/BiP and Lhs1p forms a channel competent for SRP-dependent and post-translational SRP-independent protein targeting and import into the ER
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_015231.2</databaseId>
</databaseRef>
</target>

<target>
<id>YPR028W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MSEYASSIHSQMKQFDTKYSGNRILQQLENKTNLPKSYLVAGLGFAYLLLIFINVGGVGE
ILSNFAGFVLPAYLSLVALKTPTSTDDTQLLTYWIVFSFLSVIEFWSKAILYLIPFYWFL
KTVFLIYIALPQTGGARMIYQKIVAPLTDRYILRDVSKTEKDEIRASVNEASKATGASVH
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006232</url>
<remark>Standard Name: YOP1</remark>
<remark>
Membrane protein that interacts with Yip1p to mediate membrane traffic; overexpression results in cell death and accumulation of internal cell membranes; regulates vesicular traffic in stressed cells
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_015353.1</databaseId>
</databaseRef>
</target>

<target>
<id>YPR113W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSSNSTPEKVTAEHVLWYIPNKIGYVRVITAALSFFVMKNHPTAFTWLYSTSCLLDALDG
TMARKYNQVSSLGAVLDMVTDRSSTAGLMCFLCVQYPQWCVFFQLMLGLDITSHYMHMYA
SLSAGKTSHKSVGEGESRLLHLYYTRRDVLFTICAFNELFYAGLYLQLFSNSATFGKWTT
IISFPGYVFKQTANVVQLKRAALILADNDAKNANEKNKTY
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>phosphatidylinositol synthase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006317</url>
<remark>Standard Name: PIS1</remark>
<remark>
Phosphatidylinositol synthase, required for biosynthesis of phosphatidylinositol, which is a precursor for polyphosphoinositides, sphingolipids, and glycolipid anchors for some of the plasma membrane proteins
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_015438.1</databaseId>
</databaseRef>
</target>

<target>
<id>YPR149W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<sequence>
MLALADNILRIINFLFLVISIGLISSLLNTQHRHSSRVNYCMFACAYGIFTDSLYGVFAN
FIEPLAWPLVLFTLDFLNFVFTFTAGTVLAVGIRAHSCNNSSYVDSNKITQGSGTRCRQA
QAAVAFLYFSCAIFLAKTLMSVFNMISNGAFGSGSFSKRRRTGQVGVPTISQV
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006353</url>
<remark>Standard Name: NCE102</remark>
<remark>
Protein of unknown function; contains transmembrane domains; involved in secretion of proteins that lack classical secretory signal sequences; component of the detergent-insoluble glycolipid-enriched complexes (DIGs)
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_015475.1</databaseId>
</databaseRef>
</target>

<target>
<id>YPR192W</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<sequence>
MSSNDSNDTDKQHTRLDPTGVDDAYIPPEQPETKHHRFKISRDTLRDHFIAAVGEFCGTF
MFLWCAYVICNVANHDVALVAAPDGSHPGQLIMIAIGFGFSVMFSIWCFAGVSGGALNPA
MSLSLCLARAVSPTRCVVMWVSQIVAGMAAGGAASAMTPGEVLFANSLGLGCSRTRGLFL
EMFGTAILCLTVLMTAVEKRETNFMAALPIGISLFIAHVALTAYTGTGVNPARSLGAAVA
ARYFPHYHWIYWIGTLLGSILAWSVWQLLQILDYTTYVTAEKAASTKEKAQKKGETSSSS
AVAEV
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>aquaporin</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006396</url>
<remark>Standard Name: AQY1</remark>
<remark>
Spore-specific water channel that mediates the transport of water across cell membranes, developmentally controlled; may play a role in spore maturation, probably by allowing water outflow, may be involved in freeze tolerance
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_015518.1</databaseId>
</databaseRef>
</target>

<target>
<id>YOL097C</id>
<lab>Center for High-Throughput Structural Biology</lab>
<date>2007-04-03</date>
<status>Selected</status>
<status>Cloned</status>
<status>Expressed</status>
<status>Soluble</status>
<status>Purified</status>
<status>Crystallized</status>
<status>Diffraction-quality Crystals</status>
<status>Diffraction</status>
<status>Crystal Structure</status>
<sequence>
MSNDETVEKVTQQVSELKSTDVKEQVVTPWDVEGGVDEQGRAQNIDYDKLIKQFGTKPVN
EETLKRFKQVTGREPHHFLRKGLFFSERDFTKILDLYEQGKPFFLYTGRGPSSDSMHLGH
MIPFVFTKWLQEVFDVPLVIELTDDEKFLFKHKLTINDVKNFARENAKDIIAVGFDPKNT
FIFSDLQYMGGAFYETVVRVSRQITGSTAKAVFGFNDSDCIGKFHFASIQIATAFPSSFP
NVLGLPDKTPCLIPCAIDQDPYFRVCRDVADKLKYSKPALLHSRFFPALQGSTTKMSASD
DTTAIFMTDTPKQIQKKINKYAFSGGQVSADLHRELGGNPDVDVAYQYLSFFKDDDVFLK
ECYDKYKSGELLSGEMKKLCIETLQEFVKAFQERRAQVDEETLDKFMVPHKLVWGEKERL
VAPKPKTKQEKK
</sequence>
<sourceOrganism>Saccharomyces cerevisiae</sourceOrganism>
<name>tryptophanyl-tRNA synthetase</name>
<url>http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005457</url>
<remark>Standard Name: WRS1</remark>
<remark>
Cytoplasmic tryptophanyl-tRNA synthetase, aminoacylates tryptophanyl-tRNA
</remark>
<databaseRef>
    <databaseName>NCBI</databaseName>
    <databaseId>NP_014544.1</databaseId>
</databaseRef>
</target>

</targets>
