YP117_YEAST
ID YP117_YEAST Reviewed; 2489 AA.
AC Q06116; D6W4B6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Uncharacterized protein YPR117W;
GN OrderedLocusNames=YPR117W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2254, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; U32445; AAB68087.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11532.1; -; Genomic_DNA.
DR PIR; S59782; S59782.
DR RefSeq; NP_015442.1; NM_001184214.1.
DR AlphaFoldDB; Q06116; -.
DR SMR; Q06116; -.
DR BioGRID; 36284; 166.
DR IntAct; Q06116; 1.
DR MINT; Q06116; -.
DR STRING; 4932.YPR117W; -.
DR iPTMnet; Q06116; -.
DR MaxQB; Q06116; -.
DR PaxDb; Q06116; -.
DR PRIDE; Q06116; -.
DR EnsemblFungi; YPR117W_mRNA; YPR117W; YPR117W.
DR GeneID; 856233; -.
DR KEGG; sce:YPR117W; -.
DR SGD; S000006321; YPR117W.
DR VEuPathDB; FungiDB:YPR117W; -.
DR eggNOG; KOG1910; Eukaryota.
DR GeneTree; ENSGT00600000084481; -.
DR HOGENOM; CLU_228568_0_0_1; -.
DR InParanoid; Q06116; -.
DR OMA; EYHFRFY; -.
DR BioCyc; YEAST:G3O-34256-MON; -.
DR PRO; PR:Q06116; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06116; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR045167; FMP27.
DR InterPro; IPR019443; FMP27_C.
DR InterPro; IPR019409; FMP27_DUF2405.
DR InterPro; IPR019441; FMP27_GFWDK_dom.
DR InterPro; IPR019415; FMP27_SW_dom.
DR InterPro; IPR019449; FMP27_WPPW_dom.
DR PANTHER; PTHR15678; PTHR15678; 1.
DR Pfam; PF10351; Apt1; 1.
DR Pfam; PF10293; DUF2405; 1.
DR Pfam; PF10347; Fmp27_GFWDK; 1.
DR Pfam; PF10305; Fmp27_SW; 1.
DR Pfam; PF10359; Fmp27_WPPW; 1.
DR SMART; SM01214; Fmp27_GFWDK; 1.
DR SMART; SM01215; Fmp27_SW; 1.
DR SMART; SM01216; Fmp27_WPPW; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..2489
FT /note="Uncharacterized protein YPR117W"
FT /id="PRO_0000257827"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1685..1704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2451..2489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1610..1676
FT /evidence="ECO:0000255"
FT COMPBIAS 2451..2470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 2278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 981
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1978
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2489 AA; 285904 MW; 6B5280F3E9EEEE31 CRC64;
MSMLPWSQIR DVSKLLLGFM LFIISIQKIA SILMSWILML RHSTIRKISF GYFFGTSIRR
AFILTDFAQI YIGKITLRIG WKPGIVFHNV DLKLFGKDSH ITAHSTKDSR TYFNPRDQTF
TFVINRRVLS ILKLVFSFST FFHTLALTVP NGKQYKLNIG SITISHPHDD TIKLEAFLHD
FTHPETKDTL NHTGFFMVCK IGKEDDTGSN CTKVILKNWK SSLKISDVCW HLPEKKGKNL
HSEPVEPFSA GDDAEMLTSY RKMLKPFHYP LKTLNILDLK VENVKLIYKK KFTIRISSAQ
LYLESISILN NVSALELLPL NKPTWGDFEL SLSANAVVVD IDGNTAVRIP FGNVILTSDI
LLFLLDNVPL RRTKVSSILN IINPSVFLTI HQVLEVLHLV DKFDSPETSS CTNTNDRSLN
ILDLDIDRLP SFNFELLMSN FISRLHISDE ENVTFKVFST HALFSRNNLS MTPKKGQVMQ
IRPDWPFAKT ALVSDQLSNY IKIVGTSLSY LRIPTEQDAN PVSIPVCGFE RLDTFLDEFS
NSKLIVQSTL RHSYVSLENI EVLHTLSRAF DKIYLLISSR TKRNAAHKAN GGKLGDLNEA
KKTFNWSLKL RMKDISCSLL VAGFLPKNLD PVEAENFNLS DVTRGAKVVF TESILLADSQ
EKNFTIIDAS VYRFMDGTTY KPSPEVIIQF TNLLLSFNDS DEIHFSLPKI KFKMDVNIIW
LWFYIRSIWI KFRPNSKLSR NSVSSVKSVN VLDRLRVDIG KMIIELTLPH NTEVLLIFER
IGLSSSTKNL TIASLSAYVV SVYVKHIKVY VSLLNINDFE LDTEELICKK SAVINTSLIH
FHAEYHFRFY MITDNIVTLY KSFKQIKLAF SNLNEFKRLY PQQQFPKKVP NLHICCQDFL
IDIEEDPFEQ ELGLILKVGV LEQRERLKKL EEFKEKLSTY EDMNVRLRSL YDTSRGQSFF
PEFYANDQEY EQKAYLRLLE NFSTSWIARY RKAKLSFYGM PYRVISREEL GTKYHLFTRQ
KTSTVANLVV KDLDFKLGSP SFPLDNYMDF VYQYGKKVPK STEYTLLIIL GLKIKSALWE
LRLRDYPIPA ISFPDTFTTG DVVFAEKMPA PCALHTVYVP FVSSAQRSPY NDANTIYGLH
IIRTINSVKT YFNIRSMVTS SSSARITWGK SLQPGYESLM LWFDFLTKPL IDPSKKLGFW
DKFRYLVHGK WIYEFSEESE IHLNIKGSHD PYKITDDGAG LAFCWSGGTT IYVHNSTDPK
EFLKIESQRF QLAVPDFAKV SKFDKVFMKL DGRVIWTLGL LFEQGDISKA GDEERFLPNR
PHYEIQLMNP DGVADLDHHD TYKGFRTSFI HMSFGVYSSE HGSINSLYLA PYALTHFFKW
WNLFHTYTSG PIRQGRLFTD VLQNKTKFGR SLFTIAYQLH LKRLMVTHIY RHITTQYDLE
KDRKITFTGL KGRFDSLKID LHQKRVKLTH TNQKLNKSKP VWKFKMSRGE IDCAEADIRI
LSTLFDQEAV KEILTSGLDG ILEDEPSRPI TPQDVEYLRE SDWYDYEDYI DLNQVPLGSS
LPLKLEAIPL LYSPRISYFR KINDDGYVLA YPFGTEESHN CLIGKNHPEL TQEKLATERK
REIEEQLKLL HITLSELQSN KGGGSVSGNS ERYARELKAE VAELNHRLHT VNTILSDLKI
SETIPGGNTD GDSSSSLSDT DVNLENAPPI QNRISLLRTN TVESFVSMRK ASTMQVESTY
DNRFMVHNIE LKIDNKIRHH LLEYASSAFE RKSMRFAVTY KSVTILKELL GNVLTGVRTS
VEDYGSILED DLASNSEFIE HFEKLIREVP SDDFDYVDNY LFRLISPQVQ IKSDVERNAA
VILAARDIEM GIIDIVQVYG KSGKRIPVDV DTIVETRYSA VSKDIQLFTL FKKDLEGPEG
RFFHKNGYGS DKESDIWPPW IPLEMCFDGS LLDKHVFLKR RSMFLTYVAP NPLFFSANDT
SAFSYDSRFR IAFPGLVLTS DCQQYCAVYA IAEDLLSFGS SLDEKVEKLS RILFTDEVRN
NLENLDVSVV TALQERIKEL YYTRAYLKLH EPRLFMKSGQ ELTFDIQTST LKLTLLMTAI
KKTYDRMGSG NRVIQKRLRW QVGTDELIWE LYDESKTPFV TIGLGPSTFI RSETSDGTNS
NKVSISSLQC FNQQENPVYT ELLAPFYENS SYNKNAPMVE IFWILGPSVG GISDLQDLIV
SLQPLIFKMD HKTSEKLMNY LFPKIEQTSI EPNSPELVPR SSTSSFFSSS PVLRHSLSNG
SLSVYDAKDV DSWDLRSIQS KEGIKKHKGD HRKLSASLFV QPDYNINEMV KRSGTFFNVK
SIIIRKTLMS VCYKGSHSLL TDVNNLIVRV PVLKYHNKLW SREEFFTALK RDVVRIVLQH
LGNIIGNKFL PHKKENKKKT SMEIHRLLSP DSQNRDNSHI LEVEGHNSFY SSTHSSDIRS
INSDETYNEN DGNGVKPFYP VTSEFSKNK
