OPY2_YEAST
ID OPY2_YEAST Reviewed; 360 AA.
AC Q06810; D6W479; Q6B149;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein OPY2;
DE AltName: Full=Overproduction-induced pheromone-resistant protein 2;
GN Name=OPY2; OrderedLocusNames=YPR075C;
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 [MRNA].
RX PubMed=9383053; DOI=10.1093/genetics/147.3.1063;
RA Edwards M.C., Liegeois N., Horecka J., DePinho R.A., Sprague G.F. Jr.,
RA Tyers M., Elledge S.J.;
RT "Human CPR (cell cycle progression restoration) genes impart a Far-
RT phenotype on yeast cells.";
RL Genetics 147:1063-1076(1997).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STE50.
RX PubMed=16543225; DOI=10.1101/gad.1375706;
RA Wu C., Jansen G., Zhang J., Thomas D.Y., Whiteway M.;
RT "Adaptor protein Ste50p links the Ste11p MEKK to the HOG pathway through
RT plasma membrane association.";
RL Genes Dev. 20:734-746(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, 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 -!- FUNCTION: Component of the high-osmolarity glycerol (HOG) pathway
CC involved in mating response and osmotolerance. May act as a membrane
CC anchor for the STE50/STE11 complex. {ECO:0000269|PubMed:16543225}.
CC -!- INTERACTION:
CC Q06810; P32334: MSB2; NbExp=3; IntAct=EBI-2068557, EBI-11328;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16543225};
CC Single-pass membrane protein {ECO:0000269|PubMed:16543225}. Vacuole
CC membrane {ECO:0000269|PubMed:16543225}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16543225}.
CC -!- MISCELLANEOUS: Present with 1160 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; AF016263; AAB81506.1; -; mRNA.
DR EMBL; U51033; AAB68126.1; -; Genomic_DNA.
DR EMBL; AY693231; AAT93250.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11495.1; -; Genomic_DNA.
DR PIR; S69063; S69063.
DR RefSeq; NP_015400.1; NM_001184172.1.
DR AlphaFoldDB; Q06810; -.
DR BioGRID; 36248; 168.
DR ComplexPortal; CPX-1302; OPY2-MSB2 osmosensory complex.
DR IntAct; Q06810; 4.
DR MINT; Q06810; -.
DR STRING; 4932.YPR075C; -.
DR iPTMnet; Q06810; -.
DR MaxQB; Q06810; -.
DR PaxDb; Q06810; -.
DR PRIDE; Q06810; -.
DR EnsemblFungi; YPR075C_mRNA; YPR075C; YPR075C.
DR GeneID; 856191; -.
DR KEGG; sce:YPR075C; -.
DR SGD; S000006279; OPY2.
DR VEuPathDB; FungiDB:YPR075C; -.
DR eggNOG; ENOG502RY3X; Eukaryota.
DR HOGENOM; CLU_062466_0_0_1; -.
DR InParanoid; Q06810; -.
DR OMA; SCPKYYC; -.
DR BioCyc; YEAST:G3O-34221-MON; -.
DR PRO; PR:Q06810; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06810; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0000751; P:mitotic cell cycle G1 arrest in response to pheromone; IMP:SGD.
DR GO; GO:0007231; P:osmosensory signaling pathway; IGI:SGD.
DR GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IDA:ComplexPortal.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:SGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IGI:SGD.
DR DisProt; DP01516; -.
DR InterPro; IPR018571; Membrane_anchor_Opy2_N.
DR Pfam; PF09463; Opy2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..360
FT /note="Protein OPY2"
FT /id="PRO_0000268694"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..345
FT /note="STE50-binding"
FT REGION 282..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 234
FT /note="I -> T (in Ref. 4; AAT93250)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 38901 MW; 6D444AFA25042FFB CRC64;
MSSSSKASAS SSLSSTATSS TSATRGSDGC VVCDSTASCP VCASGEYCVM TSLTCDKCPS
TYCAKQSDSQ LSSLSSSSSS SSSSNSNEKT SLIVGFTVGI VGGAMLIALV ALYFINKRYW
KPKRQKNKAL KLEEASQSYG NEEEYFDDED DDDEDDEDDG GMRKDESHTL FNTSLVPPTL
NVPGNRSSAS TTRTRASNIL PIAYIPGVTS GLSTDKLQSK LRSSSKRQNA AGDIRSHITL
GSSILDGLDD EDDEHNQVLN KDADDNLITA IRAKPKLVQI AEEESDKEIQ DLDVIEEQTE
ADDLSHMAKS EASHGNNDED DDEEGSFILD LEIPESIRES TQGSRTESPF EDKFEIHDER
