SST2_YEAST
ID SST2_YEAST Reviewed; 698 AA.
AC P11972; D6VZ86; Q06207;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Protein SST2;
GN Name=SST2; OrderedLocusNames=YLR452C; ORFNames=L9324.9;
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 [GENOMIC DNA].
RX PubMed=2830483; DOI=10.1128/mcb.7.12.4169-4177.1987;
RA Dietzel C., Kurjan J.;
RT "Pheromonal regulation and sequence of the Saccharomyces cerevisiae SST2
RT gene: a model for desensitization to pheromone.";
RL Mol. Cell. Biol. 7:4169-4177(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 PHOSPHORYLATION AT SER-539.
RX PubMed=10593933; DOI=10.1074/jbc.274.51.36387;
RA Garrison T.R., Zhang Y., Pausch M., Apanovitch D., Aebersold R.,
RA Dohlman H.G.;
RT "Feedback phosphorylation of an RGS protein by MAP kinase in yeast.";
RL J. Biol. Chem. 274:36387-36391(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 AND SER-587, AND
RP IDENTIFICATION BY 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-408 AND SER-587, AND
RP IDENTIFICATION BY 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 IDENTIFICATION BY 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: Desensitization to alpha-factor pheromone. Is involved in
CC regulating the signaling pathway for responding to mating pheromone.
CC -!- INTERACTION:
CC P11972; P08539: GPA1; NbExp=3; IntAct=EBI-18232, EBI-7376;
CC P11972; P0CI39: STE2; Xeno; NbExp=4; IntAct=EBI-18232, EBI-18360;
CC -!- INDUCTION: By exposure to pheromone.
CC -!- DOMAIN: The fungal-differentiation regulator (Fungal-DR) domain is only
CC found in fungal regulator of G-protein signaling (RGS) proteins that
CC regulate differentiation pathways. It is required for function (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by FUS3 and KSS1. {ECO:0000269|PubMed:10593933}.
CC -!- MISCELLANEOUS: Present with 5980 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M18105; AAA35104.1; -; Genomic_DNA.
DR EMBL; U22382; AAB67534.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09752.1; -; Genomic_DNA.
DR PIR; S55974; S55974.
DR RefSeq; NP_013557.1; NM_001182340.1.
DR AlphaFoldDB; P11972; -.
DR BioGRID; 31710; 433.
DR DIP; DIP-2354N; -.
DR IntAct; P11972; 11.
DR MINT; P11972; -.
DR STRING; 4932.YLR452C; -.
DR iPTMnet; P11972; -.
DR MaxQB; P11972; -.
DR PaxDb; P11972; -.
DR PRIDE; P11972; -.
DR EnsemblFungi; YLR452C_mRNA; YLR452C; YLR452C.
DR GeneID; 851173; -.
DR KEGG; sce:YLR452C; -.
DR SGD; S000004444; SST2.
DR VEuPathDB; FungiDB:YLR452C; -.
DR eggNOG; KOG3589; Eukaryota.
DR HOGENOM; CLU_024143_0_0_1; -.
DR InParanoid; P11972; -.
DR OMA; WLMDCTD; -.
DR BioCyc; YEAST:G3O-32505-MON; -.
DR PRO; PR:P11972; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P11972; protein.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IMP:SGD.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00049; DEP; 2.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Pheromone response; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..698
FT /note="Protein SST2"
FT /id="PRO_0000204173"
FT DOMAIN 273..358
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 420..689
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 10..203
FT /note="Fungal-DR"
FT REGION 545..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 539
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:10593933"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT CONFLICT 616
FT /note="H -> D (in Ref. 1; AAA35104)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="E -> D (in Ref. 1; AAA35104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 698 AA; 79716 MW; 48CF5BB6E456C11C CRC64;
MVDKNRTLHE LSSKNFSRTP NGLIFTNDLK TVYSIFLICL DLKEKKHSSD TKSFLLTAFT
KHFHFTFTYQ EAIKAMGQLE LKVDMNTTCI NVSYNIKPSL ARHLLTLFMS SKLLHTPQDR
TRGEPKEKVL FQPTPKGVAV LQKYVRDIGL KTMPDILLSS FNSMKLFTFE RSSVTDSIIH
SDYLIHILFI KMMGAKPNVW SPTNADDPLP CLSSLLEYTN NDDTFTFEKS KPEQGWQAQI
GNIDINDLER VSPLAHRFFT NPDSESHTQY YVSNAGIRLF ENKTFGTSKK IVIKYTFTTK
AIWQWIMDCT DIMHVKEAVS LAALFLKTGL IVPVLLQPSR TDKKKFQISR SSFFTLSKRG
WDLVSWTGCK SNNIRAPNGS TIDLDFTLRG HMTVRDEKKT LDDSEGFSQD MLISSSNLNK
LDYVLTDPGM RYLFRRHLEK ELCVENLDVF IEIKRFLKKM TILKKLIDSK HCDKKSNTST
SKNNIVKTID SALMKQANEC LEMAYHIYSS YIMIGSPYQL NIHHNLRQNI SDIMLHPHSP
LSEHFPTNLY DPSPASAESA ASSISSTEAD TLGEPPEVSL KPSKNLSNEN CSFKKQGFKH
QLKEYKPAPL TLAETHSPNA SVENSHTIVR YGMDNTQNDT KSVESFPATL KVLRKLYPLF
EIVSNEMYRL MNNDSFQKFT QSDVYKDASA LIEIQEKC
