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   27-MAR-2024, entry version 199.
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; 444.
DR   DIP; DIP-2354N; -.
DR   IntAct; P11972; 11.
DR   MINT; P11972; -.
DR   STRING; 4932.YLR452C; -.
DR   iPTMnet; P11972; -.
DR   MaxQB; P11972; -.
DR   PaxDb; 4932-YLR452C; -.
DR   PeptideAtlas; P11972; -.
DR   EnsemblFungi; YLR452C_mRNA; YLR452C; YLR452C.
DR   GeneID; 851173; -.
DR   KEGG; sce:YLR452C; -.
DR   AGR; SGD:S000004444; -.
DR   SGD; S000004444; SST2.
DR   VEuPathDB; FungiDB:YLR452C; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   HOGENOM; CLU_024143_0_0_1; -.
DR   InParanoid; P11972; -.
DR   OMA; DPGMRYL; -.
DR   OrthoDB; 1364107at2759; -.
DR   BioCyc; YEAST:G3O-32505-MONOMER; -.
DR   Reactome; R-SCE-416476; G alpha (q) signalling events.
DR   Reactome; R-SCE-418594; G alpha (i) signalling events.
DR   Reactome; R-SCE-418597; G alpha (z) signalling events.
DR   BioGRID-ORCS; 851173; 0 hits in 10 CRISPR screens.
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:0071444; P:cellular response to pheromone; 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   CDD; cd04450; DEP_RGS7-like; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   PANTHER; PTHR10845; REGULATOR OF G PROTEIN SIGNALING; 1.
DR   PANTHER; PTHR10845:SF192; RGS DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00615; RGS; 1.
DR   SMART; SM00049; DEP; 2.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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
//