ID MSG5_YEAST Reviewed; 489 AA. AC P38590; D6W1C6; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 16-OCT-2019, entry version 167. DE RecName: Full=Tyrosine-protein phosphatase MSG5; DE EC=3.1.3.48; GN Name=MSG5; OrderedLocusNames=YNL053W; ORFNames=N2480, YNL2480W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8306972; DOI=10.1002/j.1460-2075.1994.tb06235.x; RA Doi K., Gartner A., Ammerer G., Errede B., Shinkawa H., Sugimoto K., RA Matsumoto K.; RT "MSG5, a novel protein phosphatase promotes adaptation to pheromone RT response in S. cerevisiae."; RL EMBO J. 13:61-70(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S288c / FY1676; RX PubMed=8533472; DOI=10.1002/yea.320111008; RA Bergez P., Doignon F., Crouzet M.; RT "The sequence of a 44 420 bp fragment located on the left arm of RT chromosome XIV from Saccharomyces cerevisiae."; RL Yeast 11:967-974(1995). RN [3] RP ERRATUM. RX PubMed=8904343; RX DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d; RA Bergez P., Doignon F., Crouzet M.; RL Yeast 12:297-297(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., RA Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., RA Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., RA Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., RA Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., RA Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., RA Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., RA Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., RA Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., RA Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., RA Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., RA Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., RA Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., RA Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV RT and its evolutionary implications."; RL Nature 387:93-98(1997). RN [5] 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 415-489. RX PubMed=2836092; DOI=10.1007/bf00434047; RA Seraphin B., Simon M., Faye G.; RT "Primary structure of a gene for subunit V of the cytochrome c oxidase RT from Saccharomyces cerevisiae."; RL Curr. Genet. 9:435-439(1985). RN [7] 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., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-151 AND THR-178, RP AND 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 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION RP 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 RT insights into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Dual specificity phosphatase that dephosphorylates MAP CC kinase FUS3 on both a Tyr and a Ser or Thr. Has a role in CC adaptation to pheromone. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] CC + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, CC Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; CC -!- INDUCTION: By pheromone. CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Non-receptor class dual specificity subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D17548; BAA04485.1; -; Genomic_DNA. DR EMBL; U12141; AAA99659.1; -; Genomic_DNA. DR EMBL; Z71329; CAA95922.1; -; Genomic_DNA. DR EMBL; X02561; CAA26402.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10492.1; -; Genomic_DNA. DR PIR; S58725; S58725. DR RefSeq; NP_014345.3; NM_001182892.3. DR SMR; P38590; -. DR BioGrid; 35771; 153. DR DIP; DIP-5538N; -. DR ELM; P38590; -. DR IntAct; P38590; 16. DR MINT; P38590; -. DR STRING; 4932.YNL053W; -. DR iPTMnet; P38590; -. DR PaxDb; P38590; -. DR PRIDE; P38590; -. DR EnsemblFungi; YNL053W_mRNA; YNL053W; YNL053W. DR GeneID; 855674; -. DR KEGG; sce:YNL053W; -. DR EuPathDB; FungiDB:YNL053W; -. DR SGD; S000004998; MSG5. DR HOGENOM; HOG000066070; -. DR InParanoid; P38590; -. DR KO; K11240; -. DR OMA; MRRSEAS; -. DR BioCyc; YEAST:G3O-33085-MONOMER; -. DR Reactome; R-SCE-112409; RAF-independent MAPK1/3 activation. DR Reactome; R-SCE-202670; ERKs are inactivated. DR Reactome; R-SCE-5675221; Negative regulation of MAPK pathway. DR PRO; PR:P38590; -. DR Proteomes; UP000002311; Chromosome XIV. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase 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:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0000188; P:inactivation of MAPK activity; IDA:SGD. DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IGI:SGD. DR GO; GO:0006470; P:protein dephosphorylation; IDA:SGD. DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD. DR GO; GO:0071701; P:regulation of MAPK export from nucleus; IMP:SGD. DR GO; GO:0010969; P:regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; IBA:GO_Central. DR Gene3D; 3.90.190.10; -; 1. DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR000387; TYR_PHOSPHATASE_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR Pfam; PF00782; DSPc; 1. DR SMART; SM00195; DSPc; 1. DR SUPFAM; SSF52799; SSF52799; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. PE 1: Evidence at protein level; KW Cell cycle; Complete proteome; Hydrolase; Phosphoprotein; KW Protein phosphatase; Reference proteome. FT CHAIN 1 489 Tyrosine-protein phosphatase MSG5. FT /FTId=PRO_0000094916. FT ACT_SITE 319 319 Phosphocysteine intermediate. FT MOD_RES 22 22 Phosphoserine. FT {ECO:0000244|PubMed:17330950}. FT MOD_RES 98 98 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT MOD_RES 151 151 Phosphoserine. FT {ECO:0000244|PubMed:17330950}. FT MOD_RES 178 178 Phosphothreonine. FT {ECO:0000244|PubMed:17330950}. FT MUTAGEN 319 319 C->A: Loss of activity. FT CONFLICT 347 348 NK -> DE (in Ref. 1; BAA04485). FT {ECO:0000305}. SQ SEQUENCE 489 AA; 54217 MW; 0D02380B62EA48DC CRC64; MQFHSDKQHL DSKTDIDFKP NSPRSLQNRN TKNLSLDIAA LHPLMEFSSP SQDVPGSVKF PSPTPLNLFM KPKPIVLEKC PPKVSPRPTP PSLSMRRSEA SIYTLPTSLK NRTVSPSVYT KSSTVSSISK LSSSSPLSSF SEKPHLNRVH SLSVKTKDLK LKGIRGRSQT ISGLETSTPI SSTREGTLDS TDVNRFSNQK NMQTTLIFPE EDSDLNIDMV HAEIYQRTVY LDGPLLVLPP NLYLYSEPKL EDILSFDLVI NVAKEIPNLE FLIPPEMAHK IKYYHIEWTH TSKIVKDLSR LTRIIHTAHS QGKKILVHCQ CGVSRSASLI VAYIMRYYGL SLNDAYNKLK GVAKDISPNM GLIFQLMEWG TMLSKNSPGE EGETVHMPEE DDIGNNEVSS TTKSYSSASF RSFPMVTNLS SSPNDSSVNS SEVTPRTPAT LTGARTALAT ERGEDDEHCK SLSQPADSLE ASVDNESIST APEQMMFLP //