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   27-MAR-2024, entry version 189.
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; Saccharomycetes;
OC   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 chromosome
RT   XIV from Saccharomyces cerevisiae.";
RL   Yeast 11:967-974(1995).
RN   [3]
RP   ERRATUM OF PUBMED:8533472.
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., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   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., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and 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 from
RT   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., 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-151 AND THR-178, 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   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, 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: Dual specificity phosphatase that dephosphorylates MAP kinase
CC       FUS3 on both a Tyr and a Ser or Thr. Has a role in adaptation to
CC       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, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- INDUCTION: By pheromone.
CC   -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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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   AlphaFoldDB; P38590; -.
DR   SMR; P38590; -.
DR   BioGRID; 35771; 158.
DR   DIP; DIP-5538N; -.
DR   ELM; P38590; -.
DR   IntAct; P38590; 16.
DR   MINT; P38590; -.
DR   STRING; 4932.YNL053W; -.
DR   iPTMnet; P38590; -.
DR   PaxDb; 4932-YNL053W; -.
DR   PeptideAtlas; P38590; -.
DR   EnsemblFungi; YNL053W_mRNA; YNL053W; YNL053W.
DR   GeneID; 855674; -.
DR   KEGG; sce:YNL053W; -.
DR   AGR; SGD:S000004998; -.
DR   SGD; S000004998; MSG5.
DR   VEuPathDB; FungiDB:YNL053W; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000175236; -.
DR   HOGENOM; CLU_036115_0_0_1; -.
DR   InParanoid; P38590; -.
DR   OMA; HIEWTHT; -.
DR   OrthoDB; 53899at2759; -.
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   BioGRID-ORCS; 855674; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P38590; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P38590; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0033550; F:MAP kinase tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
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   CDD; cd14521; DSP_fungal_SDP1-like; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR10159:SF531; DUAL-SPECIFICITY PROTEIN PHOSPHATASE SDP1-RELATED; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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; Hydrolase; Phosphoprotein; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..489
FT                   /note="Tyrosine-protein phosphatase MSG5"
FT                   /id="PRO_0000094916"
FT   DOMAIN          233..375
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        319
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         178
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MUTAGEN         319
FT                   /note="C->A: Loss of activity."
FT   CONFLICT        347..348
FT                   /note="NK -> DE (in Ref. 1; BAA04485)"
FT                   /evidence="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
//