ID MSG5_YEAST STANDARD; PRT; 489 AA. AC P38590; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 07-FEB-2006 (Rel. 49, Last annotation update) DE Tyrosine-protein phosphatase MSG5 (EC 3.1.3.48). GN Name=MSG5; OrderedLocusNames=YNL053W; ORFNames=N2480, YNL2480W; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94139675; PubMed=8306972; 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 MEDLINE=96021608; PubMed=8533472; 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 MEDLINE=97060022; 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=S288c / FY1676; RX MEDLINE=97313269; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 415-489. RX MEDLINE=88223509; PubMed=2836092; 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 [6] RP LEVEL OF PROTEIN EXPRESSION. RX MEDLINE=22923965; 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). 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: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. CC -!- INDUCTION: By pheromone. CC -!- MISCELLANEOUS: Present with 538 molecules/cell. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Non-receptor class dual specificity subfamily. 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 PIR; S58725; S58725. DR HSSP; Q16828; 1MKP. DR IntAct; P38590; -. DR GermOnline; 143060; -. DR Ensembl; YNL053W; Saccharomyces cerevisiae. DR SGD; S000004998; MSG5. DR LinkHub; P38590; -. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0004727; F:prenylated protein tyrosine phosphatase act...; IMP. DR GO; GO:0000754; P:adaptation to pheromone during conjugation ...; IMP. DR GO; GO:0006470; P:protein amino acid dephosphorylation; IDA. DR InterPro; IPR000340; DS_phosphatase. DR InterPro; IPR000387; TYR_phosphatase. DR Pfam; PF00782; DSPc; 1. DR SMART; SM00195; DSPc; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. KW Cell cycle; Complete proteome; Hydrolase; Protein phosphatase. FT ACT_SITE 319 319 Phosphocysteine intermediate. FT MUTAGEN 319 319 C->A: Loss of activity. FT CONFLICT 347 348 NK -> DE (in Ref. 1). 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 //