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 15-DEC-1998 (Rel. 37, Last annotation update) DE PROTEIN-TYROSINE PHOSPHATASE MSG5 (EC 3.1.3.48). GN MSG5 OR YNL053W OR N2480 OR YNL2480W. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 94139675. RA Doi K., Gartner A., Ammerer G., Errede B., Shinkawa H., RA Sugimoto K., 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 SEQUENCE FROM N.A. RC STRAIN=FY1676; RX MEDLINE; 96021608. 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. RA Bergez P., Doignon F., Crouzet M.; RL Yeast 12:297-297(1996). RN [4] RP SEQUENCE OF 415-489 FROM N.A. RX MEDLINE; 88223509. RA Seraphin B., Simon M., Faye G.; RT "Primary structure of a gene for subunit V of the cytochrome c RT oxidase from Saccharomyces cerevisiae."; RL Curr. Genet. 9:435-439(1985). 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 = CC PROTEIN TYROSINE + ORTHOPHOSPHATE. CC -!- INDUCTION: BY PHEROMONE. CC -!- SIMILARITY: BELONGS TO THE NON-RECEPTOR CLASS OF THE PROTEIN- CC TYROSINE PHOSPHATASE FAMILY. DUAL SPECIFICITY SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; -. DR EMBL; U12141; AAA99659.1; -. DR EMBL; Z71329; CAA95922.1; -. DR EMBL; X02561; CAA26402.1; -. DR PIR; S40029; S40029. DR SGD; L0001188; MSG5. DR INTERPRO; IPR000340; -. DR INTERPRO; IPR000387; -. DR PFAM; PF00782; DSPc; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. KW Hydrolase; Cell cycle. FT ACT_SITE 319 319 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 //