PTP1_YEAST
ID PTP1_YEAST Reviewed; 335 AA.
AC P25044; D6VRC6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Tyrosine-protein phosphatase 1;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase 1;
DE Short=PTPase 1;
GN Name=PTP1; OrderedLocusNames=YDL230W;
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=1649172; DOI=10.1016/s0021-9258(18)98789-2;
RA Guan K., Deschenes R.J., Qiu H., Dixon J.E.;
RT "Cloning and expression of a yeast protein tyrosine phosphatase.";
RL J. Biol. Chem. 266:12964-12970(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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-83.
RX PubMed=10480872; DOI=10.1074/jbc.274.38.26697;
RA Moeslein F.M., Myers M.P., Landreth G.E.;
RT "The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the
RT tyrosine phosphatase, PTP-1B.";
RL J. Biol. Chem. 274:26697-26704(1999).
RN [5]
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).
CC -!- FUNCTION: Is not required for vegetative growth.
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 -!- INTERACTION:
CC P25044; P39940: RSP5; NbExp=2; IntAct=EBI-14183, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Activated by phosphorylation at Ser-83.
CC {ECO:0000269|PubMed:10480872}.
CC -!- MISCELLANEOUS: Present with 2690 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 subfamily. {ECO:0000305}.
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DR EMBL; M64062; AAA34923.1; -; Genomic_DNA.
DR EMBL; Z74278; CAA98809.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11636.1; -; Genomic_DNA.
DR PIR; A39862; A39862.
DR RefSeq; NP_010051.1; NM_001180290.1.
DR AlphaFoldDB; P25044; -.
DR SMR; P25044; -.
DR BioGRID; 31881; 123.
DR DIP; DIP-2765N; -.
DR IntAct; P25044; 14.
DR MINT; P25044; -.
DR STRING; 4932.YDL230W; -.
DR BindingDB; P25044; -.
DR ChEMBL; CHEMBL4452; -.
DR DrugCentral; P25044; -.
DR iPTMnet; P25044; -.
DR MaxQB; P25044; -.
DR PaxDb; P25044; -.
DR PRIDE; P25044; -.
DR EnsemblFungi; YDL230W_mRNA; YDL230W; YDL230W.
DR GeneID; 851368; -.
DR KEGG; sce:YDL230W; -.
DR SGD; S000002389; PTP1.
DR VEuPathDB; FungiDB:YDL230W; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000165633; -.
DR HOGENOM; CLU_001645_9_12_1; -.
DR InParanoid; P25044; -.
DR OMA; HFYFDQW; -.
DR BioCyc; YEAST:G3O-29609-MON; -.
DR Reactome; R-SCE-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:P25044; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P25044; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016277; Ptp1.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000938; PTPN1_yeast; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..335
FT /note="Tyrosine-protein phosphatase 1"
FT /id="PRO_0000094855"
FT DOMAIN 15..328
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 252
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT MOD_RES 83
FT /note="Phosphoserine; by CLK1"
FT /evidence="ECO:0000269|PubMed:10480872"
SQ SEQUENCE 335 AA; 38868 MW; 15F71E50694BE562 CRC64;
MAAAPWYIRQ RDTDLLGKFK FIQNQEDGRL REATNGTVNS RWSLGVSIEP RNDARNRYVN
IMPYERNRVH LKTLSGNDYI NASYVKVNVP GQSIEPGYYI ATQGPTRKTW DQFWQMCYHN
CPLDNIVIVM VTPLVEYNRE KCYQYWPRGG VDDTVRIASK WESPGGANDM TQFPSDLKIE
FVNVHKVKDY YTVTDIKLTP TDPLVGPVKT VHHFYFDLWK DMNKPEEVVP IMELCAHSHS
LNSRGNPIIV HCSAGVGRTG TFIALDHLMH DTLDFKNITE RSRHSDRATE EYTRDLIEQI
VLQLRSQRMK MVQTKDQFLF IYHAAKYLNS LSVNQ
