PTP3_YEAST
ID PTP3_YEAST Reviewed; 928 AA.
AC P40048; D3DLY1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Tyrosine-protein phosphatase 3;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase 3;
DE Short=PTPase 3;
GN Name=PTP3; OrderedLocusNames=YER075C;
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], AND CHARACTERIZATION.
RX PubMed=9224718; DOI=10.1101/gad.11.13.1690;
RA Zhan X.-L., Deschenes R.J., Guan K.-L.;
RT "Differential regulation of FUS3 MAP kinase by tyrosine-specific
RT phosphatases PTP2/PTP3 and dual-specificity phosphatase MSG5 in
RT Saccharomyces cerevisiae.";
RL Genes Dev. 11:1690-1702(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 717; 738 AND 857.
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 FUNCTION.
RX PubMed=9032256; DOI=10.1128/mcb.17.3.1289;
RA Wurgler-Murphy S.M., Maeda T., Witten E.A., Saito H.;
RT "Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein
RT kinase by the PTP2 and PTP3 protein tyrosine phosphatases.";
RL Mol. Cell. Biol. 17:1289-1297(1997).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOG1.
RX PubMed=9211927; DOI=10.1074/jbc.272.28.17749;
RA Jacoby T., Flanagan H., Faykin A., Seto A.G., Mattison C.P., Ota I.M.;
RT "Two protein-tyrosine phosphatases inactivate the osmotic stress response
RT pathway in yeast by targeting the mitogen-activated protein kinase, Hog1.";
RL J. Biol. Chem. 272:17749-17755(1997).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 THR-75, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-297 AND SER-368, AND
RP IDENTIFICATION 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 insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Major phosphatase responsible for tyrosine dephosphorylation
CC of MAP kinases FUS3 and HOG1 to inactivate their activity; it also has
CC important roles, along with MSG5, in the inactivation of FUS3 following
CC pheromone stimulation. {ECO:0000269|PubMed:9032256,
CC ECO:0000269|PubMed:9211927}.
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 -!- SUBUNIT: Interacts with HOG1. {ECO:0000269|PubMed:9211927}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 768 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}.
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; AF006304; AAB70811.1; -; Genomic_DNA.
DR EMBL; U18814; AAB64614.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07735.2; -; Genomic_DNA.
DR PIR; S50578; S50578.
DR RefSeq; NP_010998.2; NM_001178966.2.
DR AlphaFoldDB; P40048; -.
DR SMR; P40048; -.
DR BioGRID; 36819; 113.
DR DIP; DIP-2370N; -.
DR IntAct; P40048; 11.
DR MINT; P40048; -.
DR STRING; 4932.YER075C; -.
DR iPTMnet; P40048; -.
DR MaxQB; P40048; -.
DR PaxDb; P40048; -.
DR PRIDE; P40048; -.
DR EnsemblFungi; YER075C_mRNA; YER075C; YER075C.
DR GeneID; 856807; -.
DR KEGG; sce:YER075C; -.
DR SGD; S000000877; PTP3.
DR VEuPathDB; FungiDB:YER075C; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000171635; -.
DR HOGENOM; CLU_007989_1_0_1; -.
DR InParanoid; P40048; -.
DR OMA; NWPDLGT; -.
DR BioCyc; YEAST:G3O-30246-MON; -.
DR Reactome; R-SCE-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:P40048; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40048; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0043937; P:regulation of sporulation; IGI:SGD.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 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..928
FT /note="Tyrosine-protein phosphatase 3"
FT /id="PRO_0000094857"
FT DOMAIN 111..232
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 502..878
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 247..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 804
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 717
FT /note="A -> P (in Ref. 1; AAB70811 and 2; AAB64614)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="K -> Q (in Ref. 1; AAB70811 and 2; AAB64614)"
FT /evidence="ECO:0000305"
FT CONFLICT 857
FT /note="Q -> E (in Ref. 1; AAB70811 and 2; AAB64614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 928 AA; 105224 MW; 9BB710EDAF7E3940 CRC64;
MKDSVDCPSI LPTDRTSVLS ETSTLVGSSS HVYSRHAPMN SYHNSMNSNI YHSPKASSPL
VSYKTSSPVL LKRATAPVLP SFKPKEQRYN KPQGCSLITA VELGKIIETL PDEKVLLLDV
RPFTEHAKSI ITNSIHVCLP STLLRRKNFT FSKLLDNLTP SEQSVLKSKL AIDNLRIIIY
DSTANQTESS VSLPCYGIAS KLIEFDTNVK KTVSILMCGF PQFKILFPDH INTNTFNSDC
ISSAEPKSPK TNLMNSLHNT APHMTATTPL SSPQMNLKLK VPDDSRSDHS NFSSSPSPRN
VLSDSPMSSS SPISALFKFQ LPAPQTNINQ MFKFSQNEEI MGLETYLSAV NIKEEHERWY
NNDSAKKSLQ NFQFPKNQNS LEKDTNKDKL GFQIRYENLS KNYEKEVIDS VIPEWFQHLM
SIPKIELVSQ FQKLDFLEKR RLNHSVSFRK KENSFILEKP SSYPEQLTST SSSTIMPPKF
PDVNKVQKRS HSQPIFTQYS KYKSMLSLES DSDSESDDVI ISSGVELGAK NRYKDIFPYE
HSRVILKKGL QSSKGIKHSH STSDGGILDN YINANYLSLP RFSVEQNSSF QTTTTTTRRV
RYIATQAPMP STVHDFYTCI LNNGVPLVLS LTNDFENGIE KCYRYWQEGN YNGIHVKLLE
KKILKMPSTT SMRKNTMGTQ NSSLYSAGVQ GNSSNYSTDN DNDNDNNNNN NNNSNIAVTA
AACDDDDDDD DDAILIRKIL LTYHDQEKPY ELLQIQVKNW PDLGTLLNPI SILQAINVKN
HIIDTLFARN YYQNDQLPTI LVHCSAGCGR TGTLCTIDSI LSNFEMFEML QKEFVKLKYP
AKLFDPISWT INIFRKQRIS MVQNINQFIF IYDCLLFYFR LRLDDITERT DGDGSNKDNI
SLSALIEQIE KLEILQTFVD DKLKELPQ
