ID   PVH1_YEAST              Reviewed;         364 AA.
AC   Q02256; D6VVV7;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Tyrosine-protein phosphatase YVH1 {ECO:0000303|PubMed:1334559};
DE            Short=PTPase YVH1;
DE            EC=3.1.3.48 {ECO:0000269|PubMed:1334559};
GN   Name=YVH1; OrderedLocusNames=YIR026C;
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], CATALYTIC ACTIVITY, AND INDUCTION BY
RP   NITROGEN STARVATION.
RX   PubMed=1334559; DOI=10.1073/pnas.89.24.12175;
RA   Guan K., Hakes D.J., Wang Y., Park H.-D., Cooper T.G., Dixon J.E.;
RT   "A yeast protein phosphatase related to the vaccinia virus VH1 phosphatase
RT   is induced by nitrogen starvation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:12175-12179(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-197.
RX   PubMed=1803816; DOI=10.1002/yea.320070903;
RA   Buckholz R.G., Cooper T.G.;
RT   "The allantoinase (DAL1) gene of Saccharomyces cerevisiae.";
RL   Yeast 7:913-923(1991).
RN   [5]
RP   ERRATUM OF PUBMED:1803816.
RA   Buckholz R.G., Cooper T.G.;
RL   Yeast 8:239-239(1992).
RN   [6]
RP   SIMILARITY TO VH1.
RX   PubMed=8438236; DOI=10.1016/0968-0004(93)90079-3;
RA   Guan K., Hakes D.J., Dixon J.E., Park H.D., Cooper T.G.;
RT   "The yeast open reading frame encoding a dual specificity phosphatase.";
RL   Trends Biochem. Sci. 18:6-6(1993).
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-196, 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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: May be directly involved in signal transduction and/or cell
CC       cycle regulation. It is necessary for maintaining growth rate or spore
CC       germination. Could show both activity toward tyrosine-protein phosphate
CC       as well as with serine-protein phosphate.
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;
CC         Evidence={ECO:0000269|PubMed:1334559};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC         Evidence={ECO:0000305|PubMed:1334559};
CC   -!- INTERACTION:
CC       Q02256; P53145: LSG1; NbExp=3; IntAct=EBI-14322, EBI-23885;
CC   -!- INDUCTION: By nitrogen starvation. {ECO:0000269|PubMed:1334559}.
CC   -!- MISCELLANEOUS: Present with 7570 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; L04673; AAA34874.1; -; Genomic_DNA.
DR   EMBL; Z38061; CAA86186.1; -; Genomic_DNA.
DR   EMBL; M69294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006942; DAA08573.1; -; Genomic_DNA.
DR   PIR; S31304; S31304.
DR   RefSeq; NP_012292.3; NM_001179548.3.
DR   PDB; 6N8M; EM; 3.50 A; Y=1-364.
DR   PDB; 6N8N; EM; 3.80 A; Y=1-364.
DR   PDB; 6N8O; EM; 3.50 A; Y=1-364.
DR   PDB; 6RZZ; EM; 3.20 A; s=1-364.
DR   PDB; 6S05; EM; 3.90 A; s=1-364.
DR   PDBsum; 6N8M; -.
DR   PDBsum; 6N8N; -.
DR   PDBsum; 6N8O; -.
DR   PDBsum; 6RZZ; -.
DR   PDBsum; 6S05; -.
DR   AlphaFoldDB; Q02256; -.
DR   EMDB; EMD-0372; -.
DR   EMDB; EMD-0373; -.
DR   EMDB; EMD-0374; -.
DR   EMDB; EMD-10068; -.
DR   EMDB; EMD-10071; -.
DR   SMR; Q02256; -.
DR   BioGRID; 35017; 128.
DR   DIP; DIP-5192N; -.
DR   IntAct; Q02256; 27.
DR   MINT; Q02256; -.
DR   STRING; 4932.YIR026C; -.
DR   iPTMnet; Q02256; -.
DR   MaxQB; Q02256; -.
DR   PaxDb; 4932-YIR026C; -.
DR   PeptideAtlas; Q02256; -.
DR   EnsemblFungi; YIR026C_mRNA; YIR026C; YIR026C.
DR   GeneID; 854844; -.
DR   KEGG; sce:YIR026C; -.
DR   AGR; SGD:S000001465; -.
DR   SGD; S000001465; YVH1.
DR   VEuPathDB; FungiDB:YIR026C; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000174926; -.
DR   HOGENOM; CLU_023312_0_1_1; -.
DR   InParanoid; Q02256; -.
DR   OMA; FAWQGMQ; -.
DR   OrthoDB; 5472710at2759; -.
DR   BioCyc; YEAST:G3O-31445-MONOMER; -.
DR   BioGRID-ORCS; 854844; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q02256; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; Q02256; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:1990275; F:preribosome binding; IDA:SGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:SGD.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISA:SGD.
DR   GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR   GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:SGD.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR   CDD; cd14518; DSP_fungal_YVH1; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR016278; DUSP12.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR45848:SF4; DUAL SPECIFICITY PROTEIN PHOSPHATASE 12; 1.
DR   PANTHER; PTHR45848; DUAL SPECIFICITY PROTEIN PHOSPHATASE 12 FAMILY MEMBER; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   PIRSF; PIRSF000941; DUSP12; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Phosphoprotein; Protein phosphatase;
KW   Reference proteome; Stress response.
FT   CHAIN           1..364
FT                   /note="Tyrosine-protein phosphatase YVH1"
FT                   /id="PRO_0000094854"
FT   DOMAIN          11..173
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        117
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        71
FT                   /note="Missing (in Ref. 4; M69294)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  41185 MW;  9E75C7CC14353B43 CRC64;
     MAGNANSVDE EVTRILGGIY LGGIRPIIDH RPLGAEFNIT HILSVIKFQV IPEYLIRKGY
     TLKNIPIDDD DVTDVLQYFD ETNRFIDQCL FPNEVEYSPR LVDFKKKPQR GAVFAHCQAG
     LSRSVTFIVA YLMYRYGLSL SMAMHAVKRK KPSVEPNENF MEQLHLFEKM GGDFVDFDNP
     AYKQWKLKQS IKLDPSGSEL VSNSGMFKDS ESSQDLDKLT EAEKSKVTAV RCKKCRTKLA
     LSTSFIAHDP PSKESSEGHF IKRAANSHRI IDIQESQANC SHFFIEPLKW MQPELQGKQE
     LEGKFSCPGC SSKVGGYNWK GSRCSCGKWV IPAIHLQTSK VDQFPLQSTA LPNMVNFESE
     KVNR
//