VHP1_CAEEL
ID VHP1_CAEEL Reviewed; 657 AA.
AC Q10038; Q8IG35; Q8ST18; Q8ST19;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Tyrosine-protein phosphatase vhp-1;
DE EC=3.1.3.48;
DE AltName: Full=Vh1 dual specificity phosphatase family protein 1;
GN Name=vhp-1; ORFNames=F08B1.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF CYS-262.
RX PubMed=15116070; DOI=10.1038/sj.emboj.7600226;
RA Mizuno T., Hisamoto N., Terada T., Kondo T., Adachi M., Nishida E.,
RA Kim D.H., Ausubel F.M., Matsumoto K.;
RT "The Caenorhabditis elegans MAPK phosphatase VHP-1 mediates a novel JNK-
RT like signaling pathway in stress response.";
RL EMBO J. 23:2226-2234(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, INTERACTION WITH PMK-3, AND MUTAGENESIS OF CYS-262.
RX PubMed=21670305; DOI=10.1073/pnas.1104830108;
RA Nix P., Hisamoto N., Matsumoto K., Bastiani M.;
RT "Axon regeneration requires coordinate activation of p38 and JNK MAPK
RT pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10738-10743(2011).
CC -!- FUNCTION: Acts preferentially on the c-Jun N-terminal kinase (JNK) and
CC p38 MAPKs. Plays an important role in the heavy metal stress response
CC and in axon regeneration by negatively regulating the kgb-1 (JNK-like)
CC and the pmk-1 (p38-type) MAPK signaling pathways.
CC {ECO:0000269|PubMed:15116070, ECO:0000269|PubMed:21670305}.
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: May interact with pmk-3. {ECO:0000269|PubMed:21670305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=Q10038-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q10038-2; Sequence=VSP_014014;
CC Name=c;
CC IsoId=Q10038-3; Sequence=VSP_014013, VSP_014015;
CC -!- TISSUE SPECIFICITY: Expressed in the pharynx, intestine, neurons and
CC vulval hypodermal cells. {ECO:0000269|PubMed:15116070}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:15116070}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AY585194; AAS91377.1; -; mRNA.
DR EMBL; FO081082; CCD68973.1; -; Genomic_DNA.
DR EMBL; FO081082; CCD68974.1; -; Genomic_DNA.
DR EMBL; FO081082; CCD68975.1; -; Genomic_DNA.
DR PIR; T15969; T15969.
DR RefSeq; NP_494997.1; NM_062596.4.
DR RefSeq; NP_494998.1; NM_062597.1. [Q10038-2]
DR RefSeq; NP_871926.1; NM_182126.3.
DR AlphaFoldDB; Q10038; -.
DR SMR; Q10038; -.
DR BioGRID; 39249; 3.
DR DIP; DIP-59690N; -.
DR IntAct; Q10038; 1.
DR STRING; 6239.F08B1.1a.2; -.
DR iPTMnet; Q10038; -.
DR EPD; Q10038; -.
DR PaxDb; Q10038; -.
DR PeptideAtlas; Q10038; -.
DR EnsemblMetazoa; F08B1.1a.1; F08B1.1a.1; WBGene00006923. [Q10038-1]
DR EnsemblMetazoa; F08B1.1a.2; F08B1.1a.2; WBGene00006923. [Q10038-1]
DR EnsemblMetazoa; F08B1.1b.1; F08B1.1b.1; WBGene00006923. [Q10038-2]
DR GeneID; 173904; -.
DR UCSC; F08B1.1a.3; c. elegans. [Q10038-1]
DR CTD; 173904; -.
DR WormBase; F08B1.1a; CE27918; WBGene00006923; vhp-1. [Q10038-1]
DR WormBase; F08B1.1b; CE27919; WBGene00006923; vhp-1. [Q10038-2]
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000167194; -.
DR HOGENOM; CLU_408947_0_0_1; -.
DR InParanoid; Q10038; -.
DR OMA; CISYIMR; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q10038; -.
DR Reactome; R-CEL-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-CEL-5675221; Negative regulation of MAPK pathway.
DR SignaLink; Q10038; -.
DR PRO; PR:Q10038; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006923; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q10038; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:WormBase.
DR GO; GO:0008579; F:JUN kinase phosphatase activity; IDA:WormBase.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IDA:WormBase.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0048692; P:negative regulation of axon extension involved in regeneration; IMP:UniProtKB.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IDA:WormBase.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IMP:UniProtKB.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:1903854; P:negative regulation of stress response to copper ion; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:WormBase.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IGI:UniProtKB.
DR GO; GO:0046686; P:response to cadmium ion; IMP:UniProtKB.
DR GO; GO:0046688; P:response to copper ion; IGI:WormBase.
DR GO; GO:0006986; P:response to unfolded protein; IMP:UniProtKB.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 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; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..657
FT /note="Tyrosine-protein phosphatase vhp-1"
FT /id="PRO_0000094925"
FT DOMAIN 21..151
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 175..318
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 353..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..641
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 262
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 1..155
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_014013"
FT VAR_SEQ 1..136
FT /note="MTVLDTVTISTCGLAALIREAPDTTLVVDCRGFTEYNESHVRHSMNAFFSKL
FT IRRRLFENKLDDNCLIHQLMSCSSGCTKMDEKLDLVLYAEEDKPRGNKRRIASCNAPES
FT TAKIMRVLRERLEDTDKFRSVMVLE -> MGGQPFEAFRKNRKRKKTKNKKKRRNNNNS
FT KNKTPNTFPNEIEEQDPVSSLPTFPAKKFGLKLQLTLTSSPTNSSSPISSSSPTN (in
FT isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_014014"
FT VAR_SEQ 588..657
FT /note="ASSTPGTSRAARPECLRSSGIIISAPVLAITEEEDAESPESGFNEPEVGEED
FT DDSVSICSTSSLEIPCHQ -> VSIMKLH (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_014015"
FT MUTAGEN 262
FT /note="C->S: Loss of kgb-1 inhibition. No effect on
FT interaction with pmk-3."
FT /evidence="ECO:0000269|PubMed:15116070,
FT ECO:0000269|PubMed:21670305"
SQ SEQUENCE 657 AA; 71003 MW; A0D9153DE6326B43 CRC64;
MTVLDTVTIS TCGLAALIRE APDTTLVVDC RGFTEYNESH VRHSMNAFFS KLIRRRLFEN
KLDDNCLIHQ LMSCSSGCTK MDEKLDLVLY AEEDKPRGNK RRIASCNAPE STAKIMRVLR
ERLEDTDKFR SVMVLEGGFK QFAQQYPQLC ESSEGMTRLP QSLSQPCLSQ PTGDGITLIT
PNIYLGSQID SLDETMLDAL DISVVINLSM TCPKSVCIKE DKNFMRIPVN DSYQEKLSPY
FPMAYEFLEK CRRAGKKCLI HCLAGISRSP TLAISYIMRY MKMGSDDAYR YVKERRPSIS
PNFNFMGQLL EYENVLIKDH VLDYNQASRP HRHMDYYGPS DLCPPKVPKS ASSNCVFPGS
THDESSPSSP SVSEGSAASE PETSSSAASS SSTASAPPSM PSTSEQGTSS GTVNVNGKRN
MTMDLGLPHR PKALGLPSRI GTSVAELPSP STELSRLSFN GPEAIAPSTP ILNFTNPCFN
SPIIPVASSS REVILTLPTP AASSSSSTSS EPSFDFSSFE SSSSSSIVVE NPFFASTEVP
AGSSSISTPS GSQSTPASAS SSAASRCRMK GFFKVFSKKA PASTSTPASS TPGTSRAARP
ECLRSSGIII SAPVLAITEE EDAESPESGF NEPEVGEEDD DSVSICSTSS LEIPCHQ
