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Database: UniProt
Entry: A0A2C9C3G0_CAEEL
LinkDB: A0A2C9C3G0_CAEEL
Original site: A0A2C9C3G0_CAEEL 
ID   A0A2C9C3G0_CAEEL        Unreviewed;       448 AA.
AC   A0A2C9C3G0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Tyrosine-protein phosphatase vhp-1 {ECO:0000313|EMBL:SOF58747.1};
GN   Name=vhp-1 {ECO:0000313|EMBL:SOF58747.1,
GN   ECO:0000313|WormBase:F08B1.1g};
GN   ORFNames=CELE_F08B1.1 {ECO:0000313|EMBL:SOF58747.1}, F08B1.1
GN   {ECO:0000313|WormBase:F08B1.1g};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:SOF58747.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:SOF58747.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:SOF58747.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily.
CC       {ECO:0000256|ARBA:ARBA00008601}.
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DR   EMBL; BX284602; SOF58747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9C3G0; -.
DR   SMR; A0A2C9C3G0; -.
DR   EnsemblMetazoa; F08B1.1g.1; F08B1.1g.1; WBGene00006923.
DR   AGR; WB:WBGene00006923; -.
DR   WormBase; F08B1.1g; CE52069; WBGene00006923; vhp-1.
DR   OrthoDB; 2879982at2759; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00006923; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR   ExpressionAtlas; A0A2C9C3G0; baseline and differential.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR10159:SF540; TYROSINE-PROTEIN PHOSPHATASE VHP-1; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Proteomics identification {ECO:0007829|EPD:A0A2C9C3G0,
KW   ECO:0007829|PeptideAtlas:A0A2C9C3G0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT   DOMAIN          1..109
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          29..90
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          144..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..432
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  47587 MW;  AB96F390AAEE5309 CRC64;
     MTCPKSVCIK EDKNFMRIPV NDSYQEKLSP YFPMAYEFLE KCRRAGKKCL IHCLAGISRS
     PTLAISYIMR YMKMGSDDAY RYVKERRPSI SPNFNFMGQL LEYENVLIKD HVLDYNQASR
     PHRHMDYYGP SDLCPPKVPK SASSNCVFPG STHDESSPSS PSVSEGSAAS EPETSSSAAS
     SSSTASAPPS MPSTSEQGTS SGTVNVNGKR NMTMDLGLPH RPKALGLPSR IGTSVAELPS
     PSTELSRLSF NGPEAIAPST PILNFTNPCF NSPIIPVASS SREVILTLPT PAASSSSSTS
     SEPSFDFSSF ESSSSSSIVV ENPFFASTEV PAGSSSISTP SGSQSTPASA SSSAASRCRM
     KGFFKVFSKK APASTSTPAS STPGTSRAAR PECLRSSGII ISAPVLAITE EEDAESPESG
     FNEPEVGEED DDSVSICSTS SLEIPCHQ
//
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