PTP5_CAEEL
ID PTP5_CAEEL Reviewed; 359 AA.
AC P34442;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable tyrosine-protein phosphatase F54C8.4;
DE EC=3.1.3.48;
GN ORFNames=F54C8.4;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000305}.
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DR EMBL; Z22178; CAA80156.1; -; Genomic_DNA.
DR PIR; S40746; S40746.
DR RefSeq; NP_001254988.1; NM_001268059.1.
DR AlphaFoldDB; P34442; -.
DR SMR; P34442; -.
DR STRING; 6239.F54C8.4a; -.
DR EPD; P34442; -.
DR PaxDb; P34442; -.
DR PeptideAtlas; P34442; -.
DR EnsemblMetazoa; F54C8.4a.1; F54C8.4a.1; WBGene00010037.
DR GeneID; 176323; -.
DR KEGG; cel:CELE_F54C8.4; -.
DR UCSC; F54C8.4; c. elegans.
DR CTD; 176323; -.
DR WormBase; F54C8.4a; CE00190; WBGene00010037; -.
DR eggNOG; KOG2386; Eukaryota.
DR GeneTree; ENSGT00940000168004; -.
DR HOGENOM; CLU_065449_0_0_1; -.
DR InParanoid; P34442; -.
DR OMA; YEKINCP; -.
DR OrthoDB; 1544021at2759; -.
DR PhylomeDB; P34442; -.
DR PRO; PR:P34442; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010037; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; P34442; baseline and differential.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..359
FT /note="Probable tyrosine-protein phosphatase F54C8.4"
FT /id="PRO_0000094885"
FT DOMAIN 16..191
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 184..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..308
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 359 AA; 41111 MW; 55BB1D1E6DC45935 CRC64;
MVRVCRVVPK DWSKFQPVGN VIPRTRFIVF KTPINSQLST KIHKEQRFTT NDLFRQLSER
GQYLGLVVDL SDTDRYYDKK DITGMCVQYE KVNCPGRGFI ERDDCVESFH QVIQDYTDKC
DDPDALIGVH CTNGINRCGY LICRFLIDRL GWSSHEAIDA FEQARGYSIE KGAYVMALHK
AAKDKRDKQV DSDSDSSERQ RKKKNKRKHR EIVEHENIVL INTIIGELGS QAASVSGTDY
QNSPNGVSVD PGQPQPHHWG FAIKRSKYAQ LNQPVANGAN TPPEPSEGTP QEEEEFEEDF
EEIEEETETE PGKGQSVSSK RRARRNRMQK YMQVMQRGRF HEIQAIREEV ALSHGSARD
