ID   YK13_CAEEL              Reviewed;         398 AA.
AC   P34337;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Putative tyrosine-protein phosphatase C15H7.3;
DE            EC=3.1.3.48;
GN   ORFNames=C15H7.3;
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;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000305}.
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DR   EMBL; Z22173; CAA80125.1; -; Genomic_DNA.
DR   PIR; S40752; S40752.
DR   RefSeq; NP_499135.1; NM_066734.5.
DR   AlphaFoldDB; P34337; -.
DR   SMR; P34337; -.
DR   STRING; 6239.C15H7.3; -.
DR   PaxDb; P34337; -.
DR   EnsemblMetazoa; C15H7.3.1; C15H7.3.1; WBGene00007610.
DR   EnsemblMetazoa; C15H7.3.2; C15H7.3.2; WBGene00007610.
DR   GeneID; 182639; -.
DR   KEGG; cel:CELE_C15H7.3; -.
DR   UCSC; C15H7.3; c. elegans.
DR   CTD; 182639; -.
DR   WormBase; C15H7.3; CE00081; WBGene00007610; -.
DR   eggNOG; KOG0789; Eukaryota.
DR   GeneTree; ENSGT00970000195861; -.
DR   HOGENOM; CLU_058106_0_0_1; -.
DR   InParanoid; P34337; -.
DR   OMA; LHNWRQK; -.
DR   PhylomeDB; P34337; -.
DR   PRO; PR:P34337; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00007610; Expressed in material anatomical entity and 2 other tissues.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..398
FT                   /note="Putative tyrosine-protein phosphatase C15H7.3"
FT                   /id="PRO_0000094927"
FT   DOMAIN          125..376
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  44926 MW;  CEEDE09FA0BC8F68 CRC64;
     MERSQKSARK KKKTSKSGND RSIRSERKSK QKKPAGEKSQ KSRRTRKSRG PKGNGFTSRE
     TIQPSSSGQS EGTTRMDDQK DEKKDDKKEE KKEERKEEKK EEVKEPWSEE EPAKRMVANG
     FFTTTNVGGT FKQTDNFKTP MDSCPSFKNN MHKIRAPDCP IPEEKLVKLT NGPESFICAA
     KITVPDFNRT MILTQVPDLS SAPDIADFWR MIHQESIASV VIAVMPLEVT LQQILPLLSG
     TYSTYGKMFV NNKKVESAVG MTEYCLEIFP DGCSNSLLTT VYHLHNWRQK RGLEVVTDLV
     ATMEKVMKVN DNTVLMSMNG TGRAGTMLTL FTAMLQVQKG KEVNAKETLA SLRAERCGIV
     DNIDQFGTVH RSMACWFKNN STNEEVQRKV VEFAPSIQ