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Database: UniProt
Entry: G5EC69_CAEEL
LinkDB: G5EC69_CAEEL
Original site: G5EC69_CAEEL 
ID   G5EC69_CAEEL            Unreviewed;       864 AA.
AC   G5EC69;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 92.
DE   SubName: Full=Receptor-type tyrosine-protein phosphatase kappa {ECO:0000313|EMBL:CAO94911.2};
GN   ORFNames=CELE_T13H5.1 {ECO:0000313|EMBL:CAO94911.2}, T13H5.1
GN   {ECO:0000313|EMBL:CAO94911.2, ECO:0000313|WormBase:T13H5.1c};
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:CAO94911.2, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CAO94911.2, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAO94911.2,
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).
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DR   EMBL; BX284602; CAO94911.2; -; Genomic_DNA.
DR   RefSeq; NP_001122640.1; NM_001129168.1.
DR   AlphaFoldDB; G5EC69; -.
DR   SMR; G5EC69; -.
DR   STRING; 6239.T13H5.1c.1; -.
DR   PaxDb; 6239-T13H5-1c; -.
DR   PeptideAtlas; G5EC69; -.
DR   EnsemblMetazoa; T13H5.1c.1; T13H5.1c.1; WBGene00011755.
DR   GeneID; 174359; -.
DR   AGR; WB:WBGene00011755; -.
DR   WormBase; T13H5.1c; CE42278; WBGene00011755; -.
DR   eggNOG; KOG4228; Eukaryota.
DR   InParanoid; G5EC69; -.
DR   OrthoDB; 2875525at2759; -.
DR   PhylomeDB; G5EC69; -.
DR   Reactome; R-CEL-388844; Receptor-type tyrosine-protein phosphatases.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00011755; Expressed in larva and 3 other cell types or tissues.
DR   ExpressionAtlas; G5EC69; baseline and differential.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IBA:GO_Central.
DR   CDD; cd00047; PTPc; 2.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE S; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|EPD:G5EC69,
KW   ECO:0007829|PeptideAtlas:G5EC69}; Receptor {ECO:0000313|EMBL:CAO94911.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT   DOMAIN          207..466
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          381..457
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          499..798
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          713..789
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          810..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..840
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   864 AA;  100530 MW;  241149CFAE397236 CRC64;
     MIESNSTSKF SSFFRRKPKD VKLDMNGNGL VSPHDEHQDE LEDPMASVSI RVRNEEGDDF
     VVSPSDVVDN INEINSRRSS RRDSTPASSI RRSRPSSSAY FNENGEPIEG INRPPRKFKS
     MDHIMMRLFK PSKARKSKSV RDAEPGLRSM LYGLSQKQEK EEAIAKKLAK KMIIQEEKAM
     QAVPTSPVDA SKFVAYVQER RKKRILFKGE YLMVNRSIDN NKCRCDVGST MMDRNPYPDT
     LPYDYNRVIL PRIDGDENSH YINASYVNSW LRDKAYVVTQ AVRTKPMNAE FWRMVWELGS
     NCIVMLTKVF DFMRVMCLQY WPLTKFQFRE IEVETTEVKT YSHFVIRTFK LTRTTPESIE
     TRIVKHFHFT EWELDSFPYI SAFIELRRRV RQFMEKNPVE APMVVHCSNG AGRSGAFLAL
     DANLELMKKT GQLDFFEYAK TLVNSRPHLI DSVEQYMFIY EVLSEAVMCN VQPIEMHLLK
     ERSSMYKAKK NRELLETQET HENKLLMHLT PTLRIGDCAG GHRLENRGKN RDVMVVPPDH
     ARPYLQTLHG ESKDYTYINA VEVDGFTRKA EFIVTEWPKQ STVDSFWTLI YDHACHTVVN
     LSNQGSQRHY PSFIHNKGKA NYGPFIVEIM NYHQYPAMTS HMVKVMKRPH QVPPMKVDPE
     GKGVSKLTFM ISDIMATGAQ NQQIDAEVRI CCVIQVRMWP IENKVPLSTT GLIDVIKMAR
     SWRKRAPDRP ETKPTIVMSH NGVSRVGVYI GANICIDQMD IDHEVDVFHA VKMMRINRPQ
     LIDMKDEYKY LYDVMLHWYM TNPDYRIYDK EDSEDTDSQK TSRPPSNRHS IKEKSSFRSK
     FSFRRRNTTR QNENNAVDQR VNSN
//
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