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Database: UniProt
Entry: A0A2G5V4U3_9PELO
LinkDB: A0A2G5V4U3_9PELO
Original site: A0A2G5V4U3_9PELO 
ID   A0A2G5V4U3_9PELO        Unreviewed;      1422 AA.
AC   A0A2G5V4U3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=Cni-clr-1 {ECO:0000313|EMBL:PIC46798.1};
GN   Synonyms=Cnig_chr_II.g6376 {ECO:0000313|EMBL:PIC46798.1};
GN   ORFNames=B9Z55_006376 {ECO:0000313|EMBL:PIC46798.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC46798.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001490};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIC46798.1}.
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DR   EMBL; PDUG01000002; PIC46798.1; -; Genomic_DNA.
DR   STRING; 1611254.A0A2G5V4U3; -.
DR   Proteomes; UP000230233; Chromosome ii.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd00047; PTPc; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
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:SF495; TYROSINE-PROTEIN PHOSPHATASE 69D; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   4: Predicted;
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1422
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013962741"
FT   DOMAIN          61..102
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          159..269
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          373..503
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          796..1075
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          995..1066
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1144..1414
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1328..1405
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          646..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1422 AA;  160748 MW;  30ADB50FFE4C22D7 CRC64;
     MRINRWIWWT TVILLYLRTE LLQAADLFRS SEENEKAKDN IDNWNSTKIE PEKPKNAKEL
     GVHVCESNQD CVNGGVCHRG KDGHGICLCP RSCPSFVPPR CGNRRAAAPC LVMDKDYRSK
     YDLRDPTCYM NGCVCPPQFD TVHVTADQKP LRLNSTLLPT KCDKRDLAVV GRVHPSLSVF
     KGIDVTMFCC VNLDPEGFID VANVFFIQNG TLMREPTSHP FSPSTRGGIA RRVHEKQSCW
     ELEIKNVQTS DSGTYMCRVT ASAPDLDVTD TMQFEVKAPR QISKLNVTAS ERDAIVTWES
     EGEEMAIDLR LVRRSDTRGA VVYRGDNVTS PVVVKDLRAA TPYTLFASGK DGSVPFELTH
     HFTTGQKRPF PPKEEDVRIL NSGSSLSCEV EWKTPAETNG RITKYFVSVR GAMRKSDGTL
     TPDDFPSAEE VDKRCANWDE DESKSAQNGI NPIDFSNDFY SCKFGPLKPN RNYSVSVWAE
     NSAGRSLPAV FKKNCVTNFA QPDLVETPQT LRTANMTTFN LAFSHPPDDM NGPISCYYIA
     IVPLPTNVSL DLLPETNEIV MDSFTKVYAN NLHSSAAEKK RFFAYVAESY TELPMETVIG
     DGLGVSGLKA CNVRYLSRYT AEDLALRNGL KYTGFLIVRV DKEEELNRKG GPSGTNGSSI
     YRNLIDKSSP TTERSRTSSS ATRHLRQLHL SGPAYGYSGY FKPILLDSNS SSGGYGVFVK
     IVLPILIFLV CATCLSLFMI NRKNQFLSDW CPPFISKMAS KDVVERTLLK QTFGAIPVED
     LPTEYVTRHR DSDFLFVQEY EALPHFPMNT VASNRKENAI KNRYNDIRAF DETRVKLEQI
     GGDEHSDYIN ANFIKSWKEK KLFIAAQAPV EATIDDFWRM IWEQKSELIV MVANLTEKNR
     QQCAKYWPDE EISRYGDIIV EPTSVSFHSD YVVRKFDIAH IAECGPDVIL NENGVEYANV
     PIVKGQFAEN ARHILQYHFT NWNDYKAPEC STGLLRFMYI LRELPEFNNS PVVIHCSAGV
     GRTGTFITID SMFDQCLAER KANVFEFVCN LRRQRNLMVQ SVEQYVFIYK ALAEWHMYGY
     TDMDVADFEE HYQRLLCEST AASSSRDRAV SFNQSSSGNG SISTRVAIVS SRESILTSNS
     ETGLEEEFKK LERNLATGLP TSFASKDENL LKNRYEAAVP YDKYRVILPP TIGHADSSYI
     NASHIKGYFY DYIAAQDPVG TSSSTVFDFW RMIADQKVTT VVMLSDENDW SDSEKYWPIE
     GPGTDCHFQE GRNAIDVACV SLEQHQDFVV RHLTYTMKNA DSTSPIQDLT QYSYTAWPTD
     ALVPRSPNSL MNLISLVLQR QSNLLESRAP IVVHCRNGSS ETGIFICISL LMLRQKAEQR
     IDIFQTVKGL QSHRPMMFTR FEQYSFCYRA LADYISQTLL LR
//
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