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Database: UniProt
Entry: H3C132_TETNG
LinkDB: H3C132_TETNG
Original site: H3C132_TETNG 
ID   H3C132_TETNG            Unreviewed;      1444 AA.
AC   H3C132;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRK {ECO:0000313|Ensembl:ENSTNIP00000001948.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000001948.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000001948.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2B subfamily. {ECO:0000256|ARBA:ARBA00006396}.
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DR   STRING; 99883.ENSTNIP00000001948; -.
DR   Ensembl; ENSTNIT00000000429.1; ENSTNIP00000001948.1; ENSTNIG00000010747.1.
DR   GeneTree; ENSGT00940000156249; -.
DR   InParanoid; H3C132; -.
DR   OMA; RIATKXK; -.
DR   TreeFam; TF312900; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd06263; MAM; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000998; MAM_dom.
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:SF209; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE KAPPA; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00020; MAMDOMAIN.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50060; MAM_2; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000007303};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT   DOMAIN          2..164
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          453..559
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          891..1145
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1065..1136
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1177..1440
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1353..1431
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
SQ   SEQUENCE   1444 AA;  163272 MW;  066702963654AAEB CRC64;
     AGSCSFDEGF STCNYQHDLN GDFDWTHINT KAVPYVSPDL PQALFEYVKD RNMSQGKASS
     LLLNQVCARS DAHILCASVL IIKSDGSGQG VQSNVMVKVN RAQPANPIWN VTSFTGKNWL
     KAELAVSTFW PNEYQVLFEA SVSKSKAGFI AIDNVQVLSY PCGPLPSLPL HLLSPEISLC
     CKRKKITPHV QLWSEEVFEK ELVLALHCDS IHSSSCSSAR TLVCEVTSQD QDLFRCVTQS
     ELGSGVSNFA HLFVKGPDKP FTIDDLFCFS VSYISNWKIG QTIIKLGSII FLHVAYRMTS
     GSWTETHAVN TVTYKLWHLD PDTEYEIRVL LTRPGEGGTG KPGPPLITRT KCAEPMRTPK
     RLKIARTMSR LIAVDWESLG YNITRCHTFN VTICYQYTTA NKIFLFNKFF STAPRHLVEN
     LPPYTNVSLK LILINPEGRK ESDDTIVQTD EDVPGPVPSQ SLRAFPSEDS ILLYWKKPSE
     PNGIIIQYEI SYCGLHSFDP SFPLDQSVLT VSLPSNATNH TFSQLHPGVT YELSIRASTS
     KGFGQAVTLN ITTNISAPTI EKYDGSEAFL NETETTITVL VKPAQAKGAP ISNYYIVVDK
     ENQQRRRRQA PSDCYTVPFS YSDASKSGSN YYFAANLCPE NILEPIPFTV GDNKTYQGFW
     NPPLALRKTY NIYLQAVSST TKESKRHCLK LASKVNPWAA ATHTQMQSEC FEMLVGATEE
     PNFVPDPAKQ TNPTMKITGI CLSVIVPILL VALTVFLVKK RLAHNPRRTY YSYSYYLINR
     KLARKRQDVI RTTGQEMTDL GNSTDRSYAE RSTLHREDPM AVTFVETHTY NNRYENHGGS
     AAENSHLLDI ARYHCEGTES PYQTGQLHPA IRVADLLQHI NLMKTSDSYG FKEEYESLFE
     GQSASWDVAK KEQNRTKNRY GNIIAYDHSR VILQPIENDP SSDYINANYI DGYQRPSHYI
     ATQGPVHETV YDFWRMVWQE QSACIVMVTN LVEVGRVKCF KYWPEDAELY GDFKVTYLET
     EHLAEYVVRT FTLERRGFNE MREVKQFHFT GWPDHGVPYH ATGLLSFIRR VKISNPPSAG
     PIVVHCSAGA GRTGCFIVID IMLDMAEREG VVDIYNCVKA LRSRRINMVQ TEEQYIFIHD
     AILEACLCGE TAISICEFKA AFYELIRIDS QTNSSHLKDE FQTLNSVTPQ PQPEDCSIAL
     LPRNQDKNRF MSGLPPDRCL PFLLTMDGES SNYINAALMD SYRQPAEFIV TQHPLPNTVK
     DFWRLVYDYG CASLVMLNEI DLAQGCPQYW PEEGMLCYGH MQVDCISSSM DCDIISRLFR
     VHNVTRPQEG YLMVRQFQYL GWAGHRDVPA SKRSFLKLIL QVDQWQREVE EEGEGRTIVH
     CLNGGGRSGV FCASSIVCEM SKRQSVVDIF HAVKTLRNSK PNMVDTPEQY RFCYDLALEF
     IESS
//
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