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Database: UniProt
Entry: A0A3B5BIN7_9TELE
LinkDB: A0A3B5BIN7_9TELE
Original site: A0A3B5BIN7_9TELE 
ID   A0A3B5BIN7_9TELE        Unreviewed;      1349 AA.
AC   A0A3B5BIN7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRD {ECO:0000313|Ensembl:ENSSPAP00000031174.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000031174.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000031174.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR   Ensembl; ENSSPAT00000031674.1; ENSSPAP00000031174.1; ENSSPAG00000023367.1.
DR   GeneTree; ENSGT00940000153617; -.
DR   Proteomes; UP000261400; Unplaced.
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; 4.
DR   CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR   CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
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; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
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; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF8; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE S; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
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; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 2.
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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        703..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..86
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          94..176
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          183..273
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          278..374
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          376..455
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          457..543
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          794..1049
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          969..1040
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1081..1340
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1258..1331
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          263..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1349 AA;  152254 MW;  7355D168977C4C6F CRC64;
     MGPQLKVVER TRTATMLCAA SGNPDPDISW FKDFLPVNTT NNNGRIKQLR SGALQIEQSE
     ESDQGKYECV ATNNDGTRYS APANLYVRVR RVPPRFSIPP TDNEIMPGGS VNITCVAVGS
     PMPYVKWMLG AEDLTPEDDM PIGRNVLELT DVRQSANYTC VAMSTLGVIE AVAQITVKAL
     PKAPGIPVVT ERTATSITLT WDSGNPEPVS YYIIQHKSKY SEDLYKEIDG VATTRYSVGG
     LSPYSDYEFR VVAVNNIGRG PPSESIEAKT AEQAPSTAPR QVRGHMMSAT TAVIQWDEPE
     EANGQIMGYR VYYTMDSAQH VNLWEKQIVR GSNFVTIQGL IPNKTYYIKV LAYTSVGDGP
     LSPDLQIIAK TGVPSQPTDF KGEAKSETSI LLSWVAPADT NNLSSPQKRI SFEPTTTYLL
     KDLKPFTTYT FRLAARSKHG VGAYTSEISA ETPQTLFAKN FHVRAAMKTS VLLTWEIPDT
     YNPAQPFTIL YDNGQSVEVD GKLTQKLITG LQPETQYSFL LTNRGNSAGG LQHRVSTMTA
     PDILRTKPYL ISKTNSDGMV TVELPTVQTS ERVRGYYIVV VPLKKQRTGK FFKPWDNPDE
     MNLEELLKEI NRTSRGLRFQ RQAEPRAYIA AYYKDLPKDF TLGDGKMYGD FENKQLETGL
     EYIFFVLAVL EMSENIMYAT SPYSDPVVSA GIPPQPVIDE EEGLIWVVGP VLAVVFIICI
     VIAILLYKRK RAESEARKGS LPNSKEMPLH HPTDPVELRR LNFQTPGMAS HPPIPVMDLA
     DHLERLKAND NLKFSQEYES IDPGQQFTWE HSNLEVNKPK NRYANVIAYD HSRVLLSAID
     GIPGSDYINA NYIDGYRKQN AYIATQGSLP ETFGEFWRMI WEQRSAIVVM MTKLEERSRV
     KCDQYWPTRG TETYGLIQVT LLDTVELATY CVRTFALFKN GSSEKREVRQ FQFTAWPDHG
     VPEHPTPFLA FLRRVKACNP PDAGPMVVHC SAGVGRTGCF IVIDAMLERI KHEKTVDIYG
     HVTLMRAQRN YMVQTEDQYV FIHDALQEAV NCGTTEVPAR NLYAYIQKLT QIEGGENVTG
     MELEFKRLAN TKAHTSRFIS ANLPCNKFKN RLVNIMPYES TRVCLQPIRG VEGSDYINAS
     FIDGYRQQKA YIATQGPLAE TTEDFWRMLW EHNSTIVVML TKLREMGREK CHQYWPAERS
     ARYQYFVVDP MAEYNMPQYI LREFKVTDAR DGQSRTVRQF QFTDWPEQGV PKSGEGFIDF
     IGQVHKTKEQ FGQDGPISVH CSAGVGRTGV FITLSIVLER MRYEGVVDIF QTVKMLRTQR
     PAMVQTEDQY QFCYRAGLEY LGSFDHYAT
//
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