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Database: UniProt
Entry: A0A3Q1G2A2_9TELE
LinkDB: A0A3Q1G2A2_9TELE
Original site: A0A3Q1G2A2_9TELE 
ID   A0A3Q1G2A2_9TELE        Unreviewed;      1530 AA.
AC   A0A3Q1G2A2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000021947.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000021947.1}
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 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR   Ensembl; ENSAPOT00000015069.1; ENSAPOP00000021947.1; ENSAPOG00000002897.1.
DR   GeneTree; ENSGT00940000153617; -.
DR   Proteomes; UP000257200; 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; 7.
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; 2.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
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; 3.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 3.
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   Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1530
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018762022"
FT   TRANSMEM        869..892
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..121
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          133..228
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          240..322
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          329..419
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          424..520
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          522..616
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          618..702
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          977..1240
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1160..1231
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1272..1521
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1449..1522
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          903..922
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1530 AA;  171635 MW;  A9DE16E55722FD08 CRC64;
     MHVSTYPRMN SASPGLLLLS FLFLADADSP PRFTRTPEDQ TGVQGGVASF VCQASGEPQP
     KIVWNKKGKK VSNQRFEVIE FDDGSGSVLR IQPLRTPRDE AIYECHASNS AGEITASTRL
     SVLREDQLPS GFPTIDMGPQ LKVVERSRTA TMLCAASGNP DPEITWFKDF LPVNTSNNNG
     RIKQLRSGGT PIRGALQIEM SEESDQGKYE CVATNSDGTR YSTPANLYVR ELREVRRVPP
     RFSIPPADSE IMPGGNVNIT CVAVGSPMPY VKWMLGAEDL TPEDDMPIGR NVLELTDVRQ
     SNNYTCVAMS TLGVIEAVAQ IIVKALPKAP GTPVVTERTA TSITLTWDSG NPEPVSYYII
     QHRAKGSEDP YKEIDGIATT RYSVGGLSPY SHYDFRVAAV NTIGQGPSSD VVEARTAEQA
     PSSPPRQVIG RMLSATTAMI HWDEPEEPNG QVVGYRVYYT SDNTLPVNQW EKQMVRSANF
     ITIQDLTPNK TYYIRVLAFT SVGDGPLSQD LQIIAKTGVP SQPSEFKGEA KSETSILLSW
     VAPTPQGGPD NQITGYELVY RRADDSEEKK VTFEPTASYL LKNLKPFSTY TFQLAAKSKN
     GIGAYTNEVS IDTPQTLFAT NFRVKAAMKN SVLLSWEIRD KNPAQPFTIL YGKGQSVEVD
     GKQTQKLITG LEPDTQYSFL LTNRANSAGG LQHRVTATTA PDILKTKPTV VGKTNADGMV
     TVQLPTVQTT AKVRGYYVVV VPLKKQRGGK FLNPWEEPDQ MNLDELLKEI NRTSISRALR
     IRRQAGQSDP RAYVTAHFKT LPMEFTLGDG RNYGDFRNRP LQNGQEYVFF VLALLDLSEN
     TMYATSPYSD PVTSSDVDPQ PIVDEEEGLL WVVGPVLAVI FIVCIVIAIL LFKSKPDRKR
     AEAEGRKGSF PCSKAMSSHH PTDPVELRRI NFQTPAYRVS VYRGYRRLSS MASHPPIPIS
     ELADHIERLK ANDNLKFSQE YESVDPGQQF TWENSNLEVN KPKNRYANVI AYDHSRVILS
     SIEGVPGSDY INANYIDGYR RQNAYIATQG SLPETFGDFW RMVWEQHTAN IIMMTKLEEK
     SRMPSYFFSK VKCDQYWPTR GTETYGLIQV TLLDTVELAT YSVRTLALYK SGSNEKREVR
     HFQFTAWPDH GVPEHPTPFL AFLRRVKACN PPDAGPMVVH CSAGVGRTGC FIVIDAMTER
     IKHEKTIDIY GHVTLMRSQR NYMVQTEDQY IFIHDALLEA VTCGNTEVPA RNLYSYIQRL
     TQIEPGENVT GMELEFKRLA SAKAHTSRFV SANLPCNKFK NRLVNIMPYE TTRVCLQPIR
     GVEGSDYINA SFIDGYRQQK AYIATQGPLA ETTEDYWRML WEHNSTIVVM LTKLREMGRE
     KCHQYWPAER SARYQYFVVD PMAEYNMPQY ILREFKVTDA RDGQSRTVRQ FQFTDWPEQG
     VPKSGEGFID FIGQVHKTKE QFGQDGPITV HCSAGVGRTG VFITLSIVLE RMRYEGVVDI
     FQTVKMLRTQ RPATVQTEVN FAPVVFLSRF
//
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