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Database: UniProt
Entry: A0A3B3TZ57_9TELE
LinkDB: A0A3B3TZ57_9TELE
Original site: A0A3B3TZ57_9TELE 
ID   A0A3B3TZ57_9TELE        Unreviewed;      1356 AA.
AC   A0A3B3TZ57;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000005913.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000005913.1}
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2B subfamily. {ECO:0000256|ARBA:ARBA00006396}.
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DR   Ensembl; ENSPLAT00000007133.1; ENSPLAP00000005913.1; ENSPLAG00000008044.1.
DR   GeneTree; ENSGT00940000157151; -.
DR   Proteomes; UP000261500; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd14632; R-PTPc-U-1; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
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; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013151; Immunoglobulin.
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; PTHR24051:SF10; PROTEIN-TYROSINE-PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF00047; ig; 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; SM00409; IG; 1.
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   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 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   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};
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};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          1..117
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          119..210
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          217..312
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          315..416
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          422..523
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          836..1067
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          987..1058
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1099..1348
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1278..1353
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
SQ   SEQUENCE   1356 AA;  152485 MW;  A4AF2132378ACA70 CRC64;
     MLVNSSQHAA GHRAQLLLQT LSENDTHCVQ FSYFLYSRDG HSPGALRVYV RVNGGPLGSP
     VWNTSGSHGK QWHQVELAVS TFWPSEYQVL IEATVSRERR GYIALDDILV LNYPCYKAPH
     FSRLGDEEVN AGQNATFQCV AAGRASEAEK FLLERHNGDI LTAASVKHLS HRRFVVSFQL
     DSVQRSDQDL YRCVTQSSRG SGVSNFAELV VKVPPSPIAP PQLLRAGSTY LIIQLNTNSI
     LGDGPIIRKE IEYRASQSPW SEVHGVNMVT YKLWHLDPDT EYHISVLLTR PGEGGTGPPG
     PPLVSRTKCA EPMRPLRGLV ATDIQSRQLS LQWENLAFNL TRCHTYSVSL CYRYTMAGGG
     GGHNTTIREC LAVEHNASRF TLRDLPPYHG VHVRLSLANP EGKKESREVS FQTEEDIPGG
     IAPESLTFTP LDDMIFLKWE EPVEPNGLIT QYEISYQSTE SSDPGINVPG PRRTVSKLKN
     ETYHMFSNLH PGTTYLISVR ARTAKGFGQT ALTEITTNIS APTFDYGDMP SPLGETDHTI
     TVVLRPAQGR GAPVSTYQVV VEEETVKKVK RELGLQECFP LPMSHGEAQA RGTPHYYTAE
     LPPSSLPEAF TVGDNHTYNG YWNTPLDPRK SYLVYFQAMS NFKGESRINC IRIARKVACK
     DHQRALEVSQ HSEEMGLILG VCVGGLVILI LLLGAVIIII KKGRDHYSYY PKPVNKTPIT
     YRQEKSHMGS LERSFTDQST LQEDERMALS FMDAHTCGTR SDARSSVNEA SSLLGGSPRH
     QCGRKGSPYH TGQLHPAVRV ADLLQHINQM KTAEGYGFKQ EYESFFDGWD CTKKKDKTKG
     RHDTLLGYDR HRVKLHPLLG DPNSDYINAN YIDGYHRSNH FIATQGPKQE TLYDFWRMVW
     QENCFSIVMI TKLVEVGRVK CCKYWPDDSE MYGDIKISLL KTETLAEYTV RTFALERRGY
     STKHEVRQFH FTSWPEHGVP YHATGLLAFI RRVKASTPPD AGPVVVHCSA GAGRTGCYIV
     LDVMLDMAEC EGVVDIYNCV KTLCSRRINM IQTEEQYIFI HDAILEACLC GETAILVNEF
     AVTYKEMLRV DSQSNSSPLR EEFQTLNSVT PHLDVEECSI ALLPRNREKN RSMDVLPPDR
     ALAFLVTTEG ESNNYINAAL ADSFHRQAAF IVTPHPLPGT TADFWRLVFD YGCTAVVMLN
     QLNQSNSAWP CVQYWPEPGL QQYGPMEVEF LSMSADEDVI TRLFRVKNVT RLQEGQLVVC
     QFQFLRWSAY RDVPDSKKAF LNLLAQVHKW QRECGEGRTV VHCLNGGGRS GTFCACNILL
     EMIQYQNMVD VFYSVKTLRN CKPNMVESLV KIKNKK
//
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