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Database: UniProt
Entry: M4AT93_XIPMA
LinkDB: M4AT93_XIPMA
Original site: M4AT93_XIPMA 
ID   M4AT93_XIPMA            Unreviewed;      1455 AA.
AC   M4AT93;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 70.
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:ENSXMAP00000017688.2};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000017688.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000017688.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000017688.2};
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   -!- 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   STRING; 8083.ENSXMAP00000017688; -.
DR   Ensembl; ENSXMAT00000017713.2; ENSXMAP00000017688.2; ENSXMAG00000017572.2.
DR   eggNOG; KOG4228; Eukaryota.
DR   GeneTree; ENSGT00940000156249; -.
DR   HOGENOM; CLU_001645_0_0_1; -.
DR   InParanoid; M4AT93; -.
DR   OMA; RIATKXK; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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   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:SF11; PROTEIN-TYROSINE-PHOSPHATASE; 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; 2.
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; 2.
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, ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1455
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017223854"
FT   TRANSMEM        746..767
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..188
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          190..275
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          288..383
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          485..589
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          903..1157
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1077..1148
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1189..1451
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1365..1442
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
SQ   SEQUENCE   1455 AA;  163717 MW;  A8D9D3FF67B0DE6A CRC64;
     MDTLFSVFLG VVILCSRVGS VSAQLPTGSC TFDEGFSQCD YQQDPYDDFD WTHINTQEVP
     YVSPDLPQGS YMFVDVSQYD VGEKARFQLP VMKENDTHCI DFNYLLTSPD GSSPGTLNIL
     VKVNKGPLAN PIWNVTSYTG KGWLKAELAV STFWPNEYQV IFEAEVSDSK AGYIAIDDIQ
     VLSYPCDKSP HFLRLGDVEV NAGQNATFQC IATGRDTSSN KLWLQRRNGE DIPVAQTKNI
     NHRRFAASFH LKEVTNQDQD LYRCVTQSER GSGVSNFAGL IVREPPHPIA PPQLLGVGPT
     YLLIQLNANS IFGDGPIILK EVEYRMTSGT WTETHAVNSP NYKLWHLDPD TEYEIRVLLT
     RPGEGGTGKS GPPLITRTKC AEPMRTPKRL KIAETRARLI AVDWESLGYN ITRCHTFNVT
     ICYHYMTADN HSKADCLDMD PKAPRHLVGS LPPYTNVSLK MILTNPEGRK ESDETIIQTD
     EDVPGPVPSQ SLRATPSEET IILYWKEPAE PNGVITQYEI NYSGVRSFDP SVPLQRPGLM
     VSLPSNATHY TFAQLHPGVT YQLSIRASTS KGFGPASTLN VTTNISAPTI DEYDVSEAFL
     NETATTITVL LKPAQAKGAP ISAYQIVVEE VNPQRSRRQA SSDCYEVPVS YHSASSGGSP
     YYYAAQLSPS NLPEPLPFTV GDNKTYQGFW NPPLAPRKNY NIYLQAVSST ERETKTQCLR
     LAAKRATEEP EVIPDPAKQT DRVVKIAGIS AGVLVLILLV LVAILLLKKR RTYYSYSYYL
     KLAKKRKDAI GTTRQEMTHM VNAMDRSYAD QSTLHGEDPM AVTFMDSHNY NNRLPNDPLV
     PTAVLDENHS ASAAENSRLL DVPRYHCEGT ESPYQTGQLH PAIRVADLLQ HINLMKTSDS
     YGFKEEYESF FEGQSATWDV AKKEQNRTKN RYGNIIAYDH SRVILQPIED DPSSDYINAN
     YIDGYQRPSH YIATQGPVHE TVYDFWRMVW QEQSACIVMV TNLVEVGRVK CYKYWPDDAE
     VYGDFKVTFV EVEPLAEYVV RTFTLERRGF NEVREVKQFH FTGWPDHGVP YHATGLLSFI
     RRVKMSNPPS AGPIVVHCSA GAGRTGCFIV IDIMLDMAER EGVVDIYNCV KALRSRRINM
     VQTEEQYIFI HDAILEACLC GETAIPVCEF KAAYYELIRI DSQTNSSHLK DEFQTLNSVT
     PQPQPEDCSI ALLPRNQDKN RFMDGLPPDR CLPFLITIDG ESSNYINAAL MDSYRQPAAF
     IVTQHPLPST VKDFWRLVYD YGCTSLVMLN EIDLAQGCPQ YWPEEGMLRY GPVQVECMSC
     SMDCDIISRL FRVCNLTRPQ EGYLMVRQFQ YLGWAGHRDV PASKRSFLKL ILQVDQWQRE
     GEEGEGRTIV HCLNGGGRSG VFCASSIVCE MAKRQNVVDV FHAVKTLRNS KPNMVDTPEQ
     YRFCYDLALE FIESS
//
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