ID A0A3B5PW74_XIPMA Unreviewed; 1440 AA.
AC A0A3B5PW74;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
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:ENSXMAP00000022822.1, 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:ENSXMAP00000022822.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000022822.1};
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 Ensembl; ENSXMAT00000025017.1; ENSXMAP00000022822.1; ENSXMAG00000026721.1.
DR GeneTree; ENSGT00940000157151; -.
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 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; 4.
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; PS00740; MAM_1; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1440
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017413371"
FT TRANSMEM 750..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..190
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 192..283
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 290..385
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 388..489
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 495..596
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 901..1138
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1058..1129
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1170..1433
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1349..1424
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 825..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1440 AA; 162088 MW; C0915507AE681B0A CRC64;
MYTMNTCAFL LILSVQIYAD GIEGPTAAGC TFEEDSDPNL CDFTQGEDDD FDWMLFRTYN
SPSASSDLLR GSYMLVNSSQ HAAGHRAQLL LQTLSENDTH CVQFSYFLYS RDGHSPGALR
VYVRVNGGPL GSPVWNTSGS HGKQWHQVEL AVSTFWPSEY QVLIEATVSR ERRGYIALDD
IMVLNYPCYK APHFSRLGDE EVNAGQNATF QCVAAGRASE AEKFLLERHN GDILTAASVK
HLSHRRFVVS FQLDSVQRSD QDLYRCVTQS SRGSGVSNFA ELVVKVPPSP IAPPQLLRAG
STYLIIQLNT NSILGDGPII RKEIEYRASQ SPWSEVHGVN MVTYKLWHLD PDTEYHISVL
LTRPGEGGTG PPGPPLVSRT KCAEPMRPLR GLVATDIQSR QLSLQWENLA FNLTRCHTYS
VSLCYRYTMA GGGGGHNTTV RECLAVEHNA SRFTLRDLPP YHSVHVRLSL ANPEGKKESR
EVSFQTEEDI PGGIAPESLT FTPLDDMIFL KWEEPVEPNG LITQYEISYQ SIESSDPGIN
VPGPRRTVSK LKNETYHMFS NLHPGTTYLI SVRARTAKGF GQTALTEITT NISAPTFDYG
DMPSPLSETD HTITVVLRPA QGRGAPVSTY QVVVEEETVK KVKRELGLQE CFPLPMSHGE
AQARGTPHYY TAELPPSSLP EAFTVGDNHT YNGYWNTPLD PRKSYLVYFQ AMSNFKGESR
INCIRIARKA ACKDHQRALE VSQHSEEMGL ILGVCAGGLV ILILLLGAVI IIIKKGKPVN
KTPITYRQEK SHMGSLERSF TDQSTLQEDE RMALSFMDAH TCGTRSDARS SVNEASSLLG
GSPRHQCGRK GSPYHTGQLH PAVRVADLLQ HINQMKTAEG YGFKQEYESF FDGWDCTKKK
DKTKGRHDTL LGYDRHRVKL HPLLGDPNSD YINANYIDIR INREGYHRSN HFIATQGPKQ
ETLYDFWRMV WQENCFSIVM ITKLVEVGRV KCCKYWPDDS EMYGDIKITL LKTETLAEYT
VRTFALERRG YSTKHEVRQF HFTSWPEHGV PYHATGLLAF IRRVKASTPP DAGPVVVHCS
AGAGRTGCYI VLDVMLDMAE CEGVVDIYNC VKTLCSRRIN MIQTEEQYIF IHDAILEACL
CGETAILVNE FAVTYKEMLR VDSQSNSSPL REEFQTLNSV TPHLDVEECS IALLPRNREK
NRSMDVLPPD RALAFLVTTE GESNNYINAA LADSFHRQAA FIVTPHPLPG TTADFWRLVF
DYGCTAVVML NQLNQSNSAW PCVQYWPEPG LQQYGPMEVE FLSMSADEDV ITRLFRVKNV
TRLQEGQLVV CQFQFLRWSA YRDVPDSKKA FLNLLAQVHK WQRECGEGRT VVHCLNGGGR
SGTFCACNIL LEMIQYQNMV DVFYSVKTLR NCKPNMVESL DQYRFCYDLV LEYLDCFEDR
//
