ID A0A3Q3ASK1_KRYMA Unreviewed; 1417 AA.
AC A0A3Q3ASK1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=PTPRT {ECO:0000313|Ensembl:ENSKMAP00000019938.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000019938.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000019938.1}
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 -!- 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; ENSKMAT00000020204.1; ENSKMAP00000019938.1; ENSKMAG00000014489.1.
DR GeneTree; ENSGT00940000155326; -.
DR OMA; XPMQETV; -.
DR Proteomes; UP000264800; 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; 3.
DR CDD; cd06263; MAM; 1.
DR CDD; cd14634; R-PTPc-T-2; 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; 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:SF8; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00041; fn3; 2.
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:UP000264800};
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 742..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..185
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 187..278
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 285..378
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 383..477
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 478..583
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 876..1119
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1039..1110
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1151..1413
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1327..1404
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 772..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1417 AA; 158649 MW; 6581BF774ACB43C6 CRC64;
ERPVTDRPRF DLMDLQLPSS LSLGGCTFEE SYSSCGYSVS LGTNGFTWEQ VNSWEKPTMD
PALPTGSFMV VNASGRASGQ KAHLYMPTLK ENDTHCVDFL YSLSSRDGAS PGTLNVYVKV
NGGAQGNPVW NASDTVTEGW VKAELAISTF WPNSYQIIFE AVSVQGHPGF IAVDDIRVLA
HPCRKAPHFL RLQNVEVNVG QNATFQCTAG GKWSQHDKLW LQQWNGRDTA LMVTRVVNHR
RFSATVSVGD TSQRSTSRYR CVIRSDGGSG VSNYAELIVK APPTPIAPPE LLAVGATYLW
IKPNANSIIG DGPIILKEVE YRTTTGNWAE THVVDAPTYK LWHLDPDVEY EIKVLLSRPG
EGGTGPPGPP LTTRTKCADP VHGPQNVNVV DVRARQLTVQ WETFGYAVTR CHSYNLTVQY
QYVFNQQEFA AEELIQTSSH YTLRGLRPFV TVRLRLVLAN PEGSKESEEI VKQTEEDVPG
SVPMESLQNT PYEEKIFMQW KAPNETNGAI TLYEITYKAL SSLDPSADLT TQRGRVFKLK
NETHHLFVGL YPGTTYFFTL KASTNKGFGP PVTTRISTKI AAPMMPEYES ETPLNETETT
ITILLKPAQS RGAPISSYQL VVKEERKSKT RRAASESVEC FSAPVSFRNA SILSSPYYIA
AELPPSGLTV VQPFTVGDNK SYGGFWNPPL SPAKSYSIYF QAMSRANGET KINCVRLAHK
GASTQDSDAM EPEKQVDSTV KMAGVIAGIL MFIIILLGVI LTFKRRKLAK KQKETASSST
QQREMGPVTT ADKSTTKVST LHKDDPFSTS NQDLNGFNSS QPSLAQPSLT LQSFPYGGCE
SVELSYQSGM SFQPAIRVAD LLQHITQMKC GQGYGFKEEY EALAEGQTAP WETAKKDENR
NKNRYGNIIA YDHTRVRLQL LDGDPHSDYI NANYIDVRPM QETVRDFWRM VWQENSASIV
MVTNLVEVGR VKCVRYWPDE TEVYGDIKVT LIETEPLAEY VIRTFTVQKK GHHEIRELRQ
FHFTSWPDHG VPCYATGLLG FIRQVKFLNP PDAGPIVVHC SAGAGRTGCF IAVDIMLDMA
ENEGVVDIFN CIRELRSQRV NMVQTEEQYV FVHDAILEAC LCGNTAIPVC EFRAVYYNIS
RLDPQTNSSQ IKDEFQTLNI VTPRVRPEDC SVGLLPRNHD KNRSMDVLSA DRCLPFLISV
DGESSNYINA ALMDSHKQPA AFIVTQHPLP NTMGDFWRLV FDYNCSSIVM LNEMDAAQLC
MQYWPEKNSC CYGPIQVEFI SADIDEDIIN RIFRICNMAR PQDGYRLVQH FQFIGWPAYR
DTPLSKRSIL QLVRRLAKWQ EQYDGGDGRT VVHCLTGGGR SGTFCAICSI NEMIQQQNIV
DVFHTVKTLR NNKTNMVETM EQYKFCYEVA LEALNSF
//
