ID G1PXE7_MYOLU Unreviewed; 1437 AA.
AC G1PXE7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 83.
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:ENSMLUP00000016114.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000016114.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000016114.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000016114.2}
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 EMBL; AAPE02009341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 59463.ENSMLUP00000016114; -.
DR Ensembl; ENSMLUT00000017672.2; ENSMLUP00000016114.2; ENSMLUG00000017668.2.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000155326; -.
DR HOGENOM; CLU_001645_0_0_1; -.
DR InParanoid; G1PXE7; -.
DR OMA; XPMQETV; -.
DR TreeFam; TF312900; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
DR GO; GO:0045294; F:alpha-catenin binding; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
DR GO; GO:0070097; F:delta-catenin binding; IEA:Ensembl.
DR GO; GO:0045295; F:gamma-catenin binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0097677; F:STAT family protein binding; IEA:Ensembl.
DR GO; GO:0016790; F:thiolester hydrolase activity; IEA:Ensembl.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; IEA:Ensembl.
DR GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:1904893; P:negative regulation of receptor signaling pathway via STAT; IEA:Ensembl.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:Ensembl.
DR CDD; cd00063; FN3; 3.
DR CDD; cd06263; MAM; 1.
DR CDD; cd14630; R-PTPc-T-1; 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; 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; 3.
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};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
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 7..168
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 170..261
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 268..361
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 366..460
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 461..567
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 885..1139
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1059..1130
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1171..1433
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1347..1424
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 786..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1437 AA; 161716 MW; 0A88828DB106D25B CRC64;
ISLLFAGGCS FDEHYSNCGY SVALGTNGFT WEQINTWEKP MLDPALAQGS FMMVNSSGRA
SGQKAHLLLP TLKENDTHCI DFHYYFSSRD RSSPGALNVY VKVNGGPQGN PVWNVSGVVT
EGWVKAELAI STFWPHFYQV IFESVSLKGH PGYIAVDEVR VLAHPCRKAP HFLRLQNVEV
NVGQNATFQC IAGGKWSQHD KLWLQQWNGR DTALMVTRVV NHRRFSATVS VADTAQRSVS
KYRCVIRSDG GSGVSNYAEL IVKEPPTPIA PPELLAVGAT YLWIKPNANS IIGDGPIILK
EVEYRTTTGT WAETHIVDSP NYKLWHLDPD VEYEIRVLLT RPGEGGTGPP GPPLTTRTKC
ADPVHGPQNV EIVDIRARQL TLQWEPFGYA VTRCHSYNLT VQYQYVFNQQ QYEAEEVIQT
SSHYTLRGLR PFMTIRLRLL LSNPEGRMES EELVVQTEED VPGAVPLESI QGGPFEEKIY
IQWKPPNETN GVITLYEINY KAVGSLDPSA DLSSQRGKVF KLRNETHHLF VGLYPGTTYS
FTIKASTAKG FGPPVTTRIA TKISAPSMPE YDTDTPLNET DTTITVMLKP AQSRGAPVSV
YQLVVKEERL QKSRRAADII ECFSVPVSYR NASSLDSLHY FAAELKPANL PVTQPFTVGD
NKTYNGYWNP PLSPLKSYSI YFQALSKANG ETKINCVRLA TKAPMGSAQV TPGTPLCLLT
TGASTQNSNT VEPEKQVDNT VKMAGVIAGL LMFIIILLGV MLTIKRRRNA YSYSYYLKLA
KKQKETQSGA QREMGPVAST DKPTTKLSTS RNDEGFSSSS QDVNGFTDGS RGELSQPTLT
IQTHPYRACD PMEMSYPRDQ FQPAIRVADL LQHITQMKRG QGYGFKEEYE ALPEGQTASW
DTAKEDENRN KNRYGNIISY DHSRVRLLVL DGDPHSDYIN ANYIDGYHRP RHYIATQGPM
QETVKDFWRM IWQENSASIV MVTNLVEVGR VKCVRYWPDD TEVYGDIKVT LIETEPLAEY
VIRTFTVQKK GYHEIRELRL FHFTSWPDHG VPCYATGLLG FVRQVKFLNP PEAGPIVVHC
SAGAGRTGCF IAIDTMLDMA ENEGVVDIFN CVRELRAQRV NLVQTEEQYV FVHDAILEAC
LCGNTAIPVC EFRSLYYNIS RLDPQTNSSQ IKDEFQTLNI VTPHVRPEDC SIGLLPRNHD
KNRSMDVLPL DRCLPFLISV DGESSNYINA ALMDSHKQPA AFVVTQHPLP NTVADFWRLV
FDYNCSSVVM LNEMDTAQLC MQYWPEKTSG CYGPIQVEFV SADIDEDIIH RIFRICNMAR
PQDGYRIVQH LQYIGWPAYR DTPPSKRSLL KVVRRLEKWQ EQYDGREGRT VVHCLNGGGR
SGTFCAICSV CEMIQQQNII DVFHIVKTLR NNKSNMVETL EQYKFVYEVA LEYLSSF
//
