ID A0A2K6TX85_SAIBB Unreviewed; 1438 AA.
AC A0A2K6TX85;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:ENSSBOP00000024243.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000024243.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000024243.1}
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 STRING; 39432.ENSSBOP00000024243; -.
DR Ensembl; ENSSBOT00000041103.1; ENSSBOP00000024243.1; ENSSBOG00000028466.1.
DR GeneTree; ENSGT00940000155326; -.
DR Proteomes; UP000233220; Unplaced.
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; 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:UP000233220};
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..128
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 130..221
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 228..321
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 326..420
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 421..527
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 825..1140
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1060..1131
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1172..1434
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1348..1425
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 727..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1438 AA; 161696 MW; 89E5E639513FA456 CRC64;
MLDQAVPTGS 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 TLQWEPFGYT 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
TKGASTQNSN TVEPEKQVDN TVKMAGVIAG LLMFIIILLG VMLTIKRRRN AYSYSYYLKL
AKKQKETQSG AQREMGPVAS ADKPTTKLSA SRNDEGFSSS SQDVNGFNGS HGELSQPTLT
IQTHPYRTCD PVEMSYPRDQ FQPAIRVADL LQHITQMKRG QGYGFKEEYE ALPEGQTASW
DTAKEDENRN KNRYGNIISC RGGSPAKRAA IQKTPQLDKE MSSVFPEAPL IQRRTLAATR
DDHSRVRLLV LDGDPHSDYI NANYIDGYHR PRHYIATQGP MQETVKDFWR MIWQENSASI
VMVTNLVEVG RHPAEHTVGN ATLGRAASPG MVKCVRYWPD DTEVYGDIKV TLIETEPLAE
YVIRTFTVQK KGYHEIRELR LFHFTSWPDH GVPCYATGLL GFVRQVKFLN PPEAGPIVVH
CSAGAGRTGC FIAIDTMLDM AENEGVVDIF NCVRELRAQR VNLVQTEEQY VFVHDAILEA
CLCGNTAIPV CEFRSLYYNI SRLDPQTNSS QIKDEFQTLN IVTPRVRPED CSIGLLPRNH
DKNRSMDVLP LDRCLPFLIS VDGESSNYIN AALMDSHKQP AAFVVTQHPL PNTVADFWRL
VFDYSCSSVV MLNEMDTAQF CMQYWPEKTS GCYGPIQVEF VSADIDEDII HRIFRICNMA
RPQDGYRIVQ HLQYIGWPAY RDTPPSKRSL LKVVRRLEKW QEQYDGREGR TVVHCLNGGG
RSGTFCAVCS VCEMIQQQNI IDVFHIVKTL RNNKSNMVET LEQYKFVYEV ALEYLSSF
//
