ID M3YGB4_MUSPF Unreviewed; 1298 AA.
AC M3YGB4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=PTPRC {ECO:0000313|Ensembl:ENSMPUP00000010371.1,
GN ECO:0000313|RefSeq:XP_004756284.3};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000010371.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000010371.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004756284.3}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004756284.3};
RG RefSeq;
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};
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DR EMBL; AEYP01041053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01041054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01041055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01041056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01041057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004756284.3; XM_004756227.3.
DR STRING; 9669.ENSMPUP00000010371; -.
DR Ensembl; ENSMPUT00000010538.1; ENSMPUP00000010371.1; ENSMPUG00000010447.1.
DR KEGG; mpuf:101681059; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000159457; -.
DR HOGENOM; CLU_001645_2_1_1; -.
DR OMA; ISANKPC; -.
DR OrthoDB; 2875525at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0032059; C:bleb; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0030507; F:spectrin binding; IEA:Ensembl.
DR GO; GO:0046633; P:alpha-beta T cell proliferation; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048539; P:bone marrow development; IEA:Ensembl.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IEA:Ensembl.
DR GO; GO:0044770; P:cell cycle phase transition; IEA:Ensembl.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0016311; P:dephosphorylation; IEA:Ensembl.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0042492; P:gamma-delta T cell differentiation; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IEA:Ensembl.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
DR GO; GO:0044855; P:plasma membrane raft distribution; IEA:Ensembl.
DR GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IEA:Ensembl.
DR GO; GO:0050857; P:positive regulation of antigen receptor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0060369; P:positive regulation of Fc receptor mediated stimulatory signaling pathway; IEA:Ensembl.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IEA:Ensembl.
DR GO; GO:2000473; P:positive regulation of hematopoietic stem cell migration; IEA:Ensembl.
DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0045059; P:positive thymic T cell selection; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0032677; P:regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0048864; P:stem cell development; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR CDD; cd00063; FN3; 2.
DR CDD; cd14558; R-PTP-C-2; 1.
DR CDD; cd14557; R-PTPc-C-1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR024739; PTP_recept_N.
DR InterPro; IPR016335; Ptprc.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR19134:SF539; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE C; 1.
DR Pfam; PF12567; CD45; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF12453; PTP_N; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Receptor {ECO:0000313|RefSeq:XP_004756284.3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
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|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1298
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041158432"
FT TRANSMEM 572..595
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 389..478
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 479..569
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 646..905
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 825..896
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 937..1220
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1128..1211
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 31..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1298 AA; 146462 MW; 5835A06EE7590976 CRC64;
MTMYLWLKLW AFAFAFLDAG VFVTGEDLSS STGLKLTEEP SALTSGDPFP ARTTAFSHPS
ISERENNSSE TTPLPSNPDS TPTERSWSHL DNNTVAVTGV TQPPLHPTHA VLQTSSAGSD
TQTPSSAAAL SPLTRALGGN DTSGSPGERT TTSIFHVDPT FTQVATLSPA HSSSAALPSR
ISSTTANDNS SDVSLTSTSP ATSTNPTTAP TTIVPATSKP ACDEKYKNIS VEYHYKENKS
FEAQLNANND SVSCENVTCE NNMIYNLTEC SHASFTISHE SCVGPNKILT LEVPPDPKRF
SLEDCTKEEN ADTSLHLKVK IQNNFTCDKN KITYRFQCEN CTPSTGEEIY CEGFLPQRKY
YCDLQASYDG HKFLFLNKII ETDLGRPGSP RNFNCSDKSA TSILLTWKPP TDTFHNYTLC
YKNTECINLD KTKTQYRLSD LVPYEVYKIS LNAYATGKVQ RNGIPVETVC RTAETAPDPV
NNLQALLKTD NSIIVTCKPP TRYNGPSNGY YFLKVKPGGG DVKENRSKSC NFSVEDLQYS
TTYEFEVYYN NGHFEGPVER VSRSTSYNSR ALITFLVFLI IVTFLALLVV LYKIYDLRSK
RSSNMEEEVI LVERDDEKQL MSVEPIHADI LLETYKRKIA DEGRLFLAEF QSIPRVFSKF
SIKDARKPFN QNKNRYVDIL PYDYNRVELS DINGDAGSNY INASYIDGFK EPRKYIAAQG
PRDETVDDFW RMIWEQKATV IVMVTRCEEG NRNKCAEYWP SMEEGTRAFG DVIVKITEYK
RCPDYIIQKL NITNKKEKAT GREVTHIQFT SWPDHGVPED PHLLLKLRRR VNAFSNFFSG
PIVVHCSAGV GRTGTYIGID AMLEGLEAEN KVDVYGYVVK LRRQRCLMVQ VEAQYILIHQ
ALVEYNQFGE TEVSLSELHP YLFNMKKRDP PSEPSPLEAE FQRLPSYRSW RTQHIGNQEQ
NKSKNRNSYI IPYDFNRVPL KHELEMSKES EHDSDESSDD DSDSEETSRY INASFVMSYW
KPEVMIAAQG PLKETIGDFW QMVFQRKVRV IVMLTQLKNG DQEACAQYWE EEKQTYGDIQ
VDMKDTKESP AYTLRVFELR HSKRKDSRTV YQYQYNNWNV TELPAEPKEL ISMIQTLKEN
LPKNSPEGNK HHKSAPLLIH CRDGSQQTGL FCALLNLLES AETEEVIDVF QVVKSLRRAR
PGMVPTLEQY QFLYDVIAST YPAQNGQIKK SNNQEDKIEF DNELDNAKQG ANCVGSTGAL
DKANEGNKED EGIKVTNGPE EPEHSANGPP SPGLTQSA
//
