ID U3JJ93_FICAL Unreviewed; 1119 AA.
AC U3JJ93;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 74.
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:ENSFALP00000002847.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000002847.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000002847.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000002847.2}
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};
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DR AlphaFoldDB; U3JJ93; -.
DR STRING; 59894.ENSFALP00000002847; -.
DR Ensembl; ENSFALT00000002859.2; ENSFALP00000002847.2; ENSFALG00000002725.2.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000159457; -.
DR HOGENOM; CLU_001645_2_1_1; -.
DR OrthoDB; 2875525at2759; -.
DR Proteomes; UP000016665; Chromosome 8.
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; 1.
DR CDD; cd14558; R-PTP-C-2; 1.
DR CDD; cd14557; R-PTPc-C-1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; 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; PF00041; fn3; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000016665};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1119
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032726367"
FT TRANSMEM 391..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..300
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 467..726
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 646..717
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 758..1042
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 949..1033
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 769..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 126355 MW; 1F6DF299AA1A5FCC CRC64;
MFLWLKLLAF GVAFLGQDAL LKGQETSTTG PEDTTVIPEA DCGIFGDIED STTNSDMAVV
SLNFPAKDGR EYVILGGDKN ITVSSVNTSV ELPKCQVYTV EVKIGECSEK TSFQVPKDVN
KPFQVKDITN TSAKFCWNHS LTCANVSVAC NGFQNNFKKL GNVTCGVLEV LLPHHQYNCT
AYMYFNGRNV ASQSFDIETD YGVPEAPRNI KETHKNTTSV TVEWTKPNDI SKGPIDGYFV
NFTVGDKSVC WENISTTVYT CSGFDPYTTG SVYVSAYTIN KRNDTLESKT ENYIFTTEEG
VPEKVENVKV ALTADNAVQI TCRKQRVFGP KAIFYLIWEN DEKPEKKDKC EFKKENLLYL
TNYAFKIFVS NGKHNGTAVV ESIKTRYNSR ALIIFLAFLI IVTVIALLLV LYKIYDLHKK
KLSSSSGGVS LVAVKDDDKQ LLNIDPIPSE LLLDTYKRKI ADEGRLFLEE FQSIPRVFSK
FSIKEAKKSY NQNKNRYIDI LPYDHNRVEL SEMPGDPGSD YINASYIDGF KEPRKYIAAQ
GPKDETTDDF WRMIWEQKAT IIVMVTRCEE GKRNKCAQYW PSMENGTATY GDIIVKIHES
KTCPDYVIQK LHITNGRERT AGRDVTHIQF TGWPDHGVPE DPHLLLKLRR RVNALSNFFS
GPIVVHCSAG VGRTGTYIGI DAMLEGLDAE GRVDVYGYIV KLRRQRCLMV QVESQYILIH
QALVEYNQYG ETEISLSELH SSLNNLKRKD HPSDSSLLEA EFQRLPSYKG WRTQNTGNRE
ENKSKNRNAN VIPYDFNRVP IRHEEDCGKE GEHDSDESSD EDSDCEESSR YINASFITGY
WGPKAMIATQ GPLQETISDF WQMVFQRKVK VVVMLTELKE GDEELCAQYW GEGKQTYDGI
EVQMADVNSG PSYTIRAFDI AHLKTKETQK VYQYQYHKWS GCDVPEVPKD LVSMILNIKQ
KLPARPVSED NRRTRSVPLL VHCCDGSQQT GVFCALMTLL ESAEIEEVID VFQVVKSLRR
TRLGMVSTFE QYQFLYDTIA STYPAQNGQI KKNSQQEDKV EFCSEVGKSD QETDLITTDL
APPRPGEIEP PEICDDSKAA DGTKETESST NGPTTAVLT
//
