PTPRC_MOUSE
ID PTPRC_MOUSE Reviewed; 1293 AA.
AC P06800; E9QLT5; Q61812; Q61813; Q61814; Q61815; Q78EF1; S4R1S4; S4R2V1;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase C {ECO:0000305};
DE EC=3.1.3.48;
DE AltName: Full=Leukocyte common antigen;
DE Short=L-CA;
DE AltName: Full=Lymphocyte antigen 5;
DE Short=Ly-5;
DE AltName: Full=T200;
DE AltName: CD_antigen=CD45;
DE Flags: Precursor;
GN Name=Ptprc {ECO:0000312|MGI:MGI:97810}; Synonyms=Ly-5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=2944116; DOI=10.1073/pnas.83.18.6940;
RA Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.;
RT "Sequences of Ly-5 cDNA: isoform-related diversity of Ly-5 mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6940-6944(1986).
RN [2]
RP ERRATUM OF PUBMED:2944116, AND SEQUENCE REVISION.
RA Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.;
RL Proc. Natl. Acad. Sci. U.S.A. 84:1991-1991(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=1822988; DOI=10.1155/1991/52686;
RA Zebedee S.L., Barritt D.S., Raschke W.C.;
RT "Comparison of mouse Ly5a and Ly5b leucocyte common antigen alleles.";
RL Dev. Immunol. 1:243-254(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-228 (ISOFORM 2).
RX PubMed=3037546; DOI=10.1073/pnas.84.15.5364;
RA Saga Y., Tung J.-S., Shen F.-W.W., Boyse E.A.;
RT "Alternative use of 5' exons in the specification of Ly-5 isoforms
RT distinguishing hematopoietic cell lineages.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5364-5368(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RX PubMed=3211131; DOI=10.1128/mcb.8.11.4889-4895.1988;
RA Saga Y., Tung J.-S., Shen F.-W.W., Pancoast T.C., Boyse E.A.;
RT "Organization of the Ly-5 gene.";
RL Mol. Cell. Biol. 8:4889-4895(1988).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RX PubMed=2522930; DOI=10.1016/s0021-9258(18)83337-3;
RA Johnson N.A., Meyer C.M., Pingel J.T., Thomas M.L.;
RT "Sequence conservation in potential regulatory regions of the mouse and
RT human leukocyte common antigen gene.";
RL J. Biol. Chem. 264:6220-6229(1989).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-265 (ISOFORM 3).
RC TISSUE=T-cell;
RX PubMed=3864163; DOI=10.1073/pnas.82.21.7360;
RA Shen F.-W., Saga Y., Litman G., Freeman G., Tung J.-S., Cantor H.,
RA Boyse E.A.;
RT "Cloning of Ly-5 cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7360-7363(1985).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-75.
RX PubMed=3417340; DOI=10.1007/bf00345505;
RA Tung J.-S., Saga Y., Boyse E.A.;
RT "Structural features of Ly-5 glycoproteins of the mouse and counterparts in
RT other mammals.";
RL Immunogenetics 28:271-277(1988).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 732-840.
RX PubMed=1932742;
RA Yi T., Cleveland J.L., Ihle J.N.;
RT "Identification of novel protein tyrosine phosphatases of hematopoietic
RT cells by polymerase chain reaction amplification.";
RL Blood 78:2222-2228(1991).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 966-1293.
RX PubMed=2948186; DOI=10.1073/pnas.84.1.161;
RA Raschke W.C.;
RT "Cloned murine T200 (Ly-5) cDNA reveals multiple transcripts within B- and
RT T-lymphocyte lineages.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:161-165(1987).
RN [13]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=3570377; DOI=10.1007/bf00404697;
RA Gonez L.J., Walker I.D., Sandrin M.S., McKenzie I.F.;
RT "High sequence conservation between rat (T200) and mouse (Ly-5) leukocyte
RT common antigens.";
RL Immunogenetics 25:263-266(1987).
RN [14]
RP INTERACTION WITH GANAB AND PRKCSH.
RX PubMed=9148925; DOI=10.1074/jbc.272.20.13117;
RA Arendt C.W., Ostergaard H.L.;
RT "Identification of the CD45-associated 116-kDa and 80-kDa proteins as the
RT alpha- and beta-subunits of alpha-glucosidase II.";
RL J. Biol. Chem. 272:13117-13125(1997).
RN [15]
RP FUNCTION.
RX PubMed=10415030;
RA Katagiri T., Ogimoto M., Hasegawa K., Arimura Y., Mitomo K., Okada M.,
RA Clark M.R., Mizuno K., Yakura H.;
RT "CD45 negatively regulates lyn activity by dephosphorylating both positive
RT and negative regulatory tyrosine residues in immature B cells.";
RL J. Immunol. 163:1321-1326(1999).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964; SER-994; THR-1267 AND
RP SER-1286, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Protein tyrosine-protein phosphatase required for T-cell
CC activation through the antigen receptor. Acts as a positive regulator
CC of T-cell coactivation upon binding to DPP4. The first PTPase domain
CC has enzymatic activity, while the second one seems to affect the
CC substrate specificity of the first one. Upon T-cell activation,
CC recruits and dephosphorylates SKAP1 and FYN (By similarity).
CC Dephosphorylates LYN, and thereby modulates LYN activity. {ECO:0000250,
CC ECO:0000269|PubMed:10415030}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Interacts with SKAP1. Interacts with DPP4; the interaction is
CC enhanced in an interleukin-12-dependent manner in activated lymphocytes
CC (By similarity). Binds GANAB and PRKCSH. {ECO:0000250,
CC ECO:0000269|PubMed:9148925}.
CC -!- INTERACTION:
CC P06800; P06240: Lck; NbExp=2; IntAct=EBI-1672, EBI-1401;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08575};
CC Single-pass type I membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000250|UniProtKB:P08575}. Note=Colocalized with DPP4 in membrane
CC rafts. {ECO:0000250|UniProtKB:P08575}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P06800-4; Sequence=Displayed;
CC Name=2;
CC IsoId=P06800-5; Sequence=VSP_059411;
CC Name=3;
CC IsoId=P06800-6; Sequence=VSP_059410;
CC -!- DEVELOPMENTAL STAGE: Expression is restricted to the hematopoietic
CC compartment of development.
CC -!- DOMAIN: The first PTPase domain interacts with SKAP1. {ECO:0000250}.
CC -!- PTM: Heavily N- and O-glycosylated.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 1/6 subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39458.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA39459.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA40161.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA40161.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=AAA60449.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB46374.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M14342; AAA39458.1; ALT_INIT; mRNA.
DR EMBL; M92933; AAA39459.1; ALT_INIT; mRNA.
DR EMBL; AC122903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466520; EDL39542.1; -; Genomic_DNA.
DR EMBL; M17320; AAA60449.1; ALT_INIT; mRNA.
DR EMBL; M23354; AAA39462.1; -; Genomic_DNA.
DR EMBL; M22456; AAB46374.1; ALT_INIT; Genomic_DNA.
DR EMBL; M11934; AAA39461.1; -; mRNA.
DR EMBL; M23241; AAA39460.1; -; Genomic_DNA.
DR EMBL; M15174; AAA40161.1; ALT_SEQ; mRNA.
DR CCDS; CCDS15330.2; -. [P06800-6]
DR CCDS; CCDS48383.2; -. [P06800-4]
DR PIR; A23329; A23329.
DR PIR; A28334; A28334.
DR PIR; A28335; A28335.
DR PIR; I57644; I57644.
DR RefSeq; NP_001104786.2; NM_001111316.2. [P06800-4]
DR RefSeq; NP_035340.3; NM_011210.4. [P06800-6]
DR RefSeq; XP_006529320.1; XM_006529257.1. [P06800-4]
DR RefSeq; XP_006529321.1; XM_006529258.3. [P06800-4]
DR RefSeq; XP_006529322.1; XM_006529259.3. [P06800-4]
DR RefSeq; XP_006529323.1; XM_006529260.1. [P06800-5]
DR AlphaFoldDB; P06800; -.
DR SMR; P06800; -.
DR IntAct; P06800; 12.
DR MINT; P06800; -.
DR STRING; 10090.ENSMUSP00000138350; -.
DR GlyConnect; 2666; 1 N-Linked glycan (1 site).
DR GlyGen; P06800; 16 sites.
DR iPTMnet; P06800; -.
DR PhosphoSitePlus; P06800; -.
DR SwissPalm; P06800; -.
DR EPD; P06800; -.
DR jPOST; P06800; -.
DR MaxQB; P06800; -.
DR PaxDb; P06800; -.
DR PeptideAtlas; P06800; -.
DR PRIDE; P06800; -.
DR ProteomicsDB; 301943; -. [P06800-4]
DR ProteomicsDB; 314731; -.
DR ProteomicsDB; 337221; -.
DR ABCD; P06800; 2 sequenced antibodies.
DR Antibodypedia; 737; 9482 antibodies from 54 providers.
DR DNASU; 19264; -.
DR Ensembl; ENSMUST00000182283; ENSMUSP00000138800; ENSMUSG00000026395. [P06800-6]
DR Ensembl; ENSMUST00000183301; ENSMUSP00000138350; ENSMUSG00000026395. [P06800-4]
DR GeneID; 19264; -.
DR KEGG; mmu:19264; -.
DR UCSC; uc007cvf.3; mouse. [P06800-4]
DR UCSC; uc007cvh.3; mouse.
DR CTD; 5788; -.
DR MGI; MGI:97810; Ptprc.
DR VEuPathDB; HostDB:ENSMUSG00000026395; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000159457; -.
DR InParanoid; P06800; -.
DR OMA; IFRKCFH; -.
DR TreeFam; TF351829; -.
DR Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-MMU-416700; Other semaphorin interactions.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 19264; 2 hits in 110 CRISPR screens.
DR ChiTaRS; Ptprc; mouse.
DR PRO; PR:P06800; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P06800; protein.
DR Bgee; ENSMUSG00000026395; Expressed in peripheral lymph node and 177 other tissues.
DR ExpressionAtlas; P06800; baseline and differential.
DR GO; GO:0032059; C:bleb; ISO:MGI.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; NAS:ARUK-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0098857; C:membrane microdomain; IDA:ARUK-UCL.
DR GO; GO:0045121; C:membrane raft; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:ARUK-UCL.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0046633; P:alpha-beta T cell proliferation; IMP:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP:ARUK-UCL.
DR GO; GO:0042100; P:B cell proliferation; IMP:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0048539; P:bone marrow development; ISO:MGI.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IGI:ARUK-UCL.
DR GO; GO:0044770; P:cell cycle phase transition; ISO:MGI.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IGI:ARUK-UCL.
DR GO; GO:0051607; P:defense response to virus; IDA:MGI.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0042492; P:gamma-delta T cell differentiation; IMP:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:ARUK-UCL.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; ISO:MGI.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IGI:ARUK-UCL.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IGI:ARUK-UCL.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; IMP:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IGI:ARUK-UCL.
DR GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; IMP:UniProtKB.
DR GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0044855; P:plasma membrane raft distribution; IGI:ARUK-UCL.
DR GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IMP:MGI.
DR GO; GO:0050857; P:positive regulation of antigen receptor-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:ARUK-UCL.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:1905451; P:positive regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; IGI:ARUK-UCL.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IMP:MGI.
DR GO; GO:2000473; P:positive regulation of hematopoietic stem cell migration; ISO:MGI.
DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IGI:ARUK-UCL.
DR GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IMP:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IGI:ARUK-UCL.
DR GO; GO:1903615; P:positive regulation of protein tyrosine phosphatase activity; IGI:ARUK-UCL.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; ISO:MGI.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:MGI.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0002711; P:positive regulation of T cell mediated immunity; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IGI:ARUK-UCL.
DR GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IGI:ARUK-UCL.
DR GO; GO:0002923; P:regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
DR GO; GO:0032677; P:regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0050764; P:regulation of phagocytosis; ISO:MGI.
DR GO; GO:0061097; P:regulation of protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:UniProtKB.
DR GO; GO:0010332; P:response to gamma radiation; ISO:MGI.
DR GO; GO:0048864; P:stem cell development; ISO:MGI.
DR GO; GO:0030217; P:T cell differentiation; IMP:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IGI:ARUK-UCL.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF12567; CD45; 1.
DR Pfam; PF12453; PTP_N; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PIRSF; PIRSF002004; Leukocyte_common_antigen; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF52799; SSF52799; 2.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT CHAIN 26..1293
FT /note="Receptor-type tyrosine-protein phosphatase C"
FT /id="PRO_0000025471"
FT TOPO_DOM 26..566
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..1293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 376..472
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 473..568
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 642..901
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 933..1216
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 43..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 842
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1157
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 810
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 842..848
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 886
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 672
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04157"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08575"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04157"
FT MOD_RES 990
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04157"
FT MOD_RES 993
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04157"
FT MOD_RES 994
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04157"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04157"
FT MOD_RES 1267
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 33..171
FT /note="Missing (in isoform 3)"
FT /id="VSP_059410"
FT VAR_SEQ 33..75
FT /note="Missing (in isoform 2)"
FT /id="VSP_059411"
FT CONFLICT 302
FT /note="K -> E (in Ref. 3; AAA39459)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..405
FT /note="VSKPES -> ASKPDP (in Ref. 3; AAA39459)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="N -> T (in Ref. 3; AAA39459)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="V -> G (in Ref. 1; AAA39458)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="N -> S (in Ref. 1; AAA39458)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="I -> S (in Ref. 1; AAA39458)"
FT /evidence="ECO:0000305"
FT CONFLICT 908
FT /note="E -> Q (in Ref. 1; AAA39458)"
FT /evidence="ECO:0000305"
FT CONFLICT 933
FT /note="L -> R (in Ref. 1; AAA39458)"
FT /evidence="ECO:0000305"
FT CONFLICT 955
FT /note="E -> G (in Ref. 1; AAA39458)"
FT /evidence="ECO:0000305"
FT CONFLICT 961
FT /note="N -> K (in Ref. 1; AAA39458)"
FT /evidence="ECO:0000305"
FT CONFLICT 966..969
FT /note="VVPY -> CSID (in Ref. 12; AAA40161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1293 AA; 144837 MW; 44C3D35121181B31 CRC64;
MTMGLWLKLL AFGFALLDTE VFVTGQTPTP SDELSTTENA LLLPQSDPLP ARTTESTPPS
ISERGNGSSE TTYHPGVLST LLPHLSPQPD SQTPSAGGAD TQTFSSQADN PTLTPAPGGG
TDPPGVPGER TVPGTIPADT AFPVDTPSLA RNSSAASPTH TSNVSTTDIS SGASLTTLTP
STLGLASTDP PSTTIATTTK QTCAAMFGNI TVNYTYESSN QTFKADLKDV QNAKCGNEDC
ENVLNNLEEC SQIKNISVSN DSCAPATTID LYVPPGTDKF SLHDCTPKEK ANTSICLEWK
TKNLDFRKCN SDNISYVLHC EPENNTKCIR RNTFIPERCQ LDNLRAQTNY TCVAEILYRG
VKLVKNVINV QTDLGIPETP KPSCGDPAAR KTLVSWPEPV SKPESASKPH GYVLCYKNNS
EKCKSLPNNV TSFEVESLKP YKYYEVSLLA YVNGKIQRNG TAEKCNFHTK ADRPDKVNGM
KTSRPTDNSI NVTCGPPYET NGPKTFYILV VRSGGSFVTK YNKTNCQFYV DNLYYSTDYE
FLVSFHNGVY EGDSVIRNES TNFNAKALII FLVFLIIVTS IALLVVLYKI YDLRKKRSSN
LDEQQELVER DDEKQLMDVE PIHSDILLET YKRKIADEGR LFLAEFQSIP RVFSKFPIKD
ARKPHNQNKN RYVDILPYDY NRVELSEING DAGSTYINAS YIDGFKEPRK YIAAQGPRDE
TVDDFWRMIW EQKATVIVMV TRCEEGNRNK CAEYWPSMEE GTRAFKDIVV TINDHKRCPD
YIIQKLNVAH KKEKATGREV THIQFTSWPD HGVPEDPHLL LKLRRRVNAF SNFFSGPIVV
HCSAGVGRTG TYIGIDAMLE GLEAEGKVDV YGYVVKLRRQ RCLMVQVEAQ YILIHQALVE
YNQFGETEVN LSELHSCLHN MKKRDPPSDP SPLEAEYQRL PSYRSWRTQH IGNQEENKKK
NRNSNVVPYD FNRVPLKHEL EMSKESEPES DESSDDDSDS EETSKYINAS FVMSYWKPEM
MIAAQGPLKE TIGDFWQMIF QRKVKVIVML TELVNGDQEV CAQYWGEGKQ TYGDMEVEMK
DTNRASAYTL RTFELRHSKR KEPRTVYQYQ CTTWKGEELP AEPKDLVSMI QDLKQKLPKA
SPEGMKYHKH ASILVHCRDG SQQTGLFCAL FNLLESAETE DVVDVFQVVK SLRKARPGVV
CSYEQYQFLY DIIASIYPAQ NGQVKKTNSQ DKIEFHNEVD GGKQDANCVR PDGPLNKAQE
DSRGVGTPEP TNSAEEPEHA ANGSASPAPT QSS
