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Receptor-type tyrosine-protein phosphatase C (EC 3.1.3.48) (Leukocyte common antigen) (L-CA) (T200) (CD antigen CD45)

 PTPRC_RAT               Reviewed;        1273 AA.
P04157;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
12-JUN-2007, sequence version 2.
10-OCT-2018, entry version 183.
RecName: Full=Receptor-type tyrosine-protein phosphatase C;
EC=3.1.3.48;
AltName: Full=Leukocyte common antigen;
Short=L-CA;
AltName: Full=T200;
AltName: CD_antigen=CD45;
Flags: Precursor;
Name=Ptprc;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-147 (ISOFORM 4).
Amgen EST program;
"Amgen rat EST program.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 19-218 (ISOFORMS 1; 2; 3 AND 4).
PubMed=2440674;
Barclay A.N., Jackson D.I., Willis A.C., Williams A.F.;
"Lymphocyte specific heterogeneity in the rat leucocyte common antigen
(T200) is due to differences in polypeptide sequences near the NH2-
terminus.";
EMBO J. 6:1259-1264(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 19-1273 (ISOFORMS 1; 3; 4 AND 5).
Barclay A.N., Jackson D.I., Willis A.C., Williams A.F.;
Submitted (MAY-1987) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 208-1255 (ISOFORM 1).
PubMed=3158393; DOI=10.1016/0092-8674(85)90063-7;
Thomas M.L., Barclay A.N., Gagnon J., Williams A.F.;
"Evidence from cDNA clones that the rat leukocyte-common antigen
(T200) spans the lipid bilayer and contains a cytoplasmic domain of
80,000 Mr.";
Cell 41:83-93(1985).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-652; SER-963; SER-966;
SER-970; SER-973; SER-974; SER-978 AND SER-1209, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Protein tyrosine-protein phosphatase required for T-cell
activation through the antigen receptor. Acts as a positive
regulator of T-cell coactivation upon binding to DPP4. The first
PTPase domain has enzymatic activity, while the second one seems
to affect the substrate specificity of the first one. Upon T-cell
activation, recruits and dephosphorylates SKAP1 and FYN (By
similarity). Dephosphorylates LYN, and thereby modulates LYN
activity (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- SUBUNIT: Interacts with SKAP1. Interacts with DPP4; the
interaction is enhanced in a interleukin-12-dependent manner in
activated lymphocytes. Binds GANAB and PRKCSH (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P08575}; Single-pass type I membrane
protein {ECO:0000255}. Membrane raft
{ECO:0000250|UniProtKB:P08575}. Note=Colocalized with DPP4 in
membrane rafts. {ECO:0000250|UniProtKB:P08575}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=L-CA variant 4;
IsoId=P04157-1; Sequence=Displayed;
Name=2; Synonyms=L-CA variant 1;
IsoId=P04157-2; Sequence=VSP_005167;
Name=3; Synonyms=L-CA variant 2;
IsoId=P04157-3; Sequence=VSP_005166;
Name=4; Synonyms=L-CA variant 3;
IsoId=P04157-4; Sequence=VSP_005165, VSP_005168;
Name=5;
IsoId=P04157-5; Sequence=VSP_026163;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are found in thymocyte
and lymph node. Isoform 4 and isoform 3 are found in the lymph
nod.
-!- DOMAIN: The first PTPase domain interacts with SKAP1.
{ECO:0000250}.
-!- PTM: Heavily N- and O-glycosylated.
-!- PTM: The cytoplasmic domain contains potential phosphorylation
sites.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 1/6 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CB793707; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; Y00065; CAA68272.1; -; mRNA.
EMBL; Y00065; CAA68273.1; -; mRNA.
EMBL; Y00065; CAA68274.1; -; mRNA.
EMBL; Y00065; CAA68275.1; -; mRNA.
EMBL; M25820; AAA41518.1; -; mRNA.
EMBL; M25821; AAA41519.1; -; mRNA.
EMBL; M25822; AAA41520.1; -; mRNA.
EMBL; M25823; AAA41521.1; -; mRNA.
PIR; A45854; A45854.
RefSeq; NP_001103357.1; NM_001109887.2. [P04157-4]
RefSeq; NP_001103358.1; NM_001109888.2. [P04157-5]
RefSeq; NP_001103359.1; NM_001109889.2. [P04157-3]
RefSeq; NP_001103360.1; NM_001109890.2. [P04157-2]
RefSeq; NP_612516.2; NM_138507.3. [P04157-1]
RefSeq; XP_006249972.1; XM_006249910.2. [P04157-1]
UniGene; Rn.90166; -.
PDB; 5FN8; X-ray; 2.45 A; A/B=357-546.
PDBsum; 5FN8; -.
ProteinModelPortal; P04157; -.
SMR; P04157; -.
BioGrid; 246829; 1.
IntAct; P04157; 2.
MINT; P04157; -.
STRING; 10116.ENSRNOP00000063859; -.
iPTMnet; P04157; -.
PhosphoSitePlus; P04157; -.
PaxDb; P04157; -.
PRIDE; P04157; -.
Ensembl; ENSRNOT00000000814; ENSRNOP00000000814; ENSRNOG00000000655. [P04157-2]
Ensembl; ENSRNOT00000029865; ENSRNOP00000029889; ENSRNOG00000000655. [P04157-5]
Ensembl; ENSRNOT00000029878; ENSRNOP00000030503; ENSRNOG00000000655. [P04157-4]
Ensembl; ENSRNOT00000060292; ENSRNOP00000057042; ENSRNOG00000000655. [P04157-3]
Ensembl; ENSRNOT00000064785; ENSRNOP00000063859; ENSRNOG00000000655. [P04157-1]
GeneID; 24699; -.
KEGG; rno:24699; -.
UCSC; RGD:3451; rat. [P04157-1]
CTD; 5788; -.
RGD; 3451; Ptprc.
eggNOG; KOG4228; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00760000118900; -.
HOGENOM; HOG000049064; -.
HOVERGEN; HBG000066; -.
InParanoid; P04157; -.
KO; K06478; -.
OMA; KHELEMS; -.
OrthoDB; EOG091G015A; -.
PhylomeDB; P04157; -.
TreeFam; TF351829; -.
PRO; PR:P04157; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000000655; Expressed in 10 organ(s), highest expression level in spleen.
Genevisible; P04157; RN.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; TAS:RGD.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0019887; F:protein kinase regulator activity; TAS:RGD.
GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:RGD.
GO; GO:0042100; P:B cell proliferation; ISS:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0048539; P:bone marrow development; IEA:Ensembl.
GO; GO:0044770; P:cell cycle phase transition; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0002378; P:immunoglobulin biosynthetic process; IEA:Ensembl.
GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IEA:Ensembl.
GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
GO; GO:0050857; P:positive regulation of antigen receptor-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:2000473; P:positive regulation of hematopoietic stem cell migration; IEA:Ensembl.
GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
GO; GO:0010332; P:response to gamma radiation; IDA:RGD.
GO; GO:0048864; P:stem cell development; IEA:Ensembl.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.90.190.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR024739; PTP_recept_N.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016335; Ptprc.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF12567; CD45; 1.
Pfam; PF00041; fn3; 1.
Pfam; PF12453; PTP_N; 1.
Pfam; PF00102; Y_phosphatase; 2.
PIRSF; PIRSF002004; Leukocyte_common_antigen; 1.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 2.
SMART; SM00194; PTPc; 2.
SMART; SM00404; PTPc_motif; 2.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF52799; SSF52799; 2.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
Protein phosphatase; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 23
CHAIN 24 1273 Receptor-type tyrosine-protein
phosphatase C.
/FTId=PRO_0000025472.
TOPO_DOM 24 546 Extracellular. {ECO:0000255}.
TRANSMEM 547 567 Helical. {ECO:0000255}.
TOPO_DOM 568 1273 Cytoplasmic. {ECO:0000255}.
DOMAIN 361 452 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 453 545 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 622 881 Tyrosine-protein phosphatase 1.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
DOMAIN 913 1196 Tyrosine-protein phosphatase 2.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 822 828 Substrate binding. {ECO:0000250}.
ACT_SITE 822 822 Phosphocysteine intermediate.
{ECO:0000250}.
ACT_SITE 1137 1137 Phosphocysteine intermediate.
{ECO:0000250}.
BINDING 790 790 Substrate. {ECO:0000250}.
BINDING 866 866 Substrate. {ECO:0000250}.
MOD_RES 652 652 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 944 944 Phosphoserine.
{ECO:0000250|UniProtKB:P08575}.
MOD_RES 963 963 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 966 966 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 970 970 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 973 973 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 974 974 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 978 978 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1209 1209 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1266 1266 Phosphoserine.
{ECO:0000250|UniProtKB:P08575}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 245 245 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 374 374 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 471 471 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 502 502 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 30 161 Missing (in isoform 2).
{ECO:0000303|PubMed:2440674}.
/FTId=VSP_005167.
VAR_SEQ 30 120 Missing (in isoform 3).
{ECO:0000303|PubMed:2440674,
ECO:0000303|Ref.3}.
/FTId=VSP_005166.
VAR_SEQ 30 71 Missing (in isoform 4).
{ECO:0000303|PubMed:2440674,
ECO:0000303|Ref.1, ECO:0000303|Ref.3}.
/FTId=VSP_005165.
VAR_SEQ 72 161 Missing (in isoform 5).
{ECO:0000303|Ref.3}.
/FTId=VSP_026163.
VAR_SEQ 121 161 Missing (in isoform 4).
{ECO:0000303|PubMed:2440674,
ECO:0000303|Ref.1, ECO:0000303|Ref.3}.
/FTId=VSP_005168.
CONFLICT 56 56 S -> R (in Ref. 3; AAA41518/AAA41521).
{ECO:0000305}.
STRAND 385 387 {ECO:0000244|PDB:5FN8}.
STRAND 423 426 {ECO:0000244|PDB:5FN8}.
STRAND 445 448 {ECO:0000244|PDB:5FN8}.
STRAND 458 464 {ECO:0000244|PDB:5FN8}.
STRAND 466 468 {ECO:0000244|PDB:5FN8}.
STRAND 470 475 {ECO:0000244|PDB:5FN8}.
STRAND 486 493 {ECO:0000244|PDB:5FN8}.
STRAND 496 510 {ECO:0000244|PDB:5FN8}.
STRAND 518 526 {ECO:0000244|PDB:5FN8}.
STRAND 535 540 {ECO:0000244|PDB:5FN8}.
SEQUENCE 1273 AA; 143269 MW; EDFA48100ACF2CB2 CRC64;
MYLWLKLLAF SLALLGPEVF VTGQGTTDDG LDTTEIVLLP QTDPLPARTT EFTPPSISER
GNGSSETTYL PGFSSTLMPH LTPQPDSQTP SARGADTQTL SSQADLTTLT AAPSGETDPP
GVPEESTVPE TFPGGTPILA RNSTAPSPTH TSNVSTTDIS SGANLTTPAP STLGFASNTT
TSTEIATPQT KPSCDEKFGN VTVRYIYDDS SKNFNANLEG DKKPKCEYTD CEKELKNLPE
CSQKNVTLSN GSCTPDKIIN LDVPPGTHNF NLTNCTPDIE ANTSICLEWK IKNKFTCDIQ
KISYNFRCTP EMKTFALDKH GTLWLHNLTV RTNYTCAAEV LYNNVILLKQ DRRVQTDFGT
PEMLPHVQCK NSTNSTTLVS WAEPASKHHG YILCYKKTPS EKCENLANDV NSFEVKNLRP
YTEYTVSLFA YVIGRVQRNG PAKDCNFRTK AARPGKVNGM KTSRASDNSI NVTCNSPYEI
NGPEARYILE VKSGGSLVKT FNQSTCKFVV DNLYYSTDYE FLVYFYNGEY LGDPEIKPQS
TSYNSKALII FLVFLIIVTS IALLVVLYKI YDLRKKRSSN LDEQQELVER DEEKQLINVD
PIHSDLLLET YKRKIADEGR LFLAEFQSIP RVFSKFPIKD ARKSQNQNKN RYVDILPYDY
NRVELSEING DAGSTYINAS YIDGFKEPRK YIAAQGPRDE TVDDFWKMIW EQKATVIVMV
TRCEEGNRNK CAEYWPCMEE GTRTFRDVVV TINDHKRCPD YIIQKLSIAH KKEKATGREV
THIQFTSWPD HGVPEDPHLL LKLRRRVNAF SNFFSGPIVV HCSAGVGRTG TYIGIDAMLE
SLEAEGKVDV YGYVVNLRRQ RCLMVQVEAQ YILIHQALVE YNQFGETEVN LSELHSCLQN
LKKRDPPSDP SPLEAEYQRL PSYRSWRTQH IGNQEENKKK NRSSNVVPYD FNRVPLKHEL
EMSKESEAES DESSDEDSDS EETSKYINAS FVMSYWKPEM MIAAQGPLKE TIGDFWQMIF
QRKVKVIVML TELMSGDQEV CAQYWGEGKQ TYGDMEVMLK DTNKSSAYIL RAFELRHSKR
KEPRTVYQYQ CTTWKGEELP AEPKDLVTLI QNIKQKLPKS GSEGMKYHKH ASILVHCRDG
SQQTGLFCAL FNLLESAETE DVVDVFQVVK SLRKARPGMV GSFEQYQFLY DIMASIYPTQ
NGQVKKANSQ DKIEFHNEVD GAKQDANCVQ PADPLNKAQE DSKEVGASEP ASGSEEPEHS
ANGPMSPALT PSS


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