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P04157 (PTPRC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase C

EC=3.1.3.48
Alternative name(s):
Leukocyte common antigen
Short name=L-CA
T200
CD_antigen=CD45
Gene names
Name:Ptprc
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

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.

Subcellular location

Membrane; Single-pass type I membrane protein By similarity. Membrane raft By similarity. Note: Colocalized with DPP4 in membrane rafts By similarity.

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 By similarity.

Post-translational modification

Heavily N- and O-glycosylated.

The cytoplasmic domain contains potential phosphorylation sites.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 1/6 subfamily.

Contains 2 fibronectin type-III domains.

Contains 2 tyrosine-protein phosphatase domains.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from electronic annotation. Source: Ensembl

B cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

B cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

T cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

T cell proliferation

Inferred from electronic annotation. Source: Ensembl

T cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

activation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

bone marrow development

Inferred from electronic annotation. Source: Ensembl

defense response to virus

Inferred from sequence or structural similarity. Source: UniProtKB

dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

hematopoietic progenitor cell differentiation

Inferred from electronic annotation. Source: Ensembl

heterotypic cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

immunoglobulin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

leukocyte cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of T cell mediated cytotoxicity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell adhesion involved in substrate-bound cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytokine-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative thymic T cell selection

Inferred from electronic annotation. Source: Ensembl

positive regulation of B cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell mediated cytotoxicity

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of alpha-beta T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of antigen receptor-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of gamma-delta T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of hematopoietic stem cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of humoral immune response mediated by circulating immunoglobulin

Inferred from electronic annotation. Source: Ensembl

positive regulation of isotype switching to IgG isotypes

Inferred from electronic annotation. Source: Ensembl

positive regulation of stem cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive thymic T cell selection

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of B cell differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of B cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

response to gamma radiation

Inferred from direct assay PubMed 17290791. Source: RGD

stem cell development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from direct assay PubMed 10814697. Source: RGD

cytoplasmic side of plasma membrane

Traceable author statement PubMed 12496963. Source: RGD

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from direct assay PubMed 10814697. Source: RGD

integral component of plasma membrane

Inferred from direct assay Ref.4. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionheparin binding

Inferred from electronic annotation. Source: Ensembl

protein kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase regulator activity

Traceable author statement PubMed 12496963. Source: RGD

protein tyrosine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine phosphatase activity

Traceable author statement PubMed 12496963. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P04157-1)

Also known as: L-CA variant 4;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P04157-2)

Also known as: L-CA variant 1;

The sequence of this isoform differs from the canonical sequence as follows:
     30-161: Missing.
Isoform 3 (identifier: P04157-3)

Also known as: L-CA variant 2;

The sequence of this isoform differs from the canonical sequence as follows:
     30-120: Missing.
Isoform 4 (identifier: P04157-4)

Also known as: L-CA variant 3;

The sequence of this isoform differs from the canonical sequence as follows:
     30-71: Missing.
     121-161: Missing.
Isoform 5 (identifier: P04157-5)

The sequence of this isoform differs from the canonical sequence as follows:
     72-161: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 12731250Receptor-type tyrosine-protein phosphatase C
PRO_0000025472

Regions

Topological domain24 – 546523Extracellular Potential
Transmembrane547 – 56721Helical; Potential
Topological domain568 – 1273706Cytoplasmic Potential
Domain361 – 45292Fibronectin type-III 1
Domain453 – 54593Fibronectin type-III 2
Domain622 – 881260Tyrosine-protein phosphatase 1
Domain913 – 1196284Tyrosine-protein phosphatase 2
Region822 – 8287Substrate binding By similarity

Sites

Active site8221Phosphocysteine intermediate By similarity
Active site11371Phosphocysteine intermediate By similarity
Binding site7901Substrate By similarity
Binding site8661Substrate By similarity

Amino acid modifications

Modified residue9441Phosphoserine By similarity
Modified residue12661Phosphoserine By similarity
Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation2451N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation2821N-linked (GlcNAc...) Potential
Glycosylation3271N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation4711N-linked (GlcNAc...) Potential
Glycosylation5021N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence30 – 161132Missing in isoform 2.
VSP_005167
Alternative sequence30 – 12091Missing in isoform 3.
VSP_005166
Alternative sequence30 – 7142Missing in isoform 4.
VSP_005165
Alternative sequence72 – 16190Missing in isoform 5.
VSP_026163
Alternative sequence121 – 16141Missing in isoform 4.
VSP_005168

Experimental info

Sequence conflict561S → R in AAA41518. Ref.3
Sequence conflict561S → R in AAA41521. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (L-CA variant 4) [UniParc].

Last modified June 12, 2007. Version 2.
Checksum: EDFA48100ACF2CB2

FASTA1,273143,269
        10         20         30         40         50         60 
MYLWLKLLAF SLALLGPEVF VTGQGTTDDG LDTTEIVLLP QTDPLPARTT EFTPPSISER 

        70         80         90        100        110        120 
GNGSSETTYL PGFSSTLMPH LTPQPDSQTP SARGADTQTL SSQADLTTLT AAPSGETDPP 

       130        140        150        160        170        180 
GVPEESTVPE TFPGGTPILA RNSTAPSPTH TSNVSTTDIS SGANLTTPAP STLGFASNTT 

       190        200        210        220        230        240 
TSTEIATPQT KPSCDEKFGN VTVRYIYDDS SKNFNANLEG DKKPKCEYTD CEKELKNLPE 

       250        260        270        280        290        300 
CSQKNVTLSN GSCTPDKIIN LDVPPGTHNF NLTNCTPDIE ANTSICLEWK IKNKFTCDIQ 

       310        320        330        340        350        360 
KISYNFRCTP EMKTFALDKH GTLWLHNLTV RTNYTCAAEV LYNNVILLKQ DRRVQTDFGT 

       370        380        390        400        410        420 
PEMLPHVQCK NSTNSTTLVS WAEPASKHHG YILCYKKTPS EKCENLANDV NSFEVKNLRP 

       430        440        450        460        470        480 
YTEYTVSLFA YVIGRVQRNG PAKDCNFRTK AARPGKVNGM KTSRASDNSI NVTCNSPYEI 

       490        500        510        520        530        540 
NGPEARYILE VKSGGSLVKT FNQSTCKFVV DNLYYSTDYE FLVYFYNGEY LGDPEIKPQS 

       550        560        570        580        590        600 
TSYNSKALII FLVFLIIVTS IALLVVLYKI YDLRKKRSSN LDEQQELVER DEEKQLINVD 

       610        620        630        640        650        660 
PIHSDLLLET YKRKIADEGR LFLAEFQSIP RVFSKFPIKD ARKSQNQNKN RYVDILPYDY 

       670        680        690        700        710        720 
NRVELSEING DAGSTYINAS YIDGFKEPRK YIAAQGPRDE TVDDFWKMIW EQKATVIVMV 

       730        740        750        760        770        780 
TRCEEGNRNK CAEYWPCMEE GTRTFRDVVV TINDHKRCPD YIIQKLSIAH KKEKATGREV 

       790        800        810        820        830        840 
THIQFTSWPD HGVPEDPHLL LKLRRRVNAF SNFFSGPIVV HCSAGVGRTG TYIGIDAMLE 

       850        860        870        880        890        900 
SLEAEGKVDV YGYVVNLRRQ RCLMVQVEAQ YILIHQALVE YNQFGETEVN LSELHSCLQN 

       910        920        930        940        950        960 
LKKRDPPSDP SPLEAEYQRL PSYRSWRTQH IGNQEENKKK NRSSNVVPYD FNRVPLKHEL 

       970        980        990       1000       1010       1020 
EMSKESEAES DESSDEDSDS EETSKYINAS FVMSYWKPEM MIAAQGPLKE TIGDFWQMIF 

      1030       1040       1050       1060       1070       1080 
QRKVKVIVML TELMSGDQEV CAQYWGEGKQ TYGDMEVMLK DTNKSSAYIL RAFELRHSKR 

      1090       1100       1110       1120       1130       1140 
KEPRTVYQYQ CTTWKGEELP AEPKDLVTLI QNIKQKLPKS GSEGMKYHKH ASILVHCRDG 

      1150       1160       1170       1180       1190       1200 
SQQTGLFCAL FNLLESAETE DVVDVFQVVK SLRKARPGMV GSFEQYQFLY DIMASIYPTQ 

      1210       1220       1230       1240       1250       1260 
NGQVKKANSQ DKIEFHNEVD GAKQDANCVQ PADPLNKAQE DSKEVGASEP ASGSEEPEHS 

      1270 
ANGPMSPALT PSS 

« Hide

Isoform 2 (L-CA variant 1) [UniParc].

Checksum: D8CD289BA1873388
Show »

FASTA1,141129,697
Isoform 3 (L-CA variant 2) [UniParc].

Checksum: EDF2153D0EBBF86E
Show »

FASTA1,182133,819
Isoform 4 (L-CA variant 3) [UniParc].

Checksum: 61CD4F787C7E695F
Show »

FASTA1,190134,662
Isoform 5 [UniParc].

Checksum: 1076BD878F13B5CA
Show »

FASTA1,183134,182

References

« Hide 'large scale' references
[1]"Amgen rat EST program."
Amgen EST program
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-147 (ISOFORM 4).
[2]"Lymphocyte specific heterogeneity in the rat leucocyte common antigen (T200) is due to differences in polypeptide sequences near the NH2-terminus."
Barclay A.N., Jackson D.I., Willis A.C., Williams A.F.
EMBO J. 6:1259-1264(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-218 (ISOFORMS 1; 2; 3 AND 4).
[3]Barclay A.N., Jackson D.I., Willis A.C., Williams A.F.
Submitted (MAY-1987) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-1273 (ISOFORMS 1; 3; 4 AND 5).
[4]"Evidence from cDNA clones that the rat leukocyte-common antigen (T200) spans the lipid bilayer and contains a cytoplasmic domain of 80,000 Mr."
Thomas M.L., Barclay A.N., Gagnon J., Williams A.F.
Cell 41:83-93(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 208-1255 (ISOFORM 1).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CB793707 mRNA. No translation available.
Y00065 mRNA. Translation: CAA68272.1.
Y00065 mRNA. Translation: CAA68273.1.
Y00065 mRNA. Translation: CAA68274.1.
Y00065 mRNA. Translation: CAA68275.1.
M25820 mRNA. Translation: AAA41518.1.
M25821 mRNA. Translation: AAA41519.1.
M25822 mRNA. Translation: AAA41520.1.
M25823 mRNA. Translation: AAA41521.1.
PIRA45854.
RefSeqNP_001103357.1. NM_001109887.1.
NP_001103358.1. NM_001109888.1.
NP_001103359.1. NM_001109889.1.
NP_001103360.1. NM_001109890.1.
NP_612516.2. NM_138507.2.
XP_006249972.1. XM_006249910.1.
UniGeneRn.90166.

3D structure databases

ProteinModelPortalP04157.
SMRP04157. Positions 594-1198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246829. 1 interaction.
IntActP04157. 2 interactions.

Chemistry

GuidetoPHARMACOLOGY1852.

PTM databases

PhosphoSiteP04157.

Proteomic databases

PaxDbP04157.
PRIDEP04157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000000814; ENSRNOP00000000814; ENSRNOG00000000655. [P04157-2]
ENSRNOT00000029865; ENSRNOP00000029889; ENSRNOG00000000655. [P04157-5]
ENSRNOT00000029878; ENSRNOP00000030503; ENSRNOG00000000655. [P04157-4]
ENSRNOT00000060292; ENSRNOP00000057042; ENSRNOG00000000655. [P04157-3]
ENSRNOT00000064785; ENSRNOP00000063859; ENSRNOG00000000655. [P04157-1]
GeneID24699.
KEGGrno:24699.
UCSCRGD:3451. rat. [P04157-1]

Organism-specific databases

CTD5788.
RGD3451. Ptprc.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00680000099951.
HOGENOMHOG000049064.
HOVERGENHBG000066.
KOK06478.
OMAEPEHSAN.
OrthoDBEOG7XSTCW.
PhylomeDBP04157.
TreeFamTF351829.

Gene expression databases

ArrayExpressP04157.
GenevestigatorP04157.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR016335. Leukocyte_common_ag.
IPR024739. PTP_recept_N.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF12567. CD45. 1 hit.
PF00041. fn3. 1 hit.
PF12453. PTP_N. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 2 hits.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
PROSITEPS50853. FN3. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio604155.
PROP04157.

Entry information

Entry namePTPRC_RAT
AccessionPrimary (citable) accession number: P04157
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families