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Reviewed, UniProtKB/Swiss-Prot P06800 (CD45_MOUSE)

Last modified February 9, 2010. Version 107. Feed History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Leukocyte common antigen
      Short name=L-CA
    EC=3.1.3.48
Alternative name(s):
    Lymphocyte antigen 5
      Short name=Ly-5
    T200
    CD_antigen=CD45
Gene names
Name: Ptprc
Synonyms: Ly-5
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length1291 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Acts as a positive regulator of T-cell coactivation, by binding DPP4 By similarity. Required for T-cell activation through the antigen receptor. 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 an dephosphorylates SKAP1 and FYN.

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 By similarity. Binds GANAB and PRKCSH.

Subcellular location

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

Developmental stage

Expression is restricted to the hematopoietic compartment of development.

Domain

The first PTPase domain interacts with SKAP1 By similarity.

Post-translational modification

Heavily N- and O-glycosylated.

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.

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Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
   Molecular functionHydrolase
Protein phosphatase
   PTMGlycoprotein
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processB cell differentiation

Inferred from mutant phenotype. Source: MGI

B cell proliferation

Inferred from mutant phenotype. Source: UniProtKB

B cell receptor signaling pathway

Inferred from mutant phenotype. Source: UniProtKB

T cell proliferation

Inferred from mutant phenotype. Source: MGI

T cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

activation of MAPK activity

Inferred from mutant phenotype. Source: MGI

defense response to virus

Inferred from mutant phenotype. Source: UniProtKB

heterotypic cell-cell adhesion

Inferred from mutant phenotype. Source: MGI

leukocyte adhesion

Inferred from mutant phenotype. Source: MGI

negative regulation of T cell mediated cytotoxicity

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of cytokine-mediated signaling pathway

Inferred from direct assay. Source: UniProtKB

negative regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype. Source: MGI

negative regulation of protein amino acid autophosphorylation

Inferred from mutant phenotype. Source: MGI

negative regulation of protein kinase activity

Inferred from direct assay. Source: UniProtKB

negative thymic T cell selection

Inferred from mutant phenotype. Source: MGI

positive regulation of B cell proliferation

Inferred from mutant phenotype. Source: MGI

positive regulation of MAPKKK cascade

Inferred from mutant phenotype. Source: MGI

positive regulation of T cell mediated cytotoxicity

Inferred from mutant phenotype. Source: MGI

positive regulation of alpha-beta T cell proliferation

Inferred from mutant phenotype. Source: MGI

positive regulation of antigen receptor-mediated signaling pathway

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of apoptosis

Inferred from mutant phenotype. Source: MGI

positive regulation of gamma-delta T cell differentiation

Inferred from mutant phenotype. Source: MGI

positive regulation of humoral immune response mediated by circulating immunoglobulin

Inferred from mutant phenotype. Source: MGI

positive regulation of isotype switching to IgG isotypes

Inferred from mutant phenotype. Source: MGI

positive thymic T cell selection

Inferred from mutant phenotype. Source: MGI

protein amino acid dephosphorylation

Inferred from direct assay. Source: UniProtKB

regulation of B cell differentiation

Inferred from mutant phenotype. Source: MGI

regulation of B cell receptor signaling pathway

Inferred from mutant phenotype. Source: MGI

regulation of cell cycle

Inferred from direct assay. Source: UniProtKB

release of sequestered calcium ion into cytosol

Inferred from direct assay. Source: UniProtKB

   Cellular componentexternal side of plasma membrane

Inferred from direct assay. Source: MGI

focal adhesion

Inferred from direct assay. Source: UniProtKB

integral to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionheparan sulfate proteoglycan binding

Inferred from direct assay. Source: MGI

heparin binding

Inferred from direct assay. Source: MGI

protein kinase binding

Inferred from physical interaction. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

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Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06800-1)

Also known as: B220;

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: P06800-2)

The sequence of this isoform differs from the canonical sequence as follows:
     31-73: Missing.
Isoform 3 (identifier: P06800-3)

The sequence of this isoform differs from the canonical sequence as follows:
     31-169: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 12911268Leukocyte common antigen
PRO_0000025471

Regions

Topological domain24 – 564541Extracellular Potential
Transmembrane565 – 58622 Potential
Topological domain587 – 1291705Cytoplasmic Potential
Domain371 – 46797Fibronectin type-III 1
Domain472 – 55988Fibronectin type-III 2
Domain640 – 899260Tyrosine-protein phosphatase 1
Domain931 – 1214284Tyrosine-protein phosphatase 2

Sites

Active site8401Phosphocysteine intermediate By similarity
Active site11551Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue9401Phosphoserine Ref.14
Modified residue9621Phosphoserine Ref.14 Ref.13
Modified residue9841Phosphoserine By similarity
Modified residue9921Phosphoserine By similarity
Modified residue9961Phosphoserine By similarity
Modified residue12841Phosphoserine By similarity
Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2111N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation3111N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential
Glycosylation4271N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Glycosylation4891N-linked (GlcNAc...) Potential
Glycosylation5181N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence31 – 169139Missing in isoform 3.
VSP_012442
Alternative sequence31 – 7343Missing in isoform 2.
VSP_012441

Experimental info

Sequence conflict3001K → E in AAA39459. Ref.3
Sequence conflict3981V → A in AAA39459. Ref.3
Sequence conflict402 – 4032ES → DP in AAA39459. Ref.3
Sequence conflict4761N → T in AAA39459. Ref.3
Sequence conflict518 – 5203NTT → KYN in AAA39459. Ref.3
Sequence conflict5281G → V in AAA39459. Ref.3
Sequence conflict5561S → N in AAA39459. Ref.3
Sequence conflict5881S → I in AAA39459. Ref.3
Sequence conflict9061Q → E in AAA39459. Ref.3
Sequence conflict9311R → L in AAA39459. Ref.3
Sequence conflict9531G → E in AAA39459. Ref.3
Sequence conflict9591K → N in AAA39459. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (B220) [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: A8061F3590C0F4FA

FASTA1,291144,404
        10         20         30         40         50         60 
MGLWLKLLAF GFALLDTEVF VTGQTPTPSD ELSTTENALL LPQSDPLPAR TTESTPPSIS 

        70         80         90        100        110        120 
ERGNGSSETT YHPGVLSTLL PHLSPQPDSQ TPSAGGADTQ TFSSQADNPT LTPAPGGGTD 

       130        140        150        160        170        180 
PPGVPGERTV PGTIPADTAF PVDTPSLARN SSAASPTHTS NVSTTDISSG ASLTTLTPST 

       190        200        210        220        230        240 
LGLASTDPPS TTIATTTKQT CAAMFGNITV NYTYESSNQT FKADLKDVQN AKCGNEDCEN 

       250        260        270        280        290        300 
VLNNLEECSQ IKNISVSNDS CAPATTIDLY VPPGTDKFSL HDCTPKEKAN TSICLEWKTK 

       310        320        330        340        350        360 
NLDFRKCNSD NISYVLHCEP ENNTKCIRRN TFIPERCQLD NLRAQTNYTC VAEILYRGVK 

       370        380        390        400        410        420 
LVKNVINVQT DLGIPETPKP SCGDPAARKT LVSWPEPVSK PESASKPHGY VLCYKNNSEK 

       430        440        450        460        470        480 
CKSLPNNVTS FEVESLKPYK YYEVSLLAYV NGKIQRNGTA EKCNFHTKAD RPDKVNGMKT 

       490        500        510        520        530        540 
SRPTDNSINV TCGPPYETNG PKTFYILVVR SGGSFVTNTT KTNCQFYGDN LYYSTDYEFL 

       550        560        570        580        590        600 
VSFHNGVYEG DSVIRSESTN FNAKALIIFL VFLIIVTSIA LLVVLYKSYD LRKKRSSNLD 

       610        620        630        640        650        660 
EQQELVERDD EKQLMDVEPI HSDILLETYK RKIADEGRLF LAEFQSIPRV FSKFPIKDAR 

       670        680        690        700        710        720 
KPHNQNKNRY VDILPYDYNR VELSEINGDA GSTYINASYI DGFKEPRKYI AAQGPRDETV 

       730        740        750        760        770        780 
DDFWRMIWEQ KATVIVMVTR CEEGNRNKCA EYWPSMEEGT RAFKDIVVTI NDHKRCPDYI 

       790        800        810        820        830        840 
IQKLNVAHKK EKATGREVTH IQFTSWPDHG VPEDPHLLLK LRRRVNAFSN FFSGPIVVHC 

       850        860        870        880        890        900 
SAGVGRTGTY IGIDAMLEGL EAEGKVDVYG YVVKLRRQRC LMVQVEAQYI LIHQALVEYN 

       910        920        930        940        950        960 
QFGETQVNLS ELHSCLHNMK KRDPPSDPSP REAEYQRLPS YRSWRTQHIG NQGENKKKKR 

       970        980        990       1000       1010       1020 
NSNVVPYDFN RVPLKHELEM SKESEPESDE SSDDDSDSEE TSKYINASFV MSYWKPEMMI 

      1030       1040       1050       1060       1070       1080 
AAQGPLKETI GDFWQMIFQR KVKVIVMLTE LVNGDQEVCA QYWGEGKQTY GDMEVEMKDT 

      1090       1100       1110       1120       1130       1140 
NRASAYTLRT FELRHSKRKE PRTVYQYQCT TWKGEELPAE PKDLVSMIQD LKQKLPKASP 

      1150       1160       1170       1180       1190       1200 
EGMKYHKHAS ILVHCRDGSQ QTGLFCALFN LLESAETEDV VDVFQVVKSL RKARPGVVCS 

      1210       1220       1230       1240       1250       1260 
YEQYQFLYDI IASIYPAQNG QVKKTNSQDK IEFHNEVDGG KQDANCVRPD GPLNKAQEDS 

      1270       1280       1290 
RGVGTPEPTN SAEEPEHAAN GSASPAPTQS S

« Hide

Isoform 2.

Checksum: 95F1B1244344C3CD
Show »

FASTA1,248139,839
Isoform 3.

Checksum: B4D956B4E32EA812
Show »

FASTA1,152130,422

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References

« Hide 'large scale' references
[1]"Sequences of Ly-5 cDNA: isoform-related diversity of Ly-5 mRNA."
Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.
Proc. Natl. Acad. Sci. U.S.A. 83:6940-6944(1986) [PubMed: 2944116] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[2]Erratum
Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.
Proc. Natl. Acad. Sci. U.S.A. 84:1991-1991(1987)
Cited for: SEQUENCE REVISION.
[3]"Comparison of mouse Ly5a and Ly5b leucocyte common antigen alleles."
Zebedee S.L., Barritt D.S., Raschke W.C.
Dev. Immunol. 1:243-254(1991) [PubMed: 1822988] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
[4]"Alternative use of 5' exons in the specification of Ly-5 isoforms distinguishing hematopoietic cell lineages."
Saga Y., Tung J.-S., Shen F.-W.W., Boyse E.A.
Proc. Natl. Acad. Sci. U.S.A. 84:5364-5368(1987) [PubMed: 3037546] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-226 (ISOFORM 2).
[5]"Organization of the Ly-5 gene."
Saga Y., Tung J.-S., Shen F.-W.W., Pancoast T.C., Boyse E.A.
Mol. Cell. Biol. 8:4889-4895(1988) [PubMed: 3211131] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[6]"Sequence conservation in potential regulatory regions of the mouse and human leukocyte common antigen gene."
Johnson N.A., Meyer C.M., Pingel J.T., Thomas M.L.
J. Biol. Chem. 264:6220-6229(1989) [PubMed: 2522930] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[7]"Cloning of Ly-5 cDNA."
Shen F.-W., Saga Y., Litman G., Freeman G., Tung J.-S., Cantor H., Boyse E.A.
Proc. Natl. Acad. Sci. U.S.A. 82:7360-7363(1985) [PubMed: 3864163] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-263 (ISOFORM 3).
Tissue: T-cell.
[8]"Structural features of Ly-5 glycoproteins of the mouse and counterparts in other mammals."
Tung J.-S., Saga Y., Boyse E.A.
Immunogenetics 28:271-277(1988) [PubMed: 3417340] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-73.
[9]"Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification."
Yi T., Cleveland J.L., Ihle J.N.
Blood 78:2222-2228(1991) [PubMed: 1932742] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 730-838.
[10]"Cloned murine T200 (Ly-5) cDNA reveals multiple transcripts within B- and T-lymphocyte lineages."
Raschke W.C.
Proc. Natl. Acad. Sci. U.S.A. 84:161-165(1987) [PubMed: 2948186] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 961-1291.
[11]"High sequence conservation between rat (T200) and mouse (Ly-5) leukocyte common antigens."
Gonez L.J., Walker I.D., Sandrin M.S., McKenzie I.F.
Immunogenetics 25:263-266(1987) [PubMed: 3570377] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[12]"Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II."
Arendt C.W., Ostergaard H.L.
J. Biol. Chem. 272:13117-13125(1997) [PubMed: 9148925] [Abstract]
Cited for: INTERACTION WITH GANAB AND PRKCSH.
[13]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962, MASS SPECTROMETRY.
[14]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940 AND SER-962, MASS SPECTROMETRY.
Tissue: Macrophage.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M14342 mRNA. Translation: AAA39458.1.
M92933 mRNA. Translation: AAA39459.1.
M17320 mRNA. Translation: AAA60449.1.
M22456 Genomic DNA. Translation: AAB46374.1.
M11934 mRNA. Translation: AAA39461.1.
M23241 Genomic DNA. Translation: AAA39460.1. Different initiation.
M15174 mRNA. Translation: AAA40161.1.
M23354 Genomic DNA. Translation: AAA39462.1. Different initiation.
IPIIPI00126092.
IPI00128856.
IPI00461132.
PIRA23329.
A28334.
A28335.
I57644.
UniGeneMm.391573

3D structure databases

SMRP06800. Positions 287-556, 612-1216.
ModBaseSearch...

Protein-protein interaction databases

STRINGP06800.

PTM databases

PhosphoSiteP06800.

Proteomic databases

PRIDEP06800.

Genome annotation databases

EnsemblENSMUST00000027645; ENSMUSP00000027645; ENSMUSG00000026395; Mus musculus. [Genome view]
ENSMUST00000081416; ENSMUSP00000080145; ENSMUSG00000026395; Mus musculus. [Genome view]
ENSMUST00000112036; ENSMUSP00000107667; ENSMUSG00000026395; Mus musculus. [Genome view]
ENSMUST00000112038; ENSMUSP00000107669; ENSMUSG00000026395; Mus musculus. [Genome view]
UCSCuc007cvg.1. mouse.
uc007cvh.1. mouse.

Organism-specific databases

MGIMGI:97810. Ptprc.

Phylogenomic databases

HOVERGENP06800.
PhylomeDBP06800.

Enzyme and pathway databases

BRENDA3.1.3.48. 244.

Gene expression databases

ArrayExpressP06800.
BgeeP06800.
CleanExMM_PTPRC.
GenevestigatorP06800.
GermOnlineENSMUSG00000026395. Mus musculus.

Family and domain databases

InterProIPR000387. Dual-sp/Tyr_phosphatase.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR016335. Leukocyte_common_Ag.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 1 hit.
PfamPF00102. Y_phosphatase. 2 hits.
[Graphical view]
PIRSFPIRSF002004. Leukocyte_common_antigen. 1 hit.
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 2 hits.
SM00194. PTPc. 2 hits.
[Graphical view]
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 Resources

SOURCESearch...

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Entry information

Entry nameCD45_MOUSE
AccessionPrimary (citable) accession number: P06800
Secondary accession number(s): Q61812 expand/collapse secondary AC list , Q61813, Q61814, Q61815, Q78EF1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 4, 2005
Last modified: February 9, 2010
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents