P06800 (PTPRC_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 140.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Receptor-type tyrosine-protein phosphatase C EC=3.1.3.48 Alternative name(s): Leukocyte common antigen Short name=L-CA Lymphocyte antigen 5 Short name=Ly-5 T200 CD_antigen=CD45 | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 1291 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein 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. Ref.14 |
| 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. Ref.13 |
| Subcellular location | Membrane; Single-pass type I membrane protein. Membrane raft By similarity. Note: Colocalized with DPP4 in membrane rafts By similarity. |
| 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. |
| Sequence caution | The sequence AAA39462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
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. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | |||||||
| Chain | 24 – 1291 | 1268 | Receptor-type tyrosine-protein phosphatase C | PRO_0000025471 | |||||
Regions | |||||||||
| Topological domain | 24 – 564 | 541 | Extracellular Potential | ||||||
| Transmembrane | 565 – 586 | 22 | Helical; Potential | ||||||
| Topological domain | 587 – 1291 | 705 | Cytoplasmic Potential | ||||||
| Domain | 371 – 467 | 97 | Fibronectin type-III 1 | ||||||
| Domain | 472 – 559 | 88 | Fibronectin type-III 2 | ||||||
| Domain | 640 – 899 | 260 | Tyrosine-protein phosphatase 1 | ||||||
| Domain | 931 – 1214 | 284 | Tyrosine-protein phosphatase 2 | ||||||
| Region | 840 – 846 | 7 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 840 | 1 | Phosphocysteine intermediate By similarity | ||||||
| Active site | 1155 | 1 | Phosphocysteine intermediate By similarity | ||||||
| Binding site | 808 | 1 | Substrate By similarity | ||||||
| Binding site | 884 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 940 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 962 | 1 | Phosphoserine Ref.15 Ref.16 | ||||||
| Modified residue | 1284 | 1 | Phosphoserine By similarity | ||||||
| Glycosylation | 64 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 150 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 161 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 207 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 211 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 218 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 253 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 258 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 290 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 311 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 322 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 347 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 416 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 427 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 457 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 489 | 1 | N-linked (GlcNAc...) Potential | ||||||
Natural variations | |||||||||
| Alternative sequence | 31 – 169 | 139 | Missing in isoform 3. | VSP_012442 | |||||
| Alternative sequence | 31 – 73 | 43 | Missing in isoform 2. | VSP_012441 | |||||
Experimental info | |||||||||
| Sequence conflict | 300 | 1 | K → E in AAA39459. Ref.3 | ||||||
| Sequence conflict | 398 | 1 | V → A in AAA39459. Ref.3 | ||||||
| Sequence conflict | 402 – 403 | 2 | ES → DP in AAA39459. Ref.3 | ||||||
| Sequence conflict | 476 | 1 | N → T in AAA39459. Ref.3 | ||||||
| Sequence conflict | 518 – 520 | 3 | KYN → NTT in AAA39458. Ref.1 | ||||||
| Sequence conflict | 528 | 1 | V → G in AAA39458. Ref.1 | ||||||
| Sequence conflict | 556 | 1 | N → S in AAA39458. Ref.1 | ||||||
| Sequence conflict | 588 | 1 | I → S in AAA39458. Ref.1 | ||||||
| Sequence conflict | 906 | 1 | E → Q in AAA39458. Ref.1 | ||||||
| Sequence conflict | 931 | 1 | L → R in AAA39458. Ref.1 | ||||||
| Sequence conflict | 953 | 1 | E → G in AAA39458. Ref.1 | ||||||
| Sequence conflict | 959 | 1 | N → K in AAA39458. Ref.1 | ||||||
Sequences
| ||||||||||||||||||||||||||||||
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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: BALB/c. |
| [4] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [5] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-226 (ISOFORM 2). |
| [6] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. |
| [7] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. |
| [8] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-263 (ISOFORM 3). Tissue: T-cell. |
| [9] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-73. |
| [10] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 730-838. |
| [11] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 961-1291. |
| [12] | "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] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. |
| [13] | "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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GANAB AND PRKCSH. |
| [14] | "CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells." Katagiri T., Ogimoto M., Hasegawa K., Arimura Y., Mitomo K., Okada M., Clark M.R., Mizuno K., Yakura H. J. Immunol. 163:1321-1326(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [15] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962, MASS SPECTROMETRY. Tissue: Melanoma. |
| [16] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940 AND SER-962, MASS SPECTROMETRY. Tissue: Macrophage. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M14342 mRNA. Translation: AAA39458.1. M92933 mRNA. Translation: AAA39459.1. AC122903 Genomic DNA. No translation available. AC159278 Genomic DNA. No translation available. M17320 mRNA. Translation: AAA60449.1. M23354 Genomic DNA. Translation: AAA39462.1. Different initiation. M22456 Genomic DNA. Translation: AAB46374.1. M11934 mRNA. Translation: AAA39461.1. M23241 Genomic DNA. Translation: AAA39460.1. M15174 mRNA. Translation: AAA40161.1. |
| IPI | IPI00126092. IPI00128856. IPI00461132. |
| PIR | A23329. A28334. A28335. I57644. |
| UniGene | Mm.391573. |
3D structure databases | |
| ProteinModelPortal | P06800. |
| SMR | P06800. Positions 471-550, 612-1216. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P06800. 6 interactions. |
| MINT | MINT-188397. |
| STRING | 10090.ENSMUSP00000074352. |
PTM databases | |
| PhosphoSite | P06800. |
Proteomic databases | |
| PaxDb | P06800. |
| PRIDE | P06800. |
Protocols and materials databases | |
| DNASU | 19264. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000027645; ENSMUSP00000027645; ENSMUSG00000026395. ENSMUST00000112036; ENSMUSP00000107667; ENSMUSG00000026395. |
| UCSC | uc007cvg.2. mouse. |
Organism-specific databases | |
| MGI | MGI:97810. Ptprc. |
Phylogenomic databases | |
| eggNOG | COG5599. |
| GeneTree | ENSGT00640000091300. |
| HOVERGEN | HBG000066. |
| OMA | KHELEMS. |
| OrthoDB | EOG4MPHPN. |
Gene expression databases | |
| ArrayExpress | P06800. |
| Bgee | P06800. |
| CleanEx | MM_PTPRC. |
| Genevestigator | P06800. |
| GermOnline | ENSMUSG00000026395. Mus musculus. |
Family and domain databases | |
| Gene3D | 2.60.40.10. 2 hits. |
| InterPro | IPR003961. 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] |
| Pfam | PF12567. CD45. 1 hit. PF12453. PTP_N. 1 hit. PF00102. Y_phosphatase. 2 hits. [Graphical view] |
| PIRSF | PIRSF002004. Leukocyte_common_antigen. 1 hit. |
| PRINTS | PR00700. PRTYPHPHTASE. |
| SMART | SM00060. FN3. 2 hits. SM00194. PTPc. 2 hits. [Graphical view] |
| SUPFAM | SSF49265. FN_III-like. 2 hits. |
| PROSITE | PS50853. FN3. 2 hits. PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 2 hits. PS50055. TYR_PHOSPHATASE_PTP. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 296132. |
| SOURCE | Search... |
Entry information
| Entry name | PTPRC_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P06800 Secondary accession number(s): E9QLT5 Q78EF1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
