P04157 (PTPRC_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 130.
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 T200 CD_antigen=CD45 | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 1273 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | |||||||
| Chain | 24 – 1273 | 1250 | Receptor-type tyrosine-protein phosphatase C | PRO_0000025472 | |||||
Regions | |||||||||
| Topological domain | 24 – 546 | 523 | Extracellular Potential | ||||||
| Transmembrane | 547 – 567 | 21 | Helical; Potential | ||||||
| Topological domain | 568 – 1273 | 706 | Cytoplasmic Potential | ||||||
| Domain | 361 – 449 | 89 | Fibronectin type-III 1 | ||||||
| Domain | 454 – 541 | 88 | Fibronectin type-III 2 | ||||||
| Domain | 622 – 881 | 260 | Tyrosine-protein phosphatase 1 | ||||||
| Domain | 913 – 1196 | 284 | Tyrosine-protein phosphatase 2 | ||||||
| Region | 822 – 828 | 7 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 822 | 1 | Phosphocysteine intermediate By similarity | ||||||
| Active site | 1137 | 1 | Phosphocysteine intermediate By similarity | ||||||
| Binding site | 790 | 1 | Substrate By similarity | ||||||
| Binding site | 866 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 922 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 944 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 966 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 974 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 978 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1266 | 1 | Phosphoserine By similarity | ||||||
| Glycosylation | 62 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 142 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 153 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 164 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 178 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 200 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 245 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 250 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 271 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 282 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 327 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 333 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 371 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 374 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 471 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 502 | 1 | N-linked (GlcNAc...) Potential | ||||||
Natural variations | |||||||||
| Alternative sequence | 30 – 161 | 132 | Missing in isoform 2. | VSP_005167 | |||||
| Alternative sequence | 30 – 120 | 91 | Missing in isoform 3. | VSP_005166 | |||||
| Alternative sequence | 30 – 71 | 42 | Missing in isoform 4. | VSP_005165 | |||||
| Alternative sequence | 72 – 161 | 90 | Missing in isoform 5. | VSP_026163 | |||||
| Alternative sequence | 121 – 161 | 41 | Missing in isoform 4. | VSP_005168 | |||||
Experimental info | |||||||||
| Sequence conflict | 56 | 1 | S → R in AAA41518. Ref.3 | ||||||
| Sequence conflict | 56 | 1 | S → R in AAA41521. Ref.3 | ||||||
Sequences
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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: 2440674] [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: 3158393] [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. |
| IPI | IPI00231601. IPI00389957. IPI00777870. IPI00851110. IPI00851132. |
| PIR | A45854. |
| RefSeq | NP_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. |
| UniGene | Rn.90166. |
3D structure databases | |
| ProteinModelPortal | P04157. |
| SMR | P04157. Positions 594-1198. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P04157. |
PTM databases | |
| PhosphoSite | P04157. |
Proteomic databases | |
| PRIDE | P04157. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000000814; ENSRNOP00000000814; ENSRNOG00000000655. ENSRNOT00000029865; ENSRNOP00000029889; ENSRNOG00000000655. ENSRNOT00000029878; ENSRNOP00000030503; ENSRNOG00000000655. ENSRNOT00000060292; ENSRNOP00000057042; ENSRNOG00000000655. ENSRNOT00000064785; ENSRNOP00000063859; ENSRNOG00000000655. |
| GeneID | 24699. |
| KEGG | rno:24699. |
Organism-specific databases | |
| CTD | 5788. |
| RGD | 3451. Ptprc. |
Phylogenomic databases | |
| eggNOG | roNOG14381. |
| HOVERGEN | HBG000066. |
Gene expression databases | |
| ArrayExpress | P04157. |
| Genevestigator | P04157. |
| GermOnline | ENSRNOG00000000655. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR003961. Fibronectin_type3. IPR013783. Ig-like_fold. IPR024739. PTP_recept_N. IPR000387. Tyr/Dual-specificity_Pase. IPR016130. Tyr_Pase_AS. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view] |
| Gene3D | G3DSA:2.60.40.10. Ig-like_fold. 2 hits. |
| KO | K06478. |
| Pfam | PF00041. fn3. 1 hit. PF12453. PTP_N. 1 hit. PF00102. Y_phosphatase. 2 hits. [Graphical view] |
| 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 | 604155. |
Entry information
| Entry name | PTPRC_RAT | ||||||||
| Accession | Primary (citable) accession number: P04157 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with