Reviewed,
UniProtKB/Swiss-Prot P51682 (CCR5_MOUSE)
Last modified
June 16, 2009.
Version 77.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: C-C chemokine receptor type 5 Short name=C-C CKR-5 Short name=CC-CKR-5 Short name=CCR-5 Alternative name(s): MIP-1 alpha receptor CD_antigen=CD195 | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 354 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Receptor for a number of inflammatory CC-chemokines including MIP-1-alpha, MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation By similarity. |
| Subunit structure | Interacts with PRAF2. Efficient ligand binding to CCL3/MIP-1alpha and CCR4/MIP-1beta requires sulfation, O-glycosylation and sialic acid modifications. Glycosylation on Ser-6 is required for efficient binding of CCL4. Interacts with ADRBK1 By similarity. |
| Subcellular location | |
| Post-translational modification | Sulfated on at least 2 of the N-terminal tyrosines. Sulfation is required for efficient binding of the chemokines, CCL3 and CCL4 By similarity. O-glycosylated, but not N-glycosylated. Ser-6 appears to be the major site. Also sialylated glycans present which contribute to chemokine binding By similarity. Palmitoylation in the C-terminal is important for cell surface expression By similarity. Phosphorylation on serine residues in the C-terminal is stimulated by binding CC chemokines especially by APO-RANTES By similarity. |
| Sequence similarities | Belongs to the G-protein coupled receptor 1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Coding sequence diversity | Polymorphism |
| Domain | Transmembrane |
| Molecular function | G-protein coupled receptor Receptor Transducer |
| PTM | Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein Sulfation |
| Gene Ontology (GO) | |
| Biological process | G-protein coupled receptor protein signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | external side of plasma membrane Inferred from direct assay. Source: MGI integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | C-C chemokine receptor activity Ref.1 Inferred from direct assay. Source: MGI |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 354 | 354 | C-C chemokine receptor type 5 | PRO_0000069269 | |||||||
Regions | |||||||||||
| Topological domain | 1 – 32 | 32 | Extracellular Potential | ||||||||
| Transmembrane | 33 – 60 | 28 | 1 Potential | ||||||||
| Topological domain | 61 – 70 | 10 | Cytoplasmic Potential | ||||||||
| Transmembrane | 71 – 91 | 21 | 2 Potential | ||||||||
| Topological domain | 92 – 104 | 13 | Extracellular Potential | ||||||||
| Transmembrane | 105 – 126 | 22 | 3 Potential | ||||||||
| Topological domain | 127 – 143 | 17 | Cytoplasmic Potential | ||||||||
| Transmembrane | 144 – 168 | 25 | 4 Potential | ||||||||
| Topological domain | 169 – 200 | 32 | Extracellular Potential | ||||||||
| Transmembrane | 201 – 220 | 20 | 5 Potential | ||||||||
| Topological domain | 221 – 237 | 17 | Cytoplasmic Potential | ||||||||
| Transmembrane | 238 – 262 | 25 | 6 Potential | ||||||||
| Topological domain | 263 – 279 | 17 | Extracellular Potential | ||||||||
| Transmembrane | 280 – 303 | 24 | 7 Potential | ||||||||
| Topological domain | 304 – 354 | 51 | Cytoplasmic Potential | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 10 | 1 | Sulfotyrosine Potential | ||||||||
| Modified residue | 12 | 1 | Sulfotyrosine Potential | ||||||||
| Modified residue | 16 | 1 | Sulfotyrosine Potential | ||||||||
| Modified residue | 338 | 1 | Phosphoserine; by BARK1 By similarity | ||||||||
| Modified residue | 339 | 1 | Phosphoserine; by BARK1 By similarity | ||||||||
| Modified residue | 344 | 1 | Phosphoserine; by BARK1 By similarity | ||||||||
| Modified residue | 351 | 1 | Phosphoserine; by BARK1 By similarity | ||||||||
| Lipidation | 323 | 1 | S-palmitoyl cysteine By similarity | ||||||||
| Lipidation | 326 | 1 | S-palmitoyl cysteine By similarity | ||||||||
| Glycosylation | 6 | 1 | O-linked (GalNAc...) By similarity | ||||||||
| Disulfide bond | 103 ↔ 180 | By similarity | |||||||||
Natural variations | |||||||||||
| Natural variant | 11 | 1 | I → S | ||||||||
| Natural variant | 62 | 1 | K → R | ||||||||
| Natural variant | 66 | 1 | V → M | ||||||||
| Natural variant | 97 | 1 | I → V | ||||||||
| Natural variant | 109 | 1 | V → L | ||||||||
| Natural variant | 156 | 1 | V → A | ||||||||
| Natural variant | 160 | 1 | F → S | ||||||||
| Natural variant | 185 | 1 | P → L | ||||||||
| Natural variant | 213 | 1 | I → V | ||||||||
| Natural variant | 318 | 1 | I → M | ||||||||
| Natural variant | 337 | 1 | V → A | ||||||||
Experimental info | |||||||||||
| Sequence conflict | 3 | 1 | F → L in CAA63867. Ref.2 | ||||||||
| Sequence conflict | 80 | 1 | L → F in CAA63867. Ref.2 | ||||||||
| Sequence conflict | 145 | 1 | N → I in AAB71183. Ref.5 | ||||||||
| Sequence conflict | 190 | 1 | H → Y in AAB37273. Ref.3 | ||||||||
| Sequence conflict | 208 | 1 | P → S in AAC52454. Ref.1 | ||||||||
Sequences
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References
| [1] | "Molecular cloning and functional expression of murine JE (monocyte chemoattractant protein 1) and murine macrophage inflammatory protein 1alpha receptors: evidence for two closely linked C-C chemokine receptors on chromosome 9." Boring L., Gosling J., Monteclaro F.S., Lusis A.J., Tsou C.-L., Charo I.F. J. Biol. Chem. 271:7551-7558(1996) [PubMed: 8631787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129/SvJ. Tissue: Spleen. |
| [2] | "Cloning and characterization of a novel murine macrophage inflammatory protein-1 alpha receptor." Meyer A., Coyle A.J., Proudfoot A.E.I., Wells T.N.C., Power C.A. J. Biol. Chem. 271:14445-14451(1996) [PubMed: 8662890] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6 X CBA. Tissue: Thymus. |
| [3] | Kuziel W.A., Beck M.A., Dawson T.C., Maeda N. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Ola. |
| [4] | "Polymorphisms in the CCR5 genes of African green monkeys and mice implicate specific amino acids in infections by simian and human immunodeficiency viruses." Kuhmann S.E., Platt E.J., Kozak S.L., Kabat D. J. Virol. 71:8642-8656(1997) [PubMed: 9343222] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C57BL/6 and NIH Swiss. Tissue: Kidney, Liver and Spleen. |
| [5] | "Two distinct CCR5 domains can mediate coreceptor usage by human immunodeficiency virus type 1." Doranz B.J., Lu Z.H., Rucker J., Zhang T.Y., Sharron M., Cen Y.H., Wang Z.X., Guo H.H., Du J.G., Accavitti M.A., Doms R.W., Peiper S.C. J. Virol. 71:6305-6314(1997) [PubMed: 9261347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129. |
| [6] | Guo B., Kuno K., Harada A., Matsushima K. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U47036 mRNA. Translation: AAC52454.1. X94151 mRNA. Translation: CAA63867.1. U68565 Genomic DNA. Translation: AAB37273.1. U83327 Genomic DNA. Translation: AAC53386.1. AF022990 Genomic DNA. Translation: AAC53389.1. AF019772 Genomic DNA. Translation: AAB71183.1. D83648 mRNA. Translation: BAA12024.1. | |
| IPI | IPI00312494. |
| UniGene | Mm.14302 |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| GPCRDB | Search... |
PTM databases | |
| PhosphoSite | P51682. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000079227. Mus musculus. [Contig view] |
Organism-specific databases | |
| MGI | MGI:107182. Ccr5. |
Phylogenomic databases | |
| HOGENOM | P51682. |
| HOVERGEN | P51682. |
Gene expression databases | |
| ArrayExpress | P51682. |
| Bgee | P51682. |
| CleanEx | MM_CCR5. |
| GermOnline | ENSMUSG00000073993. Mus musculus. ENSMUSG00000075434. Mus musculus. |
Family and domain databases | |
| InterPro | IPR000276. 7TM_GPCR_Rhodpsn. IPR002240. CC_5_rcpt. IPR000355. Chmkine_rcpt. IPR017452. GPCR_Rhodpsn_supfam. [Graphical view] |
| PANTHER | PTHR19264:SF204. CC_5_rcpt. 1 hit. |
| Pfam | PF00001. 7tm_1. 1 hit. [Graphical view] |
| PRINTS | PR00657. CCCHEMOKINER. PR01110. CHEMOKINER5. PR00237. GPCRRHODOPSN. |
| PROSITE | PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| SOURCE | Search... |
Entry information
| Entry name | CCR5_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P51682 Secondary accession number(s): O35313 Q61867 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| 7-transmembrane G-linked receptors List of 7-transmembrane G-linked receptor entries |
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


