ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P51681


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CCR5_HUMAN
Primary accession number P51681
Secondary accession numbers O14692 O14693 O14695 O14696 O14697 O14698 O14699 O14700 O14701 O14702 O14703 O14704 O14705 O14706 O14707 O14708 O15538 Q9UPA4
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 86)
Name and origin of the protein
Protein name C-C chemokine receptor type 5
Synonyms C-C CKR-5
CC-CKR-5
CCR-5
CCR5
HIV-1 fusion coreceptor
CHEMR13
CD195 antigen
Gene name
Name: CCR5
Synonyms: CMKBR5
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1021/bi952950g; PubMed=8639485 [NCBI, ExPASy, EBI, Israel, Japan]
Samson M., Labbe O., Mollereau C., Vassart G., Parmentier M.;
"Molecular cloning and functional expression of a new human CC-chemokine receptor gene.";
Biochemistry 35:3362-3367(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CCL4 AND CCL5, AND TISSUE SPECIFICITY.
TISSUE=Macrophage;
DOI=10.1074/jbc.271.29.17161; PubMed=8663314 [NCBI, ExPASy, EBI, Israel, Japan]
Raport C.J., Gosling J., Schweichart V.L., Gray P.W., Charo I.F.;
"Molecular cloning and functional characterization of a novel human CC chemokine receptor (CCR5) for RANTES, MIP-1beta, and MIP-1alpha.";
J. Biol. Chem. 271:17161-17166(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CCL3; CCL4 AND CCL5.
PubMed=8699119 [NCBI, ExPASy, EBI, Israel, Japan]
Combadiere C., Ahuja S.K., Tiffany H.L., Murphy P.M.;
"Cloning and functional expression of CC CKR5, a human monocyte CC chemokine receptor selective for MIP-1(alpha), MIP-1(beta), and RANTES.";
J. Leukoc. Biol. 60:147-152(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9343222 [NCBI, ExPASy, EBI, Israel, Japan]
Kuhmann S.E., Platt E.J., Kozak S.L., Kabat D.;
"Polymorphisms in the CCR5 genes of African green monkeys and mice implicate specific amino acids in infections by simian and human immunodeficiency viruses.";
J. Virol. 71:8642-8656(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
PubMed=9359654 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang L., Carruthers C.D., He T., Huang Y., Cao Y., Wang G., Hahn B., Ho D.D.;
"HIV type 1 subtypes, coreceptor usage, and CCR5 polymorphism.";
AIDS Res. Hum. Retroviruses 13:1357-1366(1997).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1074/jbc.272.49.30662; PubMed=9388201 [NCBI, ExPASy, EBI, Israel, Japan]
Mummidi S., Ahuja S.S., McDaniel B.L., Ahuja S.K.;
"The human CC chemokine receptor 5 (CCR5) gene. Multiple transcripts with 5'-end heterogeneity, dual promoter usage, and evidence for polymorphisms within the regulatory regions and noncoding exons.";
J. Biol. Chem. 272:30662-30671(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-178.
Magierowska M., Barre-Sinoussi F., Issafras H., Theodorou I., Debre P.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kopatz S.A., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04728; PubMed=16641997 [NCBI, ExPASy, EBI, Israel, Japan]
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
FUNCION AS A HIV-1 CORECEPTOR.
DOI=10.1038/381661a0; PubMed=8649511 [NCBI, ExPASy, EBI, Israel, Japan]
Deng H., Liu R., Ellmeier W., Choe S., Unutmaz D., Burkhart M., di Marzio P., Marmon S., Sutton R.E., Hill C.M., Davis C.B., Peiper S.C., Schall T.J., Littman D.R., Landau N.R.;
"Identification of a major co-receptor for primary isolates of HIV-1.";
Nature 381:661-666(1996).
[12]
FUNCTION AS A HIV-1 CORECEPTOR.
DOI=10.1038/381667a0; PubMed=8649512 [NCBI, ExPASy, EBI, Israel, Japan]
Dragic T., Litwin V., Allaway G.P., Martin S.R., Huang Y., Nagashima K.A., Cayanan C., Maddon P.J., Koup R.A., Moore J.P., Paxton W.A.;
"HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5.";
Nature 381:667-673(1996).
[13]
INTERACTION WITH HIV-1 SURFACE PROTEIN GP120.
DOI=10.1126/science.280.5371.1949; PubMed=9632396 [NCBI, ExPASy, EBI, Israel, Japan]
Rizzuto C.D., Wyatt R., Hernandez-Ramos N., Sun Y., Kwong P.D., Hendrickson W.A., Sodroski J.;
"A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding.";
Science 280:1949-1953(1998).
[14]
SULFATION AT TYR-3, GLYCOSYLATION, AND MUTAGENESIS OF TYR-3; TYR-10; TYR-14 AND TYR-15.
DOI=10.1016/S0092-8674(00)80577-2; PubMed=10089882 [NCBI, ExPASy, EBI, Israel, Japan]
Farzan M., Mirzabekov T., Kolchinsky P., Wyatt R., Cayabyab M., Gerard N.P., Gerard C., Sodroski J., Choe H.;
"Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry.";
Cell 96:667-676(1999).
[15]
PHOSPHORYLATION AT SER-336; SER-337; SER-342 AND SER-349, MUTAGENESIS OF SER-336; SER-337; SER-342 AND SER-349, AND INTERACTION WITH ADRBK1.
DOI=10.1074/jbc.274.13.8875; PubMed=10085131 [NCBI, ExPASy, EBI, Israel, Japan]
Oppermann M., Mack M., Proudfoot A.E., Olbrich H.;
"Differential effects of CC chemokines on CC chemokine receptor 5 (CCR5) phosphorylation and identification of phosphorylation sites on the CCR5 carboxyl terminus.";
J. Biol. Chem. 274:8875-8885(1999).
[16]
PALMITOYLATION AT CYS-321; CYS-323 AND CYS-324, SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF CYS-321; CYS-323 AND CYS-324.
DOI=10.1074/jbc.M100583200; PubMed=11323418 [NCBI, ExPASy, EBI, Israel, Japan]
Blanpain C., Wittamer V., Vanderwinden J.-M., Boom A., Renneboog B., Lee B., Le Poul E., El Asmar L., Govaerts C., Vassart G., Doms R.W., Parmentier M.;
"Palmitoylation of CCR5 is critical for receptor trafficking and efficient activation of intracellular signaling pathways.";
J. Biol. Chem. 276:23795-23804(2001).
[17]
SULFATION, GLYCOSYLATION AT SER-6, INTERACTION WITH CCL3; CCL4 AND CCL5, MUTAGENESIS OF TYR-3; SER-6; SER-7; TYR-10; TYR-14; TYR-15; THR-16 AND SER-17, AND CHARACTERIZATION OF VARIANT ASP-10.
DOI=10.1084/jem.194.11.1661; PubMed=11733580 [NCBI, ExPASy, EBI, Israel, Japan]
Bannert N., Craig S., Farzan M., Sogah D., Santo N.V., Choe H., Sodroski J.;
"Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.";
J. Exp. Med. 194:1661-1673(2001).
[18]
INTERACTION WITH PRAF2.
DOI=10.1016/j.febslet.2005.02.037; PubMed=15757671 [NCBI, ExPASy, EBI, Israel, Japan]
Schweneker M., Bachmann A.S., Moelling K.;
"JM4 is a four-transmembrane protein binding to the CCR5 receptor.";
FEBS Lett. 579:1751-1758(2005).
[19]
INVOLVEMENT IN WEST NILE VIRUS INFECTION SUSCEPTIBILITY.
DOI=10.1084/jem.20051970; PubMed=16418398 [NCBI, ExPASy, EBI, Israel, Japan]
Glass W.G., McDermott D.H., Lim J.K., Lekhong S., Yu S.F., Frank W.A., Pape J., Cheshier R.C., Murphy P.M.;
"CCR5 deficiency increases risk of symptomatic West Nile virus infection.";
J. Exp. Med. 203:35-40(2006).
[20]
3D-STRUCTURE MODELING.
PubMed=12496074 [NCBI, ExPASy, EBI, Israel, Japan]
Paterlini M.G.;
"Structure modeling of the chemokine receptor CCR5: implications for ligand binding and selectivity.";
Biophys. J. 83:3012-3031(2002).
[21]
3D-STRUCTURE MODELING.
DOI=10.1007/s00894-003-0154-9; PubMed=14517611 [NCBI, ExPASy, EBI, Israel, Japan]
Liu S., Fan S., Sun Z.;
"Structural and functional characterization of the human CCR5 receptor in complex with HIV gp120 envelope glycoprotein and CD4 receptor by molecular modeling studies.";
J. Mol. Model. 9:329-336(2003).
[22]
VARIANTS GLN-55; LEU-215; GLN-223; VAL-335 AND PHE-339.
DOI=10.1038/ng0797-221; PubMed=9207783 [NCBI, ExPASy, EBI, Israel, Japan]
Ansari-Lari M.A., Liu X.-M., Metzker M.L., Rut A.R., Gibbs R.A.;
"The extent of genetic variation in the CCR5 gene.";
Nat. Genet. 16:221-222(1997).
[23]
VARIANTS LEU-12; SER-20; SER-29; PHE-42; GLN-55; SER-60; VAL-73; GLN-223; LYS-228 DEL; VAL-301; VAL-335 AND PHE-339, AND ASSOCIATION WITH SUSCEPTIBILITY TO HIV-1.
DOI=10.1086/301645; PubMed=9399903 [NCBI, ExPASy, EBI, Israel, Japan]
Carrington M., Kissner T., Gerrard B., Ivanov S., O'Brien S.J., Dean M.;
"Novel alleles of the chemokine-receptor gene CCR5.";
Am. J. Hum. Genet. 61:1261-1267(1997).
[24]
CHARACTERIZATION OF VARIANT SER-60.
DOI=10.1182/blood.V97.11.3651; PubMed=11369664 [NCBI, ExPASy, EBI, Israel, Japan]
Tamasauskas D., Powell V., Saksela K., Yazdanbakhsh K.;
"A homologous naturally occurring mutation in Duffy and CCR5 leading to reduced receptor expression.";
Blood 97:3651-3654(2001).
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. Acts as a coreceptor (CD4 being the primary receptor) for HIV-1 R5 isolates.
  • SUBUNIT: Interacts with PRAF2. Interacts with HIV-1 surface protein gp120. 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.
  • INTERACTION:
    P35579:MYH9; NbExp=1; IntAct=EBI-489374, EBI-350338;
  • SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
  • TISSUE SPECIFICITY: Highly expressed in spleen, thymus, in the myeloid cell line THP-1, in the promyeloblastic cell line KG-1A and on CD4+ and CD8+ T-cells. Medium levels in peripheral blood leukocytes and in small intestine. Low levels in ovary and lung.
  • PTM: Sulfated on at least 2 of the N-terminal tyrosines. Sulfation contributes to the efficiency of HIV-1 entry and is required for efficient binding of the chemokines, CCL3 and CCL4.
  • PTM: O-glycosylated, but not N-glycosylated. Ser-6 appears to be the major site. Also sialylated glycans present which contribute to chemokine binding. Thr-16 and Ser-17 may also be glycosylated and, if so, with small moieties such as a T-antigen.
  • PTM: Palmitoylation in the C-terminal is important for cell surface expression, and to a lesser extent, for HIV entry.
  • PTM: Phosphorylation on serine residues in the C-terminal is stimulated by binding CC chemokines especially by APO-RANTES.
  • POLYMORPHISM: Variations in CCR5 are associated with resistance or susceptibility to immunodeficiency virus type 1 (resistance or susceptibility to HIV-1) [MIM:609423]. Variations in CCR5 gene also influence the rate of progression to AIDS after infection.
  • POLYMORPHISM: Ser-60 variant, a naturally occurring mutation in a conserved residue in the first intracellular domain of CCR5, results in reduced amounts of the protein in the membrane and consequently may be associated with reduced susceptibility to infection by microbes that depend on these molecules as their receptors.
  • POLYMORPHISM: Variations in CCR5 are associated with susceptibility to West Nile virus (WNV) infection [MIM:610379].
  • SIMILARITY: Belongs to the G-protein coupled receptor 1 family [view classification].
  • WEB RESOURCE: Name=Wikipedia; Note=CC chemokine receptors entry; URL="http://en.wikipedia.org/wiki/CC_chemokine_receptors";.
  • WEB RESOURCE: Name=Wikipedia; Note=CCR5 receptor entry; URL="http://en.wikipedia.org/wiki/CCR5";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X91492; CAA62796.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U54994; AAC50598.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U57840; AAB17071.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U83326; AAC51797.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011500; AAB65700.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011501; AAB65701.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011502; AAB65702.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011503; AAB65703.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011505; AAB65705.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011506; AAB65706.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011507; AAB65707.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011508; AAB65708.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011509; AAB65709.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011510; AAB65710.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011511; AAB65711.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011512; AAB65712.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011513; AAB65713.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011514; AAB65714.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011515; AAB65715.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011516; AAB65716.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011517; AAB65717.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011518; AAB65718.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011519; AAB65719.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011520; AAB65720.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011521; AAB65721.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011522; AAB65722.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011523; AAB65723.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011524; AAB65724.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011525; AAB65725.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011526; AAB65726.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011527; AAB65727.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011528; AAB65728.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011529; AAB65729.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011530; AAB65730.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011531; AAB65731.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011532; AAB65732.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011533; AAB65733.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011534; AAB65734.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011535; AAB65735.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011536; AAB65736.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011537; AAB65737.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF031237; AAB94735.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF052539; AAD18131.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY221093; AAO65971.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U95626; AAB57793.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC038398; AAH38398.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A43113; A43113.
RefSeq NP_000570.1; -.
NP_001093638.1; -.
NP_001099006.1; -.
UniGene Hs.450802
3D structure databases
PDB
1ND8; Model; -; A=1-352.[ExPASy / RCSB / EBI]
1NE0; Model; -; A=1-352.[ExPASy / RCSB / EBI]
1OPN; Model; -; A=1-352.[ExPASy / RCSB / EBI]
1OPT; Model; -; A=1-352.[ExPASy / RCSB / EBI]
1OPW; Model; -; A=1-352.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ND8; -.
1NE0; -.
1OPN; -.
1OPT; -.
1OPW; -.
ModBase P51681.
Protein-protein interaction databases
IntAct P51681; -.
Protein family/group databases
GPCRDB P51681; CCR5_HUMAN.
PTM databases
PhosphoSite P51681; -.
Enzyme and pathway databases
Reactome REACT_6185; HIV Infection.
Organism-specific databases
H-InvDB HIX0024272; -.
HIX0031337; -.
HGNC HGNC:1606; CCR5.
GenAtlas CCR5.
MIM 601373; gene. [NCBI / EBI]
609423; phenotype. [NCBI / EBI]
610379; phenotype. [NCBI / EBI]
PharmGKB PA26170; -.
GeneCards P51681.
Gene expression databases
GermOnline ENSG00000160791; Homo sapiens.
Ontologies
GO
GO:0005768; Cellular component: endosome (traceable author statement from ProtInc).
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0003779; Molecular function: actin binding (inferred from direct assay from UniProtKB).
GO:0016493; Molecular function: C-C chemokine receptor activity (non-traceable author statement from UniProtKB).
GO:0015026; Molecular function: coreceptor activity (traceable author statement from ProtInc).
GO:0004435; Molecular function: phosphoinositide phospholipase C activity (traceable author statement from ProtInc).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0006968; Biological process: cellular defense response (traceable author statement from ProtInc).
GO:0006935; Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0007204; Biological process: elevation of cytosolic calcium ion concentration (traceable author statement from ProtInc).
GO:0007186; Biological process: G-protein coupled receptor protein signaling pathway (traceable author statement from ProtInc).
GO:0006955; Biological process: immune response (traceable author statement from ProtInc).
GO:0006954; Biological process: inflammatory response (traceable author statement from ProtInc).
GO:0019059; Biological process: initiation of viral infection (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR002240; CC_5_rcpt.
IPR000355; Chmkine_rcpt.
IPR000276; GPCR_Rhodpsn.
IPR017452; GPCR_Rhodpsn_supfam.
Graphical view of domain structure.
PANTHER PTHR19264:SF204; CC_5_rcpt; 1.
Pfam PF00001; 7tm_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00657; CCCHEMOKINER.
PR01110; CHEMOKINER5.
PR00237; GPCRRHODOPSN.
PROSITE PS00237; G_PROTEIN_RECEP_F1_1; 1.
PS50262; G_PROTEIN_RECEP_F1_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P51681.
Genome annotation databases
Ensembl ENSG00000160791; Homo sapiens. [Contig view]
ENSG00000215778; Homo sapiens. [Contig view]
GeneID 1234; -.
727797; -.
KEGG hsa:1234; -.
hsa:727797; -.
Phylogenomic databases
HOVERGEN P51681; -.
Other
DrugBank DB04835; Maraviroc.
SOURCE CCR5; Homo sapiens.
GPCRDB-Snakes P51681.
ProtoNet P51681.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; G-protein coupled receptor; Glycoprotein; Host-virus interaction; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism; Receptor; Sulfation; Transducer; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   352  352     C-C chemokine receptor type 5. PRO_0000069257
TOPO_DOM   1    30  30     Extracellular (Potential). 
TRANSMEM   31    58  28     1 (Potential). 
TOPO_DOM   59    68  10     Cytoplasmic (Potential). 
TRANSMEM   69    89  21     2 (Potential). 
TOPO_DOM   90   102  13     Extracellular (Potential). 
TRANSMEM   103   124  22     3 (Potential). 
TOPO_DOM   125   141  17     Cytoplasmic (Potential). 
TRANSMEM   142   166  25     4 (Potential). 
TOPO_DOM   167   198  32     Extracellular (Potential). 
TRANSMEM   199   218  20     5 (Potential). 
TOPO_DOM   219   235  17     Cytoplasmic (Potential). 
TRANSMEM   236   260  25     6 (Potential). 
TOPO_DOM   261   277  17     Extracellular (Potential). 
TRANSMEM   278   301  24     7 (Potential). 
TOPO_DOM   302   352  51     Cytoplasmic (Potential). 
MOD_RES   3     3        Sulfotyrosine. 
MOD_RES   10    10        Sulfotyrosine (Potential). 
MOD_RES   14    14        Sulfotyrosine (Potential). 
MOD_RES   15    15        Sulfotyrosine (Potential). 
MOD_RES   336   336        Phosphoserine; by BARK1. 
MOD_RES   337   337        Phosphoserine; by BARK1. 
MOD_RES   342   342        Phosphoserine; by BARK1. 
MOD_RES   349   349        Phosphoserine; by BARK1. 
LIPID   321   321        S-palmitoyl cysteine. 
LIPID   323   323        S-palmitoyl cysteine. 
LIPID   324   324        S-palmitoyl cysteine. 
CARBOHYD   6     6        O-linked (GalNAc...). 
CARBOHYD   7     7        O-linked (GalNAc...) (Probable). 
CARBOHYD   16    16        O-linked (GalNAc...)