[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).
[25]	INVOLVEMENT IN INSULIN-DEPENDENT DIABETES MELLITUS TYPE 22. DOI=10.1056/NEJMoa0807917; PubMed=19073967 [NCBI, ExPASy, EBI, Israel, Japan] Smyth D.J., Plagnol V., Walker N.M., Cooper J.D., Downes K., Yang J.H.M., Howson J.M.M., Stevens H., McManus R., Wijmenga C., Heap G.A., Dubois P.C., Clayton D.G., Hunt K.A., van Heel D.A., Todd J.A.; "Shared and distinct genetic variants in type 1 diabetes and celiac disease."; N. Engl. J. Med. 359:2767-2777(2008).

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].
DISEASE: Genetic variation in CCR5 is associated with suseptibility to insulin-dependent diabetes mellitus type 22 (IDDM22) [MIM:612522]. IDDM is caused by the body's own immune system which destroys the insulin-producing beta cells in the pancreas. Classical features are polydipsia, polyphagia and polyuria, due to hyperglycemia-induced osmotic diuresis.
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]

IPI

IPI00743929; -.

PIR

A43113; A43113.

RefSeq

NP_000570.1; -.
NP_001093638.1; -.

UniGene

Hs.536735

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]
2RLL; NMR; -; A=7-15.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1ND8; -.
1NE0; -.
1OPN; -.
1OPT; -.
1OPW; -.
2RLL; -.

ModBase

P51681.

Protein-protein interaction databases

IntAct

P51681; 5.

Protein family/group databases

GPCRDB

P51681; CCR5_HUMAN.

PTM databases

PhosphoSite

P51681; -.

Enzyme and pathway databases

Pathway_Interaction_DB

il12_2pathway; IL12-mediated signaling events.

Reactome

REACT_14797; Signaling by GPCR.
REACT_6185; HIV Infection.

Organism-specific databases

GeneCards

GC03P046386; -.
GC03P9K0058; -.

H-InvDB

HIX0024272; -.
HIX0031337; -.

HGNC:1606; CCR5.

601373; gene. [NCBI / EBI]
609423; phenotype. [NCBI / EBI]
610379; phenotype. [NCBI / EBI]
612522; phenotype. [NCBI / EBI]

PharmGKB

PA26170; -.

Gene expression databases

Bgee

P51681; -.

GermOnline

ENSG00000160791; Homo sapiens.

Ontologies

GO:0005768;	Cellular component: endosome (traceable author statement from ProtInc).
GO:0009897;	Cellular component: external side of plasma membrane (inferred from direct assay from MGI).
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).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000276; 7TM_GPCR_Rhodpsn.
IPR002240; CC_5_rcpt.
IPR000355; Chmkine_rcpt.
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).

Proteomic databases

PRIDE

P51681; -.

Genome annotation databases

Ensembl

ENSG00000160791; Homo sapiens. [Contig view]
ENSG00000215778; Homo sapiens. [Contig view]

GeneID

1234; -.

KEGG

hsa:1234; -.
hsa:727797; -.

Phylogenomic databases

HOVERGEN

P51681; -.

OMA

P51681; IIFTRSQ.

Other

DB04835; Maraviroc.

5035; -.

CCR5; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell membrane; Diabetes mellitus; Disulfide bond; G-protein coupled receptor; Glycoprotein; Host-virus interaction; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism; Receptor; Sulfation; Transducer; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From 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...) (Potential).`
`CARBOHYD`	`17 17`		`O-linked (GalNAc...) (Potential).`
`DISULFID`	`101 178`		`By similarity.`
`VARIANT`	`10 10`	`1`	`Y -> D (in INCCR5-71A) (No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-3; D-10 and D-15. Restored most CCL4 binding; when associated with D-3 and D-15).`	`VAR_003481`
`VARIANT`	`12 12`	`1`	`I -> L.`	`VAR_024066`
`VARIANT`	`20 20`	`1`	`C -> S.`	`VAR_024067`
`VARIANT`	`29 29`	`1`	`A -> S (in dbSNP:rs1800939 [NCBI]).`	`VAR_011839`
`VARIANT`	`31 31`	`1`	`R -> H (in INCCR5-72A).`	`VAR_003482`
`VARIANT`	`34 34`	`1`	`P -> L (in TZCCR5-179).`	`VAR_003483`
`VARIANT`	`42 42`	`1`	`I -> F.`	`VAR_024068`
`VARIANT`	`55 55`	`1`	`L -> Q (in dbSNP:rs1799863 [NCBI]).`	`VAR_011840`
`VARIANT`	`60 60`	`1`	`R -> S (associated with susceptibility to HIV-1; reduced surface expression and function of CCR5 protein; dbSNP:rs1800940 [NCBI]).`	`VAR_011841`
`VARIANT`	`62 62`	`1`	`K -> R (in UGCCR5-145B).`	`VAR_003484`
`VARIANT`	`68 68`	`1`	`Y -> H (in ZWCCR5-7).`	`VAR_003485`
`VARIANT`	`73 73`	`1`	`A -> V.`	`VAR_024069`
`VARIANT`	`95 95`	`1`	`D -> N (in MWCCR5-107).`	`VAR_003486`
`VARIANT`	`97 97`	`1`	`G -> E (in INCCR5-467).`	`VAR_003487`
`VARIANT`	`122 122`	`1`	`L -> P (in ZWCCR5-7).`	`VAR_003488`
`VARIANT`	`158 158`	`1`	`F -> S (in UGCCR5-145A).`	`VAR_003489`
`VARIANT`	`176 176`	`1`	`Y -> C (in KECCR5-116).`	`VAR_003490`
`VARIANT`	`177 177`	`1`	`T -> A (in INCCR5-45C).`	`VAR_003491`
`VARIANT`	`178 178`	`1`	`C -> R (found in a HIV-resistant individiual).`	`VAR_012481`
`VARIANT`	`185 185`	`1`	`S -> N (in UGCCR5-145A).`	`VAR_003492`
`VARIANT`	`210 210`	`1`	`M -> V (in ZWCCR5-7).`	`VAR_003493`
`VARIANT`	`214 214`	`1`	`Y -> C (in KECCR5-3B).`	`VAR_003494`
`VARIANT`	`215 215`	`1`	`S -> L.`	`VAR_024070`
`VARIANT`	`223 223`	`1`	`R -> Q (in dbSNP:rs1800452 [NCBI]).`	`VAR_011842`
`VARIANT`	`228 228`	`1`	`Missing.`	`VAR_024071`
`VARIANT`	`239 239`	`1`	`T -> S (in INCCR5-71A).`	`VAR_003495`
`VARIANT`	`246 246`	`1`	`L -> P (in UGCCR5-145A).`	`VAR_003496`
`VARIANT`	`288 288`	`1`	`T -> M (in INCCR5-72A).`	`VAR_003497`
`VARIANT`	`301 301`	`1`	`G -> V (in dbSNP:rs1800943 [NCBI]).`	`VAR_011843`
`VARIANT`	`302 302`	`1`	`E -> G (in TZCCR5-179).`	`VAR_003498`
`VARIANT`	`303 303`	`1`	`K -> E (in THCCR5-5).`	`VAR_003499`
`VARIANT`	`306 306`	`1`	`N -> S (in MWCCR5-1567).`	`VAR_003500`
`VARIANT`	`322 322`	`1`	`K -> R (in THCCR5-5).`	`VAR_003501`
`VARIANT`	`333 333`	`1`	`E -> G (in THCCR5-2).`	`VAR_003502`
`VARIANT`	`335 335`	`1`	`A -> V (in MWCCR5-1567, MWCCR5-1568, ZWCCR5-14 and ZWCCR5-112; dbSNP:rs1800944 [NCBI]).`	`VAR_003503`
`VARIANT`	`339 339`	`1`	`Y -> F (in TZCCR5-181A and MWCCR5-107; dbSNP:rs1800945 [NCBI]).`	`VAR_003504`
`VARIANT`	`345 345`	`1`	`E -> G (in UGCCR5-145C).`	`VAR_003505`
`MUTAGEN`	`3 3`		`Y->D: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-10; D-14 and D-15. Restored most CCL4 binding; when associated with D-10 and D-15.`
`MUTAGEN`	`3 3`		`Y->F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-10; F-14 and F-15.`
`MUTAGEN`	`6 6`		`S->A: No change in glycosylation status and greatly decreased CCL4 binding. Loss of molecular mass of about 2 kDa as compared to wild type. Dramatically reduced binding of CCL4; when associated with A-7; A-16; A-17. Similar molecular mass loss. Dramatically reduced binding of CCL4; when associated with A-7 only.`
`MUTAGEN`	`7 7`		`S->A: No change in glycosylation status and binds CCL4 as efficiently as wild type. Loss of molecular mass of about 2 kDa as compared to wild type. Dramatically reduced binding of CCL4; when associated with A-6; A-16; A-17. Similar molecular mass loss. Dramatically reduced binding of CCL4; when associated with A-6 only.`
`MUTAGEN`	`10 10`		`Y->F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-14 and F-15. Small loss of sulfation; when associated with F-14 and F-15.`
`MUTAGEN`	`14 14`		`Y->D: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-3; D-10 and D-14. No restoration of CCL4 binding; when associated with D-10 and D-15.`
`MUTAGEN`	`14 14`		`Y->F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10; and F-15. Small loss of sulfation; when associated with F-10 and F-15.`
`MUTAGEN`	`15 15`		`Y->D: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-3; D-10 and D-14. Restored most CCL4 binding; when associated with D-3 and D-10.`
`MUTAGEN`	`15 15`		`Y->F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10 and F-14. Small loss of sulfation; when associated with F-10 and F-14.`
`MUTAGEN`	`16 16`		`T->A: Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-17.`
`MUTAGEN`	`17 17`		`S->A: Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-16.`
`MUTAGEN`	`321 321`		`C->A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-323 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-323 and A-324.`
`MUTAGEN`	`323 323`		`C->A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-324.`
`MUTAGEN`	`324 324`		`C->A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-323. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-323.`
`MUTAGEN`	`336 336`		`S->A: APO-RANTES-stimulated phosphorylation reduced by 15%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-337 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-337 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-337; A-342 and A349.`
`MUTAGEN`	`337 337`		`S->A: APO-RANTES-stimulated phosphorylation reduced by 18%; APO-RANTES-stimulated phosphorylation reduced by 30-50% on APO-RANTES stimulation; when associated with A-336 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-342 and A349.`
`MUTAGEN`	`342 342`		`S->A: APO-RANTES-stimulated phosphorylation reduced by 42%. Phosphorylation reduced by 50% on APO-RANTES stimulation; when associated with A-336 or A-337 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80% when associated with A-336 and A-337 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-337 and A349.`
`MUTAGEN`	`349 349`		`S->A: APO-RANTES-stimulated phosphorylation reduced by 43%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-336 or A-337 or A-342; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-337 or A-342; No APO-RANTES-stimulated phosphorylation stimulation; when associated with A-336; A-337 and A347.`
`STRAND`	`3 6`	`4`
`TURN`	`21 24`	`4`
`STRAND`	`28 32`	`5`
`HELIX`	`33 58`	`26`
`HELIX`	`69 82`	`14`
`HELIX`	`84 89`	`6`
`TURN`	`92 94`	`3`
`TURN`	`99 103`	`5`
`HELIX`	`105 123`	`19`
`STRAND`	`144 147`	`4`
`HELIX`	`152 157`	`6`
`TURN`	`158 160`	`3`
`HELIX`	`162 164`	`3`
`TURN`	`165 167`	`3`
`STRAND`	`169 172`	`4`
`STRAND`	`175 177`	`3`
`HELIX`	`200 204`	`5`
`TURN`	`205 207`	`3`
`HELIX`	`208 216`	`9`
`STRAND`	`227 230`	`4`
`STRAND`	`233 235`	`3`
`HELIX`	`236 259`	`24`
`STRAND`	`275 277`	`3`
`HELIX`	`279 286`	`8`
`HELIX`	`289 297`	`9`
`STRAND`	`307 309`	`3`
`TURN`	`310 312`	`3`

Sequence information

Length: 352 AA [This is the length of the unprocessed precursor]

Molecular weight: 40524 Da [This is the MW of the unprocessed precursor]

CRC64: 88ECE1F38E6D45A7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDYQVSSPIY DINYYTSEPC QKINVKQIAA RLLPPLYSLV FIFGFVGNML VILILINCKR 

        70         80         90        100        110        120 
LKSMTDIYLL NLAISDLFFL LTVPFWAHYA AAQWDFGNTM CQLLTGLYFI GFFSGIFFII 

       130        140        150        160        170        180 
LLTIDRYLAV VHAVFALKAR TVTFGVVTSV ITWVVAVFAS LPGIIFTRSQ KEGLHYTCSS 

       190        200        210        220        230        240 
HFPYSQYQFW KNFQTLKIVI LGLVLPLLVM VICYSGILKT LLRCRNEKKR HRAVRLIFTI 

       250        260        270        280        290        300 
MIVYFLFWAP YNIVLLLNTF QEFFGLNNCS SSNRLDQAMQ VTETLGMTHC CINPIIYAFV 

       310        320        330        340        350 
GEKFRNYLLV FFQKHIAKRF CKCCSIFQQE APERASSVYT RSTGEQEISV GL

P51681 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools