P51682 (CCR5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Name:	Ccr5
Synonyms:	Cmkbr5

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
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 CCL4/MIP-1beta requires sulfation, O-glycosylation and sialic acid modifications. Glycosylation on Ser-6 is required for efficient binding of CCL4. Interacts with ADRBK1. Interacts with ARRB1 and ARRB2 By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein.
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 Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein Sulfation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chemotaxis Inferred from electronic annotation. Source: InterPro defense response Inferred from mutant phenotype PubMed 10528159. Source: MGI elevation of cytosolic calcium ion concentration Inferred from electronic annotation. Source: InterPro immune response Inferred from electronic annotation. Source: InterPro negative regulation of cAMP biosynthetic process Inferred from electronic annotation. Source: InterPro negative regulation of macrophage apoptotic process Inferred from direct assay PubMed 16208318. Source: BHF-UCL
Cellular_component	external side of plasma membrane Inferred from direct assay PubMed 16301745PubMed 19008373. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	C-C chemokine receptor activity Inferred from direct assay Ref.1. 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	Helical; Name=1; Potential
	Topological domain	61 – 70	10	Cytoplasmic Potential
	Transmembrane	71 – 91	21	Helical; Name=2; Potential
	Topological domain	92 – 104	13	Extracellular Potential
	Transmembrane	105 – 126	22	Helical; Name=3; Potential
	Topological domain	127 – 143	17	Cytoplasmic Potential
	Transmembrane	144 – 168	25	Helical; Name=4; Potential
	Topological domain	169 – 200	32	Extracellular Potential
	Transmembrane	201 – 220	20	Helical; Name=5; Potential
	Topological domain	221 – 237	17	Cytoplasmic Potential
	Transmembrane	238 – 262	25	Helical; Name=6; Potential
	Topological domain	263 – 279	17	Extracellular Potential
	Transmembrane	280 – 303	24	Helical; Name=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	S → I.
	Natural variant	97	1	V → I.
	Natural variant	109	1	L → V.
	Natural variant	156	1	A → V.
	Natural variant	213	1	V → I.
	Natural variant	318	1	M → I.
	Natural variant	337	1	A → V.
Experimental info
	Sequence conflict	3	1	F → L in CAA63867. Ref.2
	Sequence conflict	62	1	K → R in AAC53386. Ref.4
	Sequence conflict	66	1	V → M in AAC53386. Ref.4
	Sequence conflict	80	1	L → F in CAA63867. Ref.2
	Sequence conflict	145	1	N → I in AAB71183. Ref.5
	Sequence conflict	160	1	F → S in AAC53386. Ref.4
	Sequence conflict	185	1	P → L in AAC53386. Ref.4
	Sequence conflict	190	1	H → Y in AAB37273. Ref.3
	Sequence conflict	208	1	P → S in AAC52454. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P51682 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: D91F50EC9C956795	FASTA	354	40,785
	10 20 30 40 50 60 MDFQGSVPTY SYDIDYGMSA PCQKINVKQI AAQLLPPLYS LVFIFGFVGN MMVFLILISC 70 80 90 100 110 120 KKLKSVTDIY LLNLAISDLL FLLTLPFWAH YAANEWVFGN IMCKVFTGLY HIGYFGGIFF 130 140 150 160 170 180 IILLTIDRYL AIVHAVFALK VRTVNFGVIT SVVTWAVAVF ASLPEIIFTR SQKEGFHYTC 190 200 210 220 230 240 SPHFPHTQYH FWKSFQTLKM VILSLILPLL VMVICYSGIL HTLFRCRNEK KRHRAVRLIF 250 260 270 280 290 300 AIMIVYFLFW TPYNIVLLLT TFQEFFGLNN CSSSNRLDQA MQATETLGMT HCCLNPVIYA 310 320 330 340 350 FVGEKFRSYL SVFFRKHMVK RFCKRCSIFQ QDNPDRASSV YTRSTGEHEV STGL

References

	« Hide 'large scale' referencesShow 'large scale' 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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].
[7]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Spinal ganglion.
[8]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. AK141906 mRNA. Translation: BAE24879.1. AK154595 mRNA. Translation: BAE32698.1. AK155628 mRNA. Translation: BAE33354.1. AK155867 mRNA. Translation: BAE33471.1. CH466671 Genomic DNA. Translation: EDL37177.1. BC103574 mRNA. Translation: AAI03575.1. BC103586 mRNA. Translation: AAI03587.1. BC103587 mRNA. Translation: AAI03588.1.
IPI	IPI00312494.
RefSeq	NP_034047.2. NM_009917.5.
UniGene	Mm.14302.
3D structure databases
ProteinModelPortal	P51682.
SMR	P51682. Positions 39-307.
ModBase	Search...
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P51682.
Proteomic databases
PRIDE	P51682.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000111442; ENSMUSP00000107069; ENSMUSG00000079227.
GeneID	12774.
KEGG	mmu:12774.
Organism-specific databases
CTD	1234.
MGI	MGI:107182. Ccr5.
Phylogenomic databases
eggNOG	NOG148353.
GeneTree	ENSGT00700000104407.
HOVERGEN	HBG106917.
InParanoid	Q3ZAZ8.
KO	K04180.
OMA	IIFTRSQ.
OrthoDB	EOG40S0GG.
Gene expression databases
ArrayExpress	P51682.
Bgee	P51682.
CleanEx	MM_CCR5.
Genevestigator	P51682.
GermOnline	ENSMUSG00000073993. Mus musculus. ENSMUSG00000075434. Mus musculus.
Family and domain databases
InterPro	IPR002240. Chemokine_CCR5. IPR000355. Chemokine_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
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
BindingDB	P51682.
ChEMBL	CHEMBL3676.
NextBio	282158.
SOURCE	Search...

Entry information

Entry name

CCR5_MOUSE

Accession

Primary (citable) accession number: P51682
Secondary accession number(s): O35313 , O35891, P97308, P97405, Q3ZAZ8, Q61867

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 112 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program