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Protein

C-C chemokine receptor type 5

Gene

Ccr5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Molecular functioni

  • actin binding Source: MGI
  • C-C chemokine binding Source: BHF-UCL
  • C-C chemokine receptor activity Source: MGI
  • chemokine (C-C motif) ligand 5 binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_288802. Chemokine receptors bind chemokines.
REACT_306009. Beta defensins.
REACT_331048. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Ccr5
Synonyms:Cmkbr5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:107182. Ccr5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3232ExtracellularSequence AnalysisAdd
BLAST
Transmembranei33 – 6028Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini61 – 7010CytoplasmicSequence Analysis
Transmembranei71 – 9121Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini92 – 10413ExtracellularSequence AnalysisAdd
BLAST
Transmembranei105 – 12622Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini127 – 14317CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei144 – 16825Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini169 – 20032ExtracellularSequence AnalysisAdd
BLAST
Transmembranei201 – 22020Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini221 – 23717CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei238 – 26225Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini263 – 27917ExtracellularSequence AnalysisAdd
BLAST
Transmembranei280 – 30324Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini304 – 35451CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: MGI
  • endosome Source: MGI
  • external side of plasma membrane Source: MGI
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354C-C chemokine receptor type 5PRO_0000069269Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi6 – 61O-linked (GalNAc...)By similarity
Modified residuei10 – 101SulfotyrosineSequence Analysis
Modified residuei12 – 121SulfotyrosineSequence Analysis
Modified residuei16 – 161SulfotyrosineSequence Analysis
Disulfide bondi103 ↔ 180PROSITE-ProRule annotation
Lipidationi323 – 3231S-palmitoyl cysteineBy similarity
Lipidationi326 – 3261S-palmitoyl cysteineBy similarity
Modified residuei338 – 3381Phosphoserine; by BARK1By similarity
Modified residuei339 – 3391Phosphoserine; by BARK1By similarity
Modified residuei344 – 3441Phosphoserine; by BARK1By similarity
Modified residuei351 – 3511Phosphoserine; by BARK1By similarity

Post-translational modificationi

Sulfated on at least 2 of the N-terminal tyrosines. Sulfation is required for efficient binding of the chemokines, CCL3 and CCL4 (By similarity).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).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

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Sulfation

Proteomic databases

PRIDEiP51682.

PTM databases

PhosphoSiteiP51682.

Expressioni

Gene expression databases

BgeeiP51682.
CleanExiMM_CCR5.
ExpressionAtlasiP51682. baseline and differential.
GenevisibleiP51682. MM.

Interactioni

Subunit structurei

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. Interacts with CNIH4.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000107069.

Structurei

3D structure databases

ProteinModelPortaliP51682.
SMRiP51682. Positions 21-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG148353.
GeneTreeiENSGT00760000118785.
HOVERGENiHBG106917.
InParanoidiP51682.
KOiK04180.
OMAiGNTMCQL.
OrthoDBiEOG738051.
TreeFamiTF330966.

Family and domain databases

InterProiIPR002240. Chemokine_CCR5.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24227. PTHR24227. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00657. CCCHEMOKINER.
PR01110. CHEMOKINER5.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51682-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFQGSVPTY SYDIDYGMSA PCQKINVKQI AAQLLPPLYS LVFIFGFVGN
60 70 80 90 100
MMVFLILISC KKLKSVTDIY LLNLAISDLL FLLTLPFWAH YAANEWVFGN
110 120 130 140 150
IMCKVFTGLY HIGYFGGIFF IILLTIDRYL AIVHAVFALK VRTVNFGVIT
160 170 180 190 200
SVVTWAVAVF ASLPEIIFTR SQKEGFHYTC SPHFPHTQYH FWKSFQTLKM
210 220 230 240 250
VILSLILPLL VMVICYSGIL HTLFRCRNEK KRHRAVRLIF AIMIVYFLFW
260 270 280 290 300
TPYNIVLLLT TFQEFFGLNN CSSSNRLDQA MQATETLGMT HCCLNPVIYA
310 320 330 340 350
FVGEKFRSYL SVFFRKHMVK RFCKRCSIFQ QDNPDRASSV YTRSTGEHEV

STGL
Length:354
Mass (Da):40,785
Last modified:July 27, 2011 - v3
Checksum:iD91F50EC9C956795
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31F → L in CAA63867 (PubMed:8662890).Curated
Sequence conflicti62 – 621K → R in AAC53386 (PubMed:9343222).Curated
Sequence conflicti66 – 661V → M in AAC53386 (PubMed:9343222).Curated
Sequence conflicti80 – 801L → F in CAA63867 (PubMed:8662890).Curated
Sequence conflicti145 – 1451N → I in AAB71183 (PubMed:9261347).Curated
Sequence conflicti160 – 1601F → S in AAC53386 (PubMed:9343222).Curated
Sequence conflicti185 – 1851P → L in AAC53386 (PubMed:9343222).Curated
Sequence conflicti190 – 1901H → Y in AAB37273 (Ref. 3) Curated
Sequence conflicti208 – 2081P → S in AAC52454 (PubMed:8631787).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111S → I.
Natural varianti97 – 971V → I.
Natural varianti109 – 1091L → V.
Natural varianti156 – 1561A → V.
Natural varianti213 – 2131V → I.
Natural varianti318 – 3181M → I.
Natural varianti337 – 3371A → V.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS40821.1.
RefSeqiNP_034047.2. NM_009917.5.
UniGeneiMm.14302.

Genome annotation databases

EnsembliENSMUST00000111442; ENSMUSP00000107069; ENSMUSG00000079227.
GeneIDi12774.
KEGGimmu:12774.
UCSCiuc009shd.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS40821.1.
RefSeqiNP_034047.2. NM_009917.5.
UniGeneiMm.14302.

3D structure databases

ProteinModelPortaliP51682.
SMRiP51682. Positions 21-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000107069.

Chemistry

BindingDBiP51682.
ChEMBLiCHEMBL3676.
GuidetoPHARMACOLOGYi62.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP51682.

Proteomic databases

PRIDEiP51682.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000111442; ENSMUSP00000107069; ENSMUSG00000079227.
GeneIDi12774.
KEGGimmu:12774.
UCSCiuc009shd.2. mouse.

Organism-specific databases

CTDi1234.
MGIiMGI:107182. Ccr5.

Phylogenomic databases

eggNOGiNOG148353.
GeneTreeiENSGT00760000118785.
HOVERGENiHBG106917.
InParanoidiP51682.
KOiK04180.
OMAiGNTMCQL.
OrthoDBiEOG738051.
TreeFamiTF330966.

Enzyme and pathway databases

ReactomeiREACT_288802. Chemokine receptors bind chemokines.
REACT_306009. Beta defensins.
REACT_331048. G alpha (i) signalling events.

Miscellaneous databases

NextBioi282158.
PROiP51682.
SOURCEiSearch...

Gene expression databases

BgeeiP51682.
CleanExiMM_CCR5.
ExpressionAtlasiP51682. baseline and differential.
GenevisibleiP51682. MM.

Family and domain databases

InterProiIPR002240. Chemokine_CCR5.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24227. PTHR24227. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00657. CCCHEMOKINER.
PR01110. CHEMOKINER5.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].

Entry informationi

Entry nameiCCR5_MOUSE
AccessioniPrimary (citable) accession number: P51682
Secondary accession number(s): O35313
, O35891, P97308, P97405, Q3ZAZ8, Q61867
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.