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C-C chemokine receptor type 5 (C-C CKR-5) (CC-CKR-5) (CCR-5) (MIP-1 alpha receptor) (CD antigen CD195)

 CCR5_MOUSE              Reviewed;         354 AA.
P51682; O35313; O35891; P97308; P97405; Q3ZAZ8; Q61867;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
23-MAY-2018, entry version 154.
RecName: Full=C-C chemokine receptor type 5;
Short=C-C CKR-5;
Short=CC-CKR-5;
Short=CCR-5;
AltName: Full=MIP-1 alpha receptor;
AltName: CD_antigen=CD195;
Name=Ccr5; Synonyms=Cmkbr5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/SvJ; TISSUE=Spleen;
PubMed=8631787; DOI=10.1074/jbc.271.13.7551;
Boring L., Gosling J., Monteclaro F.S., Lusis A.J., Tsou C.-L.,
Charo I.F.;
"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.";
J. Biol. Chem. 271:7551-7558(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
PubMed=8662890; DOI=10.1074/jbc.271.24.14445;
Meyer A., Coyle A.J., Proudfoot A.E.I., Wells T.N.C., Power C.A.;
"Cloning and characterization of a novel murine macrophage
inflammatory protein-1 alpha receptor.";
J. Biol. Chem. 271:14445-14451(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Ola;
Kuziel W.A., Beck M.A., Dawson T.C., Maeda N.;
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J, and NIH Swiss; TISSUE=Kidney, Liver, and Spleen;
PubMed=9343222;
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 [GENOMIC DNA].
STRAIN=129;
PubMed=9261347;
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.;
"Two distinct CCR5 domains can mediate coreceptor usage by human
immunodeficiency virus type 1.";
J. Virol. 71:6305-6314(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
Guo B., Kuno K., Harada A., Matsushima K.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Spinal ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
-!- 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).
{ECO:0000250|UniProtKB:P51681}.
-!- SUBUNIT: 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 GRK2.
Interacts with ARRB1 and ARRB2. Interacts with CNIH4.
{ECO:0000250|UniProtKB:P51681}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- PTM: Sulfated on at least 2 of the N-terminal tyrosines. Sulfation
is required for efficient binding of the chemokines, CCL3 and CCL4
(By similarity). {ECO:0000250|UniProtKB:P51681}.
-!- PTM: 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).
{ECO:0000250|UniProtKB:P51681}.
-!- PTM: Palmitoylation in the C-terminal is important for cell
surface expression. {ECO:0000250|UniProtKB:P51681}.
-!- PTM: Phosphorylation on serine residues in the C-terminal is
stimulated by binding CC chemokines especially by APO-RANTES.
{ECO:0000250|UniProtKB:P51681}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; U47036; AAC52454.1; -; mRNA.
EMBL; X94151; CAA63867.1; -; mRNA.
EMBL; U68565; AAB37273.1; -; Genomic_DNA.
EMBL; U83327; AAC53386.1; -; Genomic_DNA.
EMBL; AF022990; AAC53389.1; -; Genomic_DNA.
EMBL; AF019772; AAB71183.1; -; Genomic_DNA.
EMBL; D83648; BAA12024.1; -; mRNA.
EMBL; AK141906; BAE24879.1; -; mRNA.
EMBL; AK154595; BAE32698.1; -; mRNA.
EMBL; AK155628; BAE33354.1; -; mRNA.
EMBL; AK155867; BAE33471.1; -; mRNA.
EMBL; CH466671; EDL37177.1; -; Genomic_DNA.
EMBL; BC103574; AAI03575.1; -; mRNA.
EMBL; BC103586; AAI03587.1; -; mRNA.
EMBL; BC103587; AAI03588.1; -; mRNA.
CCDS; CCDS40821.1; -.
RefSeq; NP_034047.2; NM_009917.5.
UniGene; Mm.14302; -.
ProteinModelPortal; P51682; -.
SMR; P51682; -.
IntAct; P51682; 1.
STRING; 10090.ENSMUSP00000107069; -.
BindingDB; P51682; -.
ChEMBL; CHEMBL3676; -.
iPTMnet; P51682; -.
PhosphoSitePlus; P51682; -.
EPD; P51682; -.
MaxQB; P51682; -.
PaxDb; P51682; -.
PRIDE; P51682; -.
Ensembl; ENSMUST00000111442; ENSMUSP00000107069; ENSMUSG00000079227.
GeneID; 12774; -.
KEGG; mmu:12774; -.
UCSC; uc009shd.2; mouse.
CTD; 1234; -.
MGI; MGI:107182; Ccr5.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000118785; -.
HOVERGEN; HBG106917; -.
InParanoid; P51682; -.
KO; K04180; -.
OMA; FGNTMCQ; -.
OrthoDB; EOG091G0B7A; -.
TreeFam; TF330966; -.
Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
Reactome; R-MMU-418594; G alpha (i) signalling events.
PRO; PR:P51682; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000079227; -.
CleanEx; MM_CCR5; -.
ExpressionAtlas; P51682; baseline and differential.
Genevisible; P51682; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0019957; F:C-C chemokine binding; IPI:BHF-UCL.
GO; GO:0016493; F:C-C chemokine receptor activity; IDA:MGI.
GO; GO:0071791; F:chemokine (C-C motif) ligand 5 binding; ISO:MGI.
GO; GO:0006816; P:calcium ion transport; ISO:MGI.
GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0006935; P:chemotaxis; IEA:InterPro.
GO; GO:0006952; P:defense response; IMP:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:MGI.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0006954; P:inflammatory response; IEA:InterPro.
GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
GO; GO:2000110; P:negative regulation of macrophage apoptotic process; IDA:BHF-UCL.
GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:MGI.
GO; GO:0070723; P:response to cholesterol; ISO:MGI.
InterPro; IPR002240; Chemokine_CCR5.
InterPro; IPR000355; Chemokine_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00657; CCCHEMOKINER.
PRINTS; PR01110; CHEMOKINER5.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Sulfation; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 354 C-C chemokine receptor type 5.
/FTId=PRO_0000069269.
TOPO_DOM 1 32 Extracellular. {ECO:0000255}.
TRANSMEM 33 60 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 61 70 Cytoplasmic. {ECO:0000255}.
TRANSMEM 71 91 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 92 104 Extracellular. {ECO:0000255}.
TRANSMEM 105 126 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 127 143 Cytoplasmic. {ECO:0000255}.
TRANSMEM 144 168 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 169 200 Extracellular. {ECO:0000255}.
TRANSMEM 201 220 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 221 237 Cytoplasmic. {ECO:0000255}.
TRANSMEM 238 262 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 263 279 Extracellular. {ECO:0000255}.
TRANSMEM 280 303 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 304 354 Cytoplasmic. {ECO:0000255}.
MOD_RES 10 10 Sulfotyrosine. {ECO:0000255}.
MOD_RES 12 12 Sulfotyrosine. {ECO:0000255}.
MOD_RES 16 16 Sulfotyrosine. {ECO:0000255}.
MOD_RES 338 338 Phosphoserine; by BARK1.
{ECO:0000250|UniProtKB:P51681}.
MOD_RES 339 339 Phosphoserine; by BARK1.
{ECO:0000250|UniProtKB:P51681}.
MOD_RES 344 344 Phosphoserine; by BARK1.
{ECO:0000250|UniProtKB:P51681}.
MOD_RES 351 351 Phosphoserine; by BARK1.
{ECO:0000250|UniProtKB:P51681}.
LIPID 323 323 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P51681}.
LIPID 326 326 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P51681}.
CARBOHYD 6 6 O-linked (GalNAc...) serine.
{ECO:0000250|UniProtKB:P51681}.
DISULFID 22 271 {ECO:0000250|UniProtKB:P51681}.
DISULFID 103 180 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VARIANT 11 11 S -> I.
VARIANT 97 97 V -> I.
VARIANT 109 109 L -> V.
VARIANT 156 156 A -> V.
VARIANT 213 213 V -> I.
VARIANT 318 318 M -> I.
VARIANT 337 337 A -> V.
CONFLICT 3 3 F -> L (in Ref. 2; CAA63867).
{ECO:0000305}.
CONFLICT 62 62 K -> R (in Ref. 4; AAC53386).
{ECO:0000305}.
CONFLICT 66 66 V -> M (in Ref. 4; AAC53386).
{ECO:0000305}.
CONFLICT 80 80 L -> F (in Ref. 2; CAA63867).
{ECO:0000305}.
CONFLICT 145 145 N -> I (in Ref. 5; AAB71183).
{ECO:0000305}.
CONFLICT 160 160 F -> S (in Ref. 4; AAC53386).
{ECO:0000305}.
CONFLICT 185 185 P -> L (in Ref. 4; AAC53386).
{ECO:0000305}.
CONFLICT 190 190 H -> Y (in Ref. 3; AAB37273).
{ECO:0000305}.
CONFLICT 208 208 P -> S (in Ref. 1; AAC52454).
{ECO:0000305}.
SEQUENCE 354 AA; 40785 MW; D91F50EC9C956795 CRC64;
MDFQGSVPTY SYDIDYGMSA PCQKINVKQI AAQLLPPLYS LVFIFGFVGN MMVFLILISC
KKLKSVTDIY LLNLAISDLL FLLTLPFWAH YAANEWVFGN IMCKVFTGLY HIGYFGGIFF
IILLTIDRYL AIVHAVFALK VRTVNFGVIT SVVTWAVAVF ASLPEIIFTR SQKEGFHYTC
SPHFPHTQYH FWKSFQTLKM VILSLILPLL VMVICYSGIL HTLFRCRNEK KRHRAVRLIF
AIMIVYFLFW TPYNIVLLLT TFQEFFGLNN CSSSNRLDQA MQATETLGMT HCCLNPVIYA
FVGEKFRSYL SVFFRKHMVK RFCKRCSIFQ QDNPDRASSV YTRSTGEHEV STGL


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