ID CCR8_HUMAN Reviewed; 355 AA. AC P51685; B2RC64; Q3KNQ8; Q3KNR3; Q9BYX5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 197. DE RecName: Full=C-C chemokine receptor type 8; DE Short=C-C CKR-8; DE Short=CC-CKR-8; DE Short=CCR-8; DE AltName: Full=CC chemokine receptor CHEMR1; DE AltName: Full=CMKBRL2; DE AltName: Full=Chemokine receptor-like 1; DE Short=CKR-L1; DE AltName: Full=GPR-CY6; DE Short=GPRCY6; DE AltName: Full=TER1; DE AltName: CD_antigen=CDw198; GN Name=CCR8; Synonyms=CKRL1, CMKBR8, CMKBRL2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8886020; DOI=10.1006/bbrc.1996.1595; RA Zaballos A., Varona R., Gutierrez J., Lind P., Marquez G.; RT "Molecular cloning and RNA expression of two new human chemokine receptor- RT like genes."; RL Biochem. Biophys. Res. Commun. 227:846-853(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX PubMed=8977299; DOI=10.1002/eji.1830261230; RA Samson M., Stordeur P., Labbe O., Soularue P., Vassart G., Parmentier M.; RT "Molecular cloning and chromosomal mapping of a novel human gene, ChemR1, RT expressed in T lymphocytes and polymorphonuclear cells and encoding a RT putative chemokine receptor."; RL Eur. J. Immunol. 26:3021-3028(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND FUNCTION AS A RP RECEPTOR FOR CCL1. RC TISSUE=Thymus; RX PubMed=9207005; DOI=10.1084/jem.186.1.165; RA Tiffany H.L., Lautens L.L., Gao J.-L., Pease J., Locati M., Combadiere C., RA Modi W., Bonner T.I., Murphy P.M.; RT "Identification of CCR8: a human monocyte and thymus receptor for the CC RT chemokine I-309."; RL J. Exp. Med. 186:165-170(1997). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8816377; RA Napolitano M., Zingoni A., Bernardini G., Spinetti G., Nista A., RA Storlazzi C.T., Rocchi M., Santoni A.; RT "Molecular cloning of TER1, a chemokine receptor-like gene expressed by RT lymphoid tissues."; RL J. Immunol. 157:2759-2763(1996). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Nakajima T., Yoshida R., Harada S.; RT "Molecular cloning of a human novel C-C chemokine receptor."; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-27. RX PubMed=12551893; DOI=10.1074/jbc.m211422200; RA DeVries M.E., Cao H., Wang J., Xu L., Kelvin A.A., Ran L., Chau L.A., RA Madrenas J., Hegele R.A., Kelvin D.J.; RT "Genomic organization and evolution of the CX3CR1/CCR8 chemokine receptor RT locus."; RL J. Biol. Chem. 278:11985-11994(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP INTERACTION WITH KAPOSI VIRUS PROTEIN VCCL2 (MICROBIAL INFECTION). RX PubMed=9834206; DOI=10.1182/blood.v92.11.4036; RA Sozzani S., Luini W., Bianchi G., Allavena P., Wells T.N., Napolitano M., RA Bernardini G., Vecchi A., D'Ambrosio D., Mazzeo D., Sinigaglia F., RA Santoni A., Maggi E., Romagnani S., Mantovani A.; RT "The viral chemokine macrophage inflammatory protein-II is a selective Th2 RT chemoattractant."; RL Blood 92:4036-4039(1998). RN [12] RP FUNCTION. RX PubMed=9521068; RX DOI=10.1002/(sici)1521-4141(199802)28:02<582::aid-immu582>3.0.co;2-a; RA Bernardini G., Hedrick J., Sozzani S., Luini W., Spinetti G., Weiss M., RA Menon S., Zlotnik A., Mantovani A., Santoni A., Napolitano M.; RT "Identification of the CC chemokines TARC and macrophage inflammatory RT protein-1 beta as novel functional ligands for the CCR8 receptor."; RL Eur. J. Immunol. 28:582-588(1998). RN [13] RP FUNCTION AS A RECEPTOR FOR CCL1. RX PubMed=9469461; RA Goya I., Gutierrez J., Varona R., Kremer L., Zaballos A., Marquez G.; RT "Identification of CCR8 as the specific receptor for the human beta- RT chemokine I-309: cloning and molecular characterization of murine CCR8 as RT the receptor for TCA-3."; RL J. Immunol. 160:1975-1981(1998). RN [14] RP FUNCTION. RX PubMed=10540332; RX DOI=10.1002/(sici)1521-4141(199910)29:10<3210::aid-immu3210>3.0.co;2-w; RA Garlisi C.G., Xiao H., Tian F., Hedrick J.A., Billah M.M., Egan R.W., RA Umland S.P.; RT "The assignment of chemokine-chemokine receptor pairs: TARC and MIP-1 beta RT are not ligands for human CC-chemokine receptor 8."; RL Eur. J. Immunol. 29:3210-3215(1999). RN [15] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN HERPESVIRUS RP 8/HHV8 PROTEIN VCCL1/K6 (MICROBIAL INFECTION). RX PubMed=10377196; DOI=10.1084/jem.189.12.1993; RA Endres M.J., Garlisi C.G., Xiao H., Shan L., Hedrick J.A.; RT "The Kaposi's sarcoma-related herpesvirus (KSHV)-encoded chemokine vMIP-I RT is a specific agonist for the CC chemokine receptor (CCR)8."; RL J. Exp. Med. 189:1993-1998(1999). RN [16] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=20947116; DOI=10.1016/j.virol.2010.09.020; RA Calado M., Matoso P., Santos-Costa Q., Espirito-Santo M., Machado J., RA Rosado L., Antunes F., Mansinho K., Lopes M.M., Maltez F., RA Santos-Ferreira M.O., Azevedo-Pereira J.M.; RT "Coreceptor usage by HIV-1 and HIV-2 primary isolates: the relevance of RT CCR8 chemokine receptor as an alternative coreceptor."; RL Virology 408:174-182(2010). RN [17] RP FUNCTION. RX PubMed=23999500; DOI=10.1084/jem.20130240; RA Islam S.A., Ling M.F., Leung J., Shreffler W.G., Luster A.D.; RT "Identification of human CCR8 as a CCL18 receptor."; RL J. Exp. Med. 210:1889-1898(2013). RN [18] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=35041514; DOI=10.1089/jir.2021.0123; RA Ding D., Zhang L., Liu X., Sun C., He J., Li J., Gao X., Guan F., Zhang L.; RT "Chemokine CCL18 Promotes Phagocytosis Through Its Receptor CCR8 Rather RT than PITPNM3 in Human Microglial Cells."; RL J. Interferon Cytokine Res. 42:19-28(2022). RN [19] {ECO:0007744|PDB:8TLM, ECO:0007744|PDB:8U1U} RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS), DISULFIDE BONDS, RP MUTAGENESIS OF TYR-113; TYR-172 AND GLU-286, AND INTERACTION WITH GNAI1. RX PubMed=38040762; DOI=10.1038/s41467-023-43601-8; RA Sun D., Sun Y., Janezic E., Zhou T., Johnson M., Azumaya C., Noreng S., RA Chiu C., Seki A., Arenzana T.L., Nicoludis J.M., Shi Y., Wang B., Ho H., RA Joshi P., Tam C., Payandeh J., Comps-Agrar L., Wang J., Rutz S., RA Koerber J.T., Masureel M.; RT "Structural basis of antibody inhibition and chemokine activation of the RT human CC chemokine receptor 8."; RL Nat. Commun. 14:7940-7940(2023). CC -!- FUNCTION: G protein-coupled receptor that can bind a variety of CC chemokines, such as CCL1, CCL8, CCL16, CCL18 (PubMed:23999500, CC PubMed:35041514). Regulates monocyte and eosinophil chemotaxis. CC Undergoes internalization upon CCL18 binding, leading to induced CC migration and calcium flux of highly polarized Th2 cells CC (PubMed:23999500). In microglial cells, promotes phagocytosis with CC CCL18 through NF-kappa-B and Src signaling pathways (PubMed:35041514). CC Stimulation of the CCL1-CCR8 signaling axis protects the gut from acute CC intestinal damage (By similarity). {ECO:0000250|UniProtKB:P56484, CC ECO:0000269|PubMed:10540332, ECO:0000269|PubMed:23999500, CC ECO:0000269|PubMed:35041514, ECO:0000269|PubMed:9207005, CC ECO:0000269|PubMed:9469461, ECO:0000269|PubMed:9521068}. CC -!- FUNCTION: (Microbial infection) Acts as a coreceptor for HIV-1 and HIV- CC 2 viruses. {ECO:0000269|PubMed:20947116}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Kaposi virus CC protein vCCL1/K6 and thereby inhibits apoptosis in the targeted cells. CC {ECO:0000269|PubMed:20947116}. CC -!- SUBUNIT: Interacts with GNAI1. {ECO:0000269|PubMed:38040762}. CC -!- SUBUNIT: (Microbial infection) Interacts with Kaposi virus proteins CC vCCL1 and vCCL2. {ECO:0000269|PubMed:10377196, CC ECO:0000269|PubMed:9834206}. CC -!- INTERACTION: CC P51685; O60894: RAMP1; NbExp=2; IntAct=EBI-20804763, EBI-962893; CC P51685; O60895: RAMP2; NbExp=3; IntAct=EBI-20804763, EBI-9009040; CC P51685; O60896: RAMP3; NbExp=3; IntAct=EBI-20804763, EBI-720447; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35041514}; CC Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P51685-1; Sequence=Displayed; CC Name=2; CC IsoId=P51685-2; Sequence=VSP_056340; CC -!- TISSUE SPECIFICITY: Expressed in unstimulated CD4(+) and CD8(+) T-cells CC and polymorphonuclear cells. {ECO:0000269|PubMed:8977299}. CC -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC -!- CAUTION: Was originally thought to be a receptor for SCYA3 and SCYA17. CC {ECO:0000305|PubMed:9521068}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=CC chemokine receptors entry; CC URL="https://en.wikipedia.org/wiki/CC_chemokine_receptors"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z79782; CAB02142.1; -; Genomic_DNA. DR EMBL; Y08456; CAA69712.1; -; Genomic_DNA. DR EMBL; U45983; AAB61962.1; -; Genomic_DNA. DR EMBL; AF005210; AAB62547.1; -; mRNA. DR EMBL; U62556; AAB05542.1; -; Genomic_DNA. DR EMBL; D49919; BAA23387.1; -; mRNA. DR EMBL; AY016370; AAK08628.1; -; Genomic_DNA. DR EMBL; AK314957; BAG37461.1; -; mRNA. DR EMBL; AC104850; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64577.1; -; Genomic_DNA. DR EMBL; BC069067; AAH69067.1; -; mRNA. DR EMBL; BC074743; AAH74743.1; -; mRNA. DR EMBL; BC107152; AAI07153.1; -; mRNA. DR EMBL; BC107159; AAI07160.1; -; mRNA. DR CCDS; CCDS2684.1; -. [P51685-1] DR PIR; JC5067; JC5067. DR RefSeq; NP_005192.1; NM_005201.4. [P51685-1] DR PDB; 8KFX; EM; 2.96 A; R=1-355. DR PDB; 8KFY; EM; 3.06 A; R=1-355. DR PDB; 8KFZ; EM; 3.30 A; R=1-355. DR PDB; 8TLM; EM; 2.90 A; C=1-355. DR PDB; 8U1U; EM; 3.10 A; A=2-355. DR PDB; 8XML; EM; 2.58 A; R=1-355. DR AlphaFoldDB; P51685; -. DR EMDB; EMD-37207; -. DR EMDB; EMD-37208; -. DR EMDB; EMD-37209; -. DR EMDB; EMD-38481; -. DR SMR; P51685; -. DR BioGRID; 107642; 14. DR DIP; DIP-5836N; -. DR FunCoup; P51685; 805. DR IntAct; P51685; 16. DR MINT; P51685; -. DR NDEx; IQUERY-CP-CCR8; 6 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000326432; -. DR BindingDB; P51685; -. DR ChEMBL; CHEMBL4596; -. DR DrugBank; DB28444; RAP-103. DR DrugBank; DB15748; Viral Macrophage-Inflammatory Protein. DR DrugCentral; P51685; -. DR GuidetoPHARMACOLOGY; 65; -. DR GlyGen; P51685; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P51685; -. DR PhosphoSitePlus; P51685; -. DR BioMuta; CCR8; -. DR DMDM; 1707884; -. DR MassIVE; P51685; -. DR PaxDb; 9606-ENSP00000326432; -. DR PeptideAtlas; P51685; -. DR Antibodypedia; 12174; 572 antibodies from 40 providers. DR DNASU; 1237; -. DR Ensembl; ENST00000326306.5; ENSP00000326432.4; ENSG00000179934.8. [P51685-1] DR GeneID; 1237; -. DR KEGG; hsa:1237; -. DR MANE-Select; ENST00000326306.5; ENSP00000326432.4; NM_005201.4; NP_005192.1. DR UCSC; uc010hhr.3; human. [P51685-1] DR AGR; HGNC:1609; -. DR ClinPGx; PA26173; -. DR CTD; 1237; -. DR DisGeNET; 1237; -. DR GeneCards; CCR8; -. DR HGNC; HGNC:1609; CCR8. DR HPA; ENSG00000179934; Tissue enriched (lymphoid). DR MIM; 601834; gene. DR OpenTargets; ENSG00000179934; -. DR VEuPathDB; HostDB:ENSG00000179934; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01020000230359; -. DR HOGENOM; CLU_009579_8_3_1; -. DR InParanoid; P51685; -. DR OMA; QLDQWVF; -. DR OrthoDB; 8951197at2759; -. DR PAN-GO; P51685; 7 GO annotations based on evolutionary models. DR PhylomeDB; P51685; -. DR PathwayCommons; P51685; -. DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR SignaLink; P51685; -. DR SIGNOR; P51685; -. DR Agora; ENSG00000179934; -. DR BioGRID-ORCS; 1237; 10 hits in 1141 CRISPR screens. DR GeneWiki; CCR8_(gene); -. DR GenomeRNAi; 1237; -. DR Pharos; P51685; Tchem. DR PRO; PR:P51685; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P51685; protein. DR Bgee; ENSG00000179934; Expressed in primordial germ cell in gonad and 32 other cell types or tissues. DR ExpressionAtlas; P51685; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central. DR GO; GO:0016493; F:C-C chemokine receptor activity; IBA:GO_Central. DR GO; GO:0004950; F:chemokine receptor activity; TAS:ProtInc. DR GO; GO:0015026; F:coreceptor activity; TAS:ProtInc. DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProt. DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central. DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProt. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central. DR CDD; cd15187; 7tmA_CCR8; 1. DR FunFam; 1.20.1070.10:FF:000026; C-C chemokine receptor type 5; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR050119; CCR1-9-like. DR InterPro; IPR004068; Chemokine_CCR8. DR InterPro; IPR000355; Chemokine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR10489:SF627; C-C CHEMOKINE RECEPTOR TYPE 8; 1. DR PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00657; CCCHEMOKINER. DR PRINTS; PR01530; CHEMOKINER8. DR PRINTS; PR00237; GPCRRHODOPSN. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PDBsum; 8KFX; -. DR PDBsum; 8KFY; -. DR PDBsum; 8KFZ; -. DR PDBsum; 8TLM; -. DR PDBsum; 8U1U; -. DR PDBsum; 8XML; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW G protein-coupled receptor; Membrane; Proteomics identification; Receptor; KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1..355 FT /note="C-C chemokine receptor type 8" FT /id="PRO_0000069288" FT TOPO_DOM 1..35 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 36..63 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 64..73 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 74..93 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 94..107 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 108..129 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 130..146 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 147..171 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 172..202 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 203..222 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 223..238 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 239..263 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 264..280 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 281..304 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 305..355 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DISULFID 25..272 FT /evidence="ECO:0000269|PubMed:38040762, FT ECO:0007744|PDB:8U1U" FT DISULFID 106..183 FT /evidence="ECO:0000269|PubMed:38040762, FT ECO:0007744|PDB:8U1U" FT VAR_SEQ 1..91 FT /note="MDYTLDLSVTTVTDYYYPDIFSSPCDAELIQTNGKLLLAVFYCLLFVFSLLG FT NSLVILVLVVCKKLRSITDVYLLNLALSDLLFVFSFPFQ -> MRNLFRQM (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056340" FT VARIANT 27 FT /note="A -> G (in dbSNP:rs2853699)" FT /evidence="ECO:0000269|PubMed:12551893" FT /id="VAR_049384" FT MUTAGEN 113 FT /note="Y->A: Strong decrease in ability to mediate calcium FT mobilization." FT /evidence="ECO:0000269|PubMed:38040762" FT MUTAGEN 172 FT /note="Y->A: Strong decrease in ability to mediate calcium FT mobilization." FT /evidence="ECO:0000269|PubMed:38040762" FT MUTAGEN 286 FT /note="E->A: Strong decrease in ability to mediate calcium FT mobilization." FT /evidence="ECO:0000269|PubMed:38040762" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:8U1U" FT HELIX 45..57 FT /evidence="ECO:0007829|PDB:8XML" FT HELIX 58..62 FT /evidence="ECO:0007829|PDB:8XML" FT HELIX 69..91 FT /evidence="ECO:0007829|PDB:8XML" FT HELIX 104..135 FT /evidence="ECO:0007829|PDB:8XML" FT HELIX 140..144 FT /evidence="ECO:0007829|PDB:8XML" FT HELIX 147..165 FT /evidence="ECO:0007829|PDB:8XML" FT STRAND 172..179 FT /evidence="ECO:0007829|PDB:8TLM" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:8TLM" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:8TLM" FT HELIX 199..203 FT /evidence="ECO:0007829|PDB:8XML" FT HELIX 204..208 FT /evidence="ECO:0007829|PDB:8XML" FT HELIX 209..225 FT /evidence="ECO:0007829|PDB:8XML" FT HELIX 230..261 FT /evidence="ECO:0007829|PDB:8XML" FT HELIX 286..297 FT /evidence="ECO:0007829|PDB:8XML" FT HELIX 298..302 FT /evidence="ECO:0007829|PDB:8XML" FT HELIX 305..310 FT /evidence="ECO:0007829|PDB:8XML" SQ SEQUENCE 355 AA; 40844 MW; BC14A153CF695361 CRC64; MDYTLDLSVT TVTDYYYPDI FSSPCDAELI QTNGKLLLAV FYCLLFVFSL LGNSLVILVL VVCKKLRSIT DVYLLNLALS DLLFVFSFPF QTYYLLDQWV FGTVMCKVVS GFYYIGFYSS MFFITLMSVD RYLAVVHAVY ALKVRTIRMG TTLCLAVWLT AIMATIPLLV FYQVASEDGV LQCYSFYNQQ TLKWKIFTNF KMNILGLLIP FTIFMFCYIK ILHQLKRCQN HNKTKAIRLV LIVVIASLLF WVPFNVVLFL TSLHSMHILD GCSISQQLTY ATHVTEIISF THCCVNPVIY AFVGEKFKKH LSEIFQKSCS QIFNYLGRQM PRESCEKSSS CQQHSSRSSS VDYIL //