ID CCR1_HUMAN Reviewed; 355 AA. AC P32246; Q86VA9; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 11-NOV-2015, entry version 142. DE RecName: Full=C-C chemokine receptor type 1; DE Short=C-C CKR-1; DE Short=CC-CKR-1; DE Short=CCR-1; DE Short=CCR1; DE AltName: Full=HM145; DE AltName: Full=LD78 receptor; DE AltName: Full=Macrophage inflammatory protein 1-alpha receptor; DE Short=MIP-1alpha-R; DE AltName: Full=RANTES-R; DE AltName: CD_antigen=CD191; GN Name=CCR1; Synonyms=CMKBR1, CMKR1, SCYAR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7679328; DOI=10.1016/0092-8674(93)90118-A; RA Neote K., Digregorio D., Mak J.Y., Horuk R., Schall T.J.; RT "Molecular cloning, functional expression, and signaling RT characteristics of a C-C chemokine receptor."; RL Cell 72:415-425(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7683036; DOI=10.1084/jem.177.5.1421; RA Gao J.-L., Kuhns D., Tiffany H.L., McDermott D., Li X., Francke U., RA Murphy P.M.; RT "Structure and functional expression of the human macrophage RT inflammatory protein 1 alpha/RANTES receptor."; RL J. Exp. Med. 177:1421-1427(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Monocyte; RX PubMed=7505609; DOI=10.1093/intimm/5.10.1239; RA Nomura H., Nielsen B.W., Matsushima K.; RT "Molecular cloning of cDNAs encoding a LD78 receptor and putative RT leukocyte chemotactic peptide receptors."; RL Int. Immunol. 5:1239-1249(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Blood; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INTERACTION WITH CREB3. RX PubMed=15001559; DOI=10.1096/fj.03-0867fje; RA Ko J., Jang S.W., Kim Y.S., Kim I.S., Sung H.J., Kim H.-H., Park J.Y., RA Lee Y.H., Kim J., Na D.S.; RT "Human LZIP binds to CCR1 and differentially affects the chemotactic RT activities of CCR1-dependent chemokines."; RL FASEB J. 18:890-892(2004). RN [6] RP SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=18587271; DOI=10.3858/emm.2008.40.3.332; RA Sung H.J., Kim Y.S., Kang H., Ko J.; RT "Human LZIP induces monocyte CC chemokine receptor 2 expression RT leading to enhancement of monocyte chemoattractant protein 1/CCL2- RT induced cell migration."; RL Exp. Mol. Med. 40:332-338(2008). CC -!- FUNCTION: Receptor for a C-C type chemokine. Binds to MIP-1-alpha, CC MIP-1-delta, RANTES, and MCP-3 and, less efficiently, to MIP-1- CC beta or MCP-1 and subsequently transduces a signal by increasing CC the intracellular calcium ions level. Responsible for affecting CC stem cell proliferation. CC -!- SUBUNIT: Interacts with CREB3. {ECO:0000269|PubMed:15001559}. CC -!- INTERACTION: CC O43889-2:CREB3; NbExp=7; IntAct=EBI-608322, EBI-625022; CC Q04941:PLP2; NbExp=3; IntAct=EBI-608322, EBI-608347; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18587271}; CC Multi-pass membrane protein {ECO:0000269|PubMed:18587271}. CC -!- TISSUE SPECIFICITY: Widely expressed in different hematopoietic CC cells. CC -!- INDUCTION: Up-regulated by CREB3. {ECO:0000269|PubMed:18587271}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=CC chemokine receptors entry; CC URL="https://en.wikipedia.org/wiki/CC_chemokine_receptors"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/CCR1ID44379ch3p21.html"; 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; L09230; AAA58408.1; -; mRNA. DR EMBL; L10918; AAA36543.1; -; mRNA. DR EMBL; D10925; BAA01723.1; -; mRNA. DR EMBL; BC051306; AAH51306.2; -; mRNA. DR EMBL; BC064991; AAH64991.1; -; mRNA. DR CCDS; CCDS2737.1; -. DR PIR; A45177; A45177. DR RefSeq; NP_001286.1; NM_001295.2. DR UniGene; Hs.301921; -. DR PDB; 1Y5D; Model; -; A=1-355. DR PDBsum; 1Y5D; -. DR ProteinModelPortal; P32246; -. DR SMR; P32246; 23-317. DR BioGrid; 107635; 18. DR DIP; DIP-5832N; -. DR IntAct; P32246; 3. DR MINT; MINT-140567; -. DR STRING; 9606.ENSP00000296140; -. DR BindingDB; P32246; -. DR ChEMBL; CHEMBL2413; -. DR GuidetoPHARMACOLOGY; 58; -. DR PhosphoSite; P32246; -. DR BioMuta; CCR1; -. DR DMDM; 416802; -. DR PaxDb; P32246; -. DR PRIDE; P32246; -. DR DNASU; 1230; -. DR Ensembl; ENST00000296140; ENSP00000296140; ENSG00000163823. DR GeneID; 1230; -. DR KEGG; hsa:1230; -. DR UCSC; uc003cph.1; human. DR CTD; 1230; -. DR GeneCards; CCR1; -. DR HGNC; HGNC:1602; CCR1. DR MIM; 601159; gene. DR neXtProt; NX_P32246; -. DR PharmGKB; PA26166; -. DR eggNOG; KOG3656; Eukaryota. DR eggNOG; ENOG410XRW9; LUCA. DR HOGENOM; HOG000234122; -. DR HOVERGEN; HBG106917; -. DR InParanoid; P32246; -. DR KO; K04176; -. DR OMA; FWIDYKL; -. DR OrthoDB; EOG738051; -. DR PhylomeDB; P32246; -. DR TreeFam; TF330966; -. DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR GeneWiki; CCR1; -. DR GenomeRNAi; 1230; -. DR NextBio; 5015; -. DR PRO; PR:P32246; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; P32246; -. DR CleanEx; HS_CCR1; -. DR ExpressionAtlas; P32246; baseline and differential. DR Genevisible; P32246; HS. DR GO; GO:0005829; C:cytosol; IDA:GOC. DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0019957; F:C-C chemokine binding; IPI:UniProtKB. DR GO; GO:0016493; F:C-C chemokine receptor activity; IDA:UniProtKB. DR GO; GO:0071791; F:chemokine (C-C motif) ligand 5 binding; IPI:UniProtKB. DR GO; GO:0035717; F:chemokine (C-C motif) ligand 7 binding; IPI:UniProtKB. DR GO; GO:0004950; F:chemokine receptor activity; IDA:UniProtKB. DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB. DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0007267; P:cell-cell signaling; IDA:UniProtKB. DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB. DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0006935; P:chemotaxis; NAS:UniProtKB. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; NAS:UniProtKB. DR GO; GO:0002407; P:dendritic cell chemotaxis; TAS:BHF-UCL. DR GO; GO:0006887; P:exocytosis; IDA:UniProtKB. DR GO; GO:0007187; P:G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc. DR GO; GO:0006955; P:immune response; IDA:UniProtKB. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0030502; P:negative regulation of bone mineralization; IMP:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB. DR GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:CACAO. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB. DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:UniProtKB. DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:UniProtKB. DR GO; GO:0009611; P:response to wounding; TAS:ProtInc. DR InterPro; IPR002236; Chemokine_CCR1. DR InterPro; IPR000355; Chemokine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00657; CCCHEMOKINER. DR PRINTS; PR01106; CHEMOKINER1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; KW Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1 355 C-C chemokine receptor type 1. FT /FTId=PRO_0000069228. FT TOPO_DOM 1 34 Extracellular. {ECO:0000255}. FT TRANSMEM 35 60 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 61 64 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 65 91 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 92 107 Extracellular. {ECO:0000255}. FT TRANSMEM 108 129 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 130 146 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 147 171 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 172 197 Extracellular. {ECO:0000255}. FT TRANSMEM 198 223 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 224 239 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 240 264 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 265 281 Extracellular. {ECO:0000255}. FT TRANSMEM 282 305 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 306 355 Cytoplasmic. {ECO:0000255}. FT MOD_RES 340 340 Phosphoserine. FT {ECO:0000250|UniProtKB:P51681}. FT MOD_RES 341 341 Phosphoserine. FT {ECO:0000250|UniProtKB:P51681}. FT MOD_RES 345 345 Phosphoserine. FT {ECO:0000250|UniProtKB:P51681}. FT MOD_RES 352 352 Phosphoserine. FT {ECO:0000250|UniProtKB:P51681}. FT CARBOHYD 5 5 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 106 183 {ECO:0000255|PROSITE-ProRule:PRU00521}. FT CONFLICT 337 337 E -> D (in Ref. 3; BAA01723). FT {ECO:0000305}. SQ SEQUENCE 355 AA; 41173 MW; B2C100FFED275985 CRC64; METPNTTEDY DTTTEFDYGD ATPCQKVNER AFGAQLLPPL YSLVFVIGLV GNILVVLVLV QYKRLKNMTS IYLLNLAISD LLFLFTLPFW IDYKLKDDWV FGDAMCKILS GFYYTGLYSE IFFIILLTID RYLAIVHAVF ALRARTVTFG VITSIIIWAL AILASMPGLY FSKTQWEFTH HTCSLHFPHE SLREWKLFQA LKLNLFGLVL PLLVMIICYT GIIKILLRRP NEKKSKAVRL IFVIMIIFFL FWTPYNLTIL ISVFQDFLFT HECEQSRHLD LAVQVTEVIA YTHCCVNPVI YAFVGERFRK YLRQLFHRRV AVHLVKWLPF LSVDRLERVS STSPSTGEHE LSAGF //