CCR1_HUMAN
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 03-AUG-2022, entry version 185.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 characteristics of
RT 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 inflammatory
RT 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 leukocyte
RT 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 project:
RT 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 leading to
RT enhancement of monocyte chemoattractant protein 1/CCL2-induced cell
RT migration.";
RL Exp. Mol. Med. 40:332-338(2008).
CC -!- FUNCTION: Receptor for a C-C type chemokine. Binds to MIP-1-alpha, MIP-
CC 1-delta, RANTES, and MCP-3 and, less efficiently, to MIP-1-beta or MCP-
CC 1 and subsequently transduces a signal by increasing the intracellular
CC calcium ions level. Responsible for affecting stem cell proliferation.
CC -!- SUBUNIT: Interacts with CREB3. {ECO:0000269|PubMed:15001559}.
CC -!- INTERACTION:
CC P32246; P13501: CCL5; NbExp=2; IntAct=EBI-608322, EBI-2848366;
CC P32246; O43889-2: CREB3; NbExp=7; IntAct=EBI-608322, EBI-625022;
CC P32246; Q04941: PLP2; NbExp=3; IntAct=EBI-608322, EBI-608347;
CC P32246; Q9H3N1: TMX1; NbExp=3; IntAct=EBI-608322, EBI-1051115;
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 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 and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CCR1ID44379ch3p21.html";
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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 PDB; 7VL8; EM; 2.90 A; R=1-355.
DR PDB; 7VL9; EM; 2.60 A; R=1-355.
DR PDB; 7VLA; EM; 2.70 A; R=1-355.
DR PDBsum; 7VL8; -.
DR PDBsum; 7VL9; -.
DR PDBsum; 7VLA; -.
DR AlphaFoldDB; P32246; -.
DR SMR; P32246; -.
DR BioGRID; 107635; 377.
DR DIP; DIP-5832N; -.
DR IntAct; P32246; 24.
DR MINT; P32246; -.
DR STRING; 9606.ENSP00000296140; -.
DR BindingDB; P32246; -.
DR ChEMBL; CHEMBL2413; -.
DR DrugCentral; P32246; -.
DR GuidetoPHARMACOLOGY; 58; -.
DR GlyGen; P32246; 1 site.
DR iPTMnet; P32246; -.
DR PhosphoSitePlus; P32246; -.
DR BioMuta; CCR1; -.
DR DMDM; 416802; -.
DR MassIVE; P32246; -.
DR PaxDb; P32246; -.
DR PeptideAtlas; P32246; -.
DR PRIDE; P32246; -.
DR ProteomicsDB; 54854; -.
DR Antibodypedia; 12727; 558 antibodies from 37 providers.
DR DNASU; 1230; -.
DR Ensembl; ENST00000296140.4; ENSP00000296140.3; ENSG00000163823.4.
DR GeneID; 1230; -.
DR KEGG; hsa:1230; -.
DR MANE-Select; ENST00000296140.4; ENSP00000296140.3; NM_001295.3; NP_001286.1.
DR CTD; 1230; -.
DR DisGeNET; 1230; -.
DR GeneCards; CCR1; -.
DR HGNC; HGNC:1602; CCR1.
DR HPA; ENSG00000163823; Tissue enhanced (lymphoid).
DR MalaCards; CCR1; -.
DR MIM; 601159; gene.
DR neXtProt; NX_P32246; -.
DR OpenTargets; ENSG00000163823; -.
DR Orphanet; 117; Behcet disease.
DR PharmGKB; PA26166; -.
DR VEuPathDB; HostDB:ENSG00000163823; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230359; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P32246; -.
DR OMA; CYTGIIN; -.
DR OrthoDB; 900867at2759; -.
DR PhylomeDB; P32246; -.
DR TreeFam; TF330966; -.
DR PathwayCommons; P32246; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR SignaLink; P32246; -.
DR SIGNOR; P32246; -.
DR BioGRID-ORCS; 1230; 9 hits in 1073 CRISPR screens.
DR ChiTaRS; CCR1; human.
DR GeneWiki; CCR1; -.
DR GenomeRNAi; 1230; -.
DR Pharos; P32246; Tchem.
DR PRO; PR:P32246; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P32246; protein.
DR Bgee; ENSG00000163823; Expressed in monocyte and 167 other tissues.
DR ExpressionAtlas; P32246; baseline and differential.
DR Genevisible; P32246; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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: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; IBA:GO_Central.
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; IPR034321; Chemokine_CCR1_euk.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR10489:SF711; PTHR10489:SF711; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR01106; CHEMOKINER1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
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; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..355
FT /note="C-C chemokine receptor type 1"
FT /id="PRO_0000069228"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..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..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..264
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 337
FT /note="E -> D (in Ref. 3; BAA01723)"
FT /evidence="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
