CCR1_MACFA
ID CCR1_MACFA Reviewed; 355 AA.
AC Q2Y2P0;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
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: CD_antigen=CD191;
GN Name=CCR1;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16204626; DOI=10.1189/jlb.0605326;
RA Gupta S., Schulz-Maronde S., Kutzleb C., Richter R., Forssmann W.-G.,
RA Kapp A., Forssmann U., Elsner J.;
RT "Cloning, expression, and functional characterization of cynomolgus monkey
RT (Macaca fascicularis) CC chemokine receptor 1.";
RL J. Leukoc. Biol. 78:1175-1184(2005).
CC -!- FUNCTION: Receptor for a C-C type chemokine. Binds to MIP-1-alpha,
CC RANTES, MCP-3 and, less efficiently, to MIP-1-beta or MCP-1 and
CC subsequently transduces a signal by increasing the intracellular
CC calcium ions level. Responsible for affecting stem cell proliferation
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CREB3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; DQ008589; AAY56400.1; -; mRNA.
DR RefSeq; NP_001306311.1; NM_001319382.1.
DR AlphaFoldDB; Q2Y2P0; -.
DR SMR; Q2Y2P0; -.
DR STRING; 9541.XP_005546953.1; -.
DR Ensembl; ENSMFAT00000091704; ENSMFAP00000051990; ENSMFAG00000051272.
DR Ensembl; ENSMFAT00000094321; ENSMFAP00000055480; ENSMFAG00000051272.
DR GeneID; 102137577; -.
DR CTD; 1230; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230359; -.
DR Proteomes; UP000233100; Chromosome 2.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016493; F:C-C chemokine receptor activity; IEA:Ensembl.
DR GO; GO:0071791; F:chemokine (C-C motif) ligand 5 binding; IEA:Ensembl.
DR GO; GO:0035717; F:chemokine (C-C motif) ligand 7 binding; IEA:Ensembl.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:Ensembl.
DR GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR GO; GO:0030502; P:negative regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..355
FT /note="C-C chemokine receptor type 1"
FT /id="PRO_0000069229"
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 DISULFID 106..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 355 AA; 41165 MW; F56695FE80E2EE51 CRC64;
METPDTTENY DMITEFDYGD ATPCHKVNER AILAQLLPPL YSLVFVIGVV GNLLVVLVLV
QYKRLKNMTN IYLLNLAISD LLFLFTLPFL IYYKSTDDWI FGDAMCKILS GFYYTGLYSE
IFFIILLTID RYLAIVHAVF ALRARTVTFG VITSIIIWAL AILASSPLMY FSKTQWNIVR
HSCNLHFPYE SFQQWKLFQA LKLNLFGLVL PLLVMIVCYT GIIKILLRRP NEKKSKAVRL
IFVIMIIFFL FWTPYNLTEL ISVFQEFLFT HLCEQNRQLD LAMEVTEVIA NMHCCVNPVI
YAFAGERFRK YLRQLFHRRV AVHLVKWLPF LSGDRLERVS STSPSTGEHE LSAGL
