ID CCR1_MACMU Reviewed; 355 AA.
AC P56482;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 27-MAR-2024, entry version 120.
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; Synonyms=CMKBR1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11461684; DOI=10.1089/088922201750290104;
RA Margulies B.J., Hauer D.A., Clements J.E.;
RT "Identification and comparison of eleven rhesus macaque chemokine
RT receptors.";
RL AIDS Res. Hum. Retroviruses 17:981-986(2001).
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 -!- 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; AF017282; AAB70526.1; -; mRNA.
DR RefSeq; NP_001028030.1; NM_001032858.1.
DR AlphaFoldDB; P56482; -.
DR SMR; P56482; -.
DR STRING; 9544.ENSMMUP00000072210; -.
DR GlyCosmos; P56482; 1 site, No reported glycans.
DR PaxDb; 9544-ENSMMUP00000009854; -.
DR GeneID; 574188; -.
DR KEGG; mcc:574188; -.
DR CTD; 1230; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P56482; -.
DR OrthoDB; 4604454at2759; -.
DR Proteomes; UP000006718; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016493; F:C-C chemokine receptor activity; IBA:GO_Central.
DR GO; GO:0071791; F:chemokine (C-C motif) ligand 5 binding; IBA:GO_Central.
DR GO; GO:0035717; F:chemokine (C-C motif) ligand 7 binding; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISS:UniProtKB.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR002236; Chemokine_CCR1.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR10489:SF711; C-C CHEMOKINE RECEPTOR TYPE 1; 1.
DR PANTHER; PTHR10489; CELL ADHESION MOLECULE; 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 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.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..355
FT /note="C-C chemokine receptor type 1"
FT /id="PRO_0000069230"
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"
SQ SEQUENCE 355 AA; 41199 MW; 41CAEA7CC19D23D4 CRC64;
METPNTTEDY DMITEFDYGD ATPCHKVNER AILAQLLPPL YSLVFVIGVV GNLLVVLVLV
QYKRLKNMTN IYLLNLAISD LLFLFTLPFL IYYKSTDDWI FGDAMCKILS GFYYTGLYSE
IFFIILLTID RYLAIVHAVF ALRARTVTFG VITSIIIWAL AILASSPLMY FSKTQWNIVR
HSCNIHFPYE SFQQWKLFQA LKLNLFGLVL PLLVMIVCYT GIIKILLRRP NEKKSKAVRL
IFVIMIIFFL FWTPYNLTEL ISVFQEFLFT HLCEQNRQLD LAMEVTEVIA NMHCCVNPVI
YAFAGERFRK YLRQLFHRRV AVHLVKWLPF LSGDRLERVS STSPSTGEHE LSAGF
//
