ACKR1_MACMU
ID ACKR1_MACMU Reviewed; 335 AA.
AC Q95LF2;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Atypical chemokine receptor 1;
DE AltName: Full=Duffy antigen/chemokine receptor;
DE AltName: CD_antigen=CD234;
GN Name=ACKR1; Synonyms=DARC, FY;
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 [GENOMIC DNA].
RX PubMed=14712331; DOI=10.1007/s00251-003-0633-2;
RA Tournamille C., Blancher A., Le Van Kim C., Gane P., Apoil P.-A.,
RA Nakamoto W., Cartron J.-P., Colin Y.;
RT "Sequence, evolution and ligand binding properties of mammalian Duffy
RT antigen/receptor for chemokines.";
RL Immunogenetics 55:682-694(2004).
CC -!- FUNCTION: Atypical chemokine receptor that controls chemokine levels
CC and localization via high-affinity chemokine binding that is uncoupled
CC from classic ligand-driven signal transduction cascades, resulting
CC instead in chemokine sequestration, degradation, or transcytosis. Also
CC known as interceptor (internalizing receptor) or chemokine-scavenging
CC receptor or chemokine decoy receptor. Has a promiscuous chemokine-
CC binding profile, interacting with inflammatory chemokines of both the
CC CXC and the CC subfamilies but not with homeostatic chemokines. Acts as
CC a receptor for chemokines including CCL2, CCL5, CCL7, CCL11, CCL13,
CC CCL14, CCL17, CXCL5, CXCL6, IL8/CXCL8, CXCL11, GRO, RANTES, MCP-1 and
CC TARC. May regulate chemokine bioavailability and, consequently,
CC leukocyte recruitment through two distinct mechanisms: when expressed
CC in endothelial cells, it sustains the abluminal to luminal transcytosis
CC of tissue-derived chemokines and their subsequent presentation to
CC circulating leukocytes; when expressed in erythrocytes, serves as blood
CC reservoir of cognate chemokines but also as a chemokine sink, buffering
CC potential surges in plasma chemokine levels (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome
CC {ECO:0000250}. Membrane; Multi-pass membrane protein.
CC Note=Predominantly localizes to endocytic vesicles, and upon
CC stimulation by the ligand is internalized via caveolae. Once
CC internalized, the ligand dissociates from the receptor, and is targeted
CC to degradation while the receptor is recycled back to the cell membrane
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Atypical chemokine receptor subfamily. {ECO:0000305}.
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; AF311921; AAL09456.1; -; Genomic_DNA.
DR AlphaFoldDB; Q95LF2; -.
DR SMR; Q95LF2; -.
DR STRING; 9544.ENSMMUP00000001737; -.
DR eggNOG; ENOG502SNW7; Eukaryota.
DR InParanoid; Q95LF2; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0032642; P:regulation of chemokine production; IBA:GO_Central.
DR InterPro; IPR005384; Duffy_chemokine_rcpt.
DR PANTHER; PTHR14181; PTHR14181; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Endosome; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..335
FT /note="Atypical chemokine receptor 1"
FT /id="PRO_0000152586"
FT TOPO_DOM 1..62
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..152
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..275
FT /evidence="ECO:0000250"
FT DISULFID 128..194
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 35378 MW; D0FFB02DBB9A17D7 CRC64;
MGNCLHPAEL SPSTQNSSQL NSDLWNFSYD GNDSFPDVDY DANLEAAAPC HSCNLLDDSA
LPFFILVSVL GILASGTVLF MFFRPLFHWQ LCPGWPVLAQ LAVGSALFSI VVPILAPGLG
NTRSSALCSL GYCVWYGSAF AQALLLGCHA SLGPKLGAGQ VPGLTLGLSV GLWGVAALLT
LPITLASGAS GGLCTPAYSM ELKALQATHA VACLAVFVLL PLGLFGAKGL KKALGMGPGP
WMNILWAWFI FWWPHGVVLG LDFLVRSKLL LLSTCLAQQA LDLLLNLAEA LAILHCVATP
LLLALFCHQA TRTLLPSLPL PEGWSSHLDT LGSES
