ACKR1_PAPHA
ID ACKR1_PAPHA Reviewed; 336 AA.
AC Q95LG5;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 65.
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 Papio hamadryas (Hamadryas baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9557;
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}.
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DR EMBL; AF303532; AAL09324.1; -; Genomic_DNA.
DR AlphaFoldDB; Q95LG5; -.
DR SMR; Q95LG5; -.
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:0019956; F:chemokine binding; IEA:InterPro.
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; IEA:InterPro.
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; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..336
FT /note="Atypical chemokine receptor 1"
FT /id="PRO_0000152589"
FT TOPO_DOM 1..63
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..276
FT /evidence="ECO:0000250"
FT DISULFID 129..195
FT /evidence="ECO:0000250"
SQ SEQUENCE 336 AA; 35604 MW; EBA5DADB812DB685 CRC64;
MGNCLHPAEL SPSTQNSSQL NSEDLWNFSY DGNDSFPDVD YDANLEAAAP CHSCNLLDDS
ALPFFILVSV LGILASGIVL FMFFRPLFHW QLCPGWPVLA QLAVGSALFS IVVPILAPGL
GNTRSSALCS LGYCVWYGSA FAQALLLGCH ASLGPKLGAD QVPGLTLGLS VGLWGVAALL
TLPVTLASGA SGGLCTPVYS MELKALQATH AVACLAIFVL LPLGLFGAKG LKKALGMGPG
PWMNILWAWF IFWWPHGVVL GLDFLVRSKL LLLSTCLAQQ ALDLLLNLAE ALAILHCVAT
PLLLALFCHQ ATRTLLPSLP LPEGWSSHLD TLGSKS
