ACKR1_BOSIN
ID ACKR1_BOSIN Reviewed; 330 AA.
AC Q863H8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 46.
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 Bos indicus (Zebu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9915;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Marteline M.A., Palmieri D.A., Monteiro J.P., Gimenes M.A., Nakamoto W.;
RT "Identification and sequencing of Bos indicus Duffy gene.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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; AY275716; AAP31577.1; -; Genomic_DNA.
DR AlphaFoldDB; Q863H8; -.
DR SMR; Q863H8; -.
DR Proteomes; UP000515132; Genome assembly.
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; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..330
FT /note="Atypical chemokine receptor 1"
FT /id="PRO_0000253499"
FT TOPO_DOM 1..57
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..147
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..270
FT /evidence="ECO:0000250"
FT DISULFID 123..189
FT /evidence="ECO:0000250"
SQ SEQUENCE 330 AA; 35410 MW; AEE6FB80627792A2 CRC64;
MGNCLYPVAD DNSTKLAIKE DLLIDFPEDY YPDYNETDVE AAAPCHSCSL LNYSSLPFFI
LVSILGILAS GTILYALLRP LFRWQLYQDR STLVQLAVGS ALFSIVVPIL ARGLSGALIT
SLCHLAHLVA YGSAFAQALL IGYHACLGPQ LGAGQVPGLR LGVTVGLWGV AALLSLPVVL
GSDTSQGLCT VTFSGEWETL RYIHAAACFA IFVLLPLGLL GTKGLKTVLG RAPCPWVDVL
WVWFIFWWPQ GMTLGLDSLV RSKAIVVSTC PAQQALDMLL DVAEALAILH CVATPLLLAW
VCYQATHTSP PSLPLPTTQT SHLDTLGSKS
