ACKR1_SAPAP
ID ACKR1_SAPAP Reviewed; 336 AA.
AC Q95LF4;
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 Sapajus apella (Brown-capped capuchin) (Cebus apella).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Sapajus.
OX NCBI_TaxID=9515;
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; AF311919; AAL09454.1; -; Genomic_DNA.
DR AlphaFoldDB; Q95LF4; -.
DR SMR; Q95LF4; -.
DR Proteomes; UP000504640; 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: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..336
FT /note="Atypical chemokine receptor 1"
FT /id="PRO_0000152583"
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 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; 35837 MW; 5D2CC35884F7B6F1 CRC64;
MGNCLHQAEL SPSTENSSQL NLEDLWDFPY NGNDSFPEIN YDASLEAAAP CYSCNLLDDS
SLPFFILASV LGILASSTVL FMLFRPLFRW QLCPGWPVLA QLAVGSALFS IVVPILAPGL
GNTRSSALCS LGYCVWYGSA FAQALLLGCH ASLGPKLGAG QVPGLTLGLT VGLWGAAALL
TVPITLASGA SDGLCTPIYS TELKALQATH TVACFAIFVL LPLGLFGAKG VKKALGMGPG
PWMTILWIWF IFWWPHGVVL GLDFLVRSKL LLLPTCLAQQ VLDLLLNLAE ALTIVHCVAT
PLLLALFCHQ ATRTLLPSLP LPERWSSPVD TLGSKS
