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ACKR1_BOVIN
ID   ACKR1_BOVIN             Reviewed;         330 AA.
AC   Q9GLX0; A5PKF0; Q5E941;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   25-MAY-2022, entry version 96.
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 taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tournamille C., Colin Y.;
RT   "Bovine DARC gene.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) 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; AF109158; AAG31021.1; -; Genomic_DNA.
DR   EMBL; BT021079; AAX09096.1; -; mRNA.
DR   EMBL; BC142464; AAI42465.1; -; mRNA.
DR   RefSeq; NP_001015634.1; NM_001015634.1.
DR   AlphaFoldDB; Q9GLX0; -.
DR   SMR; Q9GLX0; -.
DR   STRING; 9913.ENSBTAP00000004179; -.
DR   PaxDb; Q9GLX0; -.
DR   GeneID; 528076; -.
DR   KEGG; bta:528076; -.
DR   CTD; 2532; -.
DR   eggNOG; ENOG502SNW7; Eukaryota.
DR   InParanoid; Q9GLX0; -.
DR   OrthoDB; 1194550at2759; -.
DR   Proteomes; UP000009136; 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   2: Evidence at transcript level;
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_0000152582"
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"
FT   CONFLICT        150
FT                   /note="Q -> R (in Ref. 1; AAG31021)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        328
FT                   /note="G -> S (in Ref. 1; AAG31021)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   330 AA;  35414 MW;  7AA0064485C21F17 CRC64;
     MGNCLYPVAD DNSTKLAIKE DFLIDFPEDY 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 SHLDTLGGKS
 
 
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