ACKR4_BOVIN
ID ACKR4_BOVIN Reviewed; 350 AA.
AC P35350; A5PJM3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Atypical chemokine receptor 4;
DE AltName: Full=C-C chemokine receptor type 11;
DE Short=C-C CKR-11;
DE Short=CC-CKR-11;
DE Short=CCR-11;
DE AltName: Full=CC chemokine receptor-like 1;
DE AltName: Full=Protein PPR1;
DE AltName: Full=Putative gustatory receptor type B;
GN Name=ACKR4; Synonyms=CCR11, CCRL1;
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 [MRNA].
RC TISSUE=Tongue;
RX PubMed=8392843; DOI=10.1006/bbrc.1993.1848;
RA Matsuoka I., Mori T., Aoki J., Sato T., Kurihara K.;
RT "Identification of novel members of G-protein coupled receptor superfamily
RT expressed in bovine taste tissue.";
RL Biochem. Biophys. Res. Commun. 194:504-511(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
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. Acts as a receptor for chemokines
CC CCL2, CCL8, CCL13, CCL19, CCL21 and CCL25. Chemokine-binding does not
CC activate G-protein-mediated signal transduction but instead induces
CC beta-arrestin recruitment, leading to ligand internalization. Plays an
CC important role in controlling the migration of immune and cancer cells
CC that express chemokine receptors CCR7 and CCR9, by reducing the
CC availability of CCL19, CCL21, and CCL25 through internalization.
CC Negatively regulates CXCR3-induced chemotaxis. Regulates T-cell
CC development in the thymus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms heteromers with CXCR3. Interacts with ARRB1 and ARRB2
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome
CC {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Note=Predominantly localizes to endocytic vesicles, and
CC upon 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 -!- TISSUE SPECIFICITY: Expressed in circumvallate and fungiform papillae,
CC olfactory epithelium and lung. Lower expression in liver, kidney and
CC tongue epithelium bearing no taste papillae. Very low expression in the
CC cerebral cortex of the brain.
CC -!- PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may be
CC phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Atypical chemokine receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00521}.
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; S63848; AAB27547.1; -; mRNA.
DR EMBL; BC142169; AAI42170.1; -; mRNA.
DR PIR; JN0621; JN0621.
DR RefSeq; NP_776690.1; NM_174265.2.
DR RefSeq; XP_015328974.1; XM_015473488.1.
DR AlphaFoldDB; P35350; -.
DR SMR; P35350; -.
DR STRING; 9913.ENSBTAP00000026082; -.
DR PaxDb; P35350; -.
DR Ensembl; ENSBTAT00000026082; ENSBTAP00000026082; ENSBTAG00000019577.
DR GeneID; 281672; -.
DR KEGG; bta:281672; -.
DR CTD; 51554; -.
DR VEuPathDB; HostDB:ENSBTAG00000019577; -.
DR VGNC; VGNC:25542; ACKR4.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234667; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P35350; -.
DR OMA; YNVVKLC; -.
DR OrthoDB; 839817at2759; -.
DR TreeFam; TF330966; -.
DR Reactome; R-BTA-380108; Chemokine receptors bind chemokines.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000019577; Expressed in tongue muscle and 78 other tissues.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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:0016493; F:C-C chemokine receptor activity; IBA:GO_Central.
DR GO; GO:0004950; F:chemokine receptor activity; ISS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR InterPro; IPR005383; ACKR4.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR01558; CHEMOKINER11.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endosome; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="Atypical chemokine receptor 4"
FT /id="PRO_0000069295"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..306
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 350 AA; 40008 MW; E46BF942F3919C82 CRC64;
MAVEYNQSTD YYYEENEMND THDYSQYEVI CIKEEVRKFA KVFLPAFFTI AFIIGLAGNS
TVVAIYAYYK KRRTKTDVYI LNLAVADLFL LFTLPFWAVN AVHGWVLGKI MCKVTSALYT
VNFVSGMQFL ACISTDRYWA VTKAPSQSGV GKPCWVICFC VWVAAILLSI PQLVFYTVNH
KARCVPIFPY HLGTSMKASI QILEICIGFI IPFLIMAVCY FITAKTLIKM PNIKKSQPLK
VLFTVVIVFI VTQLPYNIVK FCQAIDIIYS LITDCDMSKR MDVAIQITES IALFHSCLNP
VLYVFMGTSF KNYIMKVAKK YGSWRRQRQN VEEIPFESED ATEPTSTFSI
