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Atypical chemokine receptor 3 (C-X-C chemokine receptor type 7) (CXC-R7) (CXCR-7) (Chemokine orphan receptor 1) (G-protein coupled receptor RDC1) (RDC-1)

 ACKR3_CANLF             Reviewed;         362 AA.
P11613;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
28-MAR-2018, entry version 136.
RecName: Full=Atypical chemokine receptor 3;
AltName: Full=C-X-C chemokine receptor type 7;
Short=CXC-R7;
Short=CXCR-7;
AltName: Full=Chemokine orphan receptor 1;
AltName: Full=G-protein coupled receptor RDC1;
Short=RDC-1;
Name=ACKR3; Synonyms=CMKOR1, CXCR7, RDC1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thyroid;
PubMed=2541503; DOI=10.1126/science.2541503;
Libert F., Parmentier M., Lefort A., Dinsart C., van Sande J.,
Maenhaut C., Simons M.-J., Dumont J.E., Vassart G.;
"Selective amplification and cloning of four new members of the G
protein-coupled receptor family.";
Science 244:569-572(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thyroid;
PubMed=2159631; DOI=10.1093/nar/18.7.1917;
Libert F., Parmentier M., Lefort A., Dumont J.E., Vassart G.;
"Complete nucleotide sequence of a putative G protein coupled
receptor: RDC1.";
Nucleic Acids Res. 18:1917-1917(1990).
[3]
SHOWS THAT RDC1 IS NOT A VIP RECEPTOR.
PubMed=1373390; DOI=10.1016/0014-5793(92)80184-I;
Cook J.S., Wolsing D.H., Lameh J., Olson C.A., Correa P.E., Sadee W.,
Blumnthal E.M., Rosenbaum J.S.;
"Characterization of the RDC1 gene which encodes the canine homolog of
a proposed human VIP receptor. Expression does not correlate with an
increase in VIP binding sites.";
FEBS Lett. 300:149-152(1992).
-!- FUNCTION: Atypical chemokine receptor that controls chemokine
levels and localization via high-affinity chemokine binding that
is uncoupled from classic ligand-driven signal transduction
cascades, resulting instead in chemokine sequestration,
degradation, or transcytosis. Also known as interceptor
(internalizing receptor) or chemokine-scavenging receptor or
chemokine decoy receptor. Acts as a receptor for chemokines CXCL11
and CXCL12/SDF1. Chemokine binding does not activate G-protein-
mediated signal transduction but instead induces beta-arrestin
recruitment, leading to ligand internalization and activation of
MAPK signaling pathway. Required for regulation of CXCR4 protein
levels in migrating interneurons, thereby adapting their chemokine
responsiveness. In glioma cells, transduces signals via MEK/ERK
pathway, mediating resistance to apoptosis. Promotes cell growth
and survival. Not involved in cell migration, adhesion or
proliferation of normal hematopoietic progenitors but activated by
CXCL11 in malignant hemapoietic cells, leading to phosphorylation
of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration.
Plays a regulatory role in CXCR4-mediated activation of cell
surface integrins by CXCL12. Required for heart valve development
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Can form heterodimers with CXCR4;
heterodimerization may regulate CXCR4 signaling activity (By
similarity). Interacts with ARRB1 and ARRB2 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Cytoplasm, perinuclear region {ECO:0000250}. Early endosome
{ECO:0000250}. Recycling endosome {ECO:0000250}.
Note=Predominantly localizes to endocytic vesicles, and upon
stimulation by the ligand is internalized via clathrin-coated pits
in a beta-arrestin-dependent manner. Once internalized, the ligand
dissociates from the receptor, and is targeted to degradation
while the receptor is recycled back to the cell membrane (By
similarity). {ECO:0000250}.
-!- DOMAIN: The C-terminal cytoplasmic tail, plays a key role in:
correct trafficking to the cell membrane, recruitment of beta-
arrestin, ubiquitination, and in chemokine scavenging and
signaling functions. The Ser/Thr residues and the Lys residues in
the C-terminal cytoplasmic tail are essential for beta-arrestin
recruitment and ubiquitination respectively (By similarity).
{ECO:0000250}.
-!- PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may
be phosphorylated. {ECO:0000250}.
-!- PTM: Ubiquitinated at the Lys residues in its C-terminal
cytoplasmic tail and is essential for correct trafficking from and
to the cell membrane. Deubiquitinated by CXCL12-stimulation in a
reversible manner (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
Atypical chemokine receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00521}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X14048; CAA32206.1; -; mRNA.
PIR; A30341; A30341.
RefSeq; NP_001003281.1; NM_001003281.2.
RefSeq; XP_005635961.1; XM_005635904.2.
RefSeq; XP_005635962.1; XM_005635905.2.
RefSeq; XP_005635963.1; XM_005635906.2.
UniGene; Cfa.3822; -.
ProteinModelPortal; P11613; -.
STRING; 9615.ENSCAFP00000017975; -.
PaxDb; P11613; -.
Ensembl; ENSCAFT00000019378; ENSCAFP00000017975; ENSCAFG00000012206.
GeneID; 403964; -.
KEGG; cfa:403964; -.
CTD; 57007; -.
VGNC; VGNC:37509; ACKR3.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000119055; -.
HOGENOM; HOG000261660; -.
HOVERGEN; HBG106832; -.
InParanoid; P11613; -.
KO; K04304; -.
OMA; YIPFTCQ; -.
OrthoDB; EOG091G091W; -.
TreeFam; TF333489; -.
Reactome; R-CFA-380108; Chemokine receptors bind chemokines.
Reactome; R-CFA-418594; G alpha (i) signalling events.
Proteomes; UP000002254; Chromosome 25.
Bgee; ENSCAFG00000012206; -.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0019958; F:C-X-C chemokine binding; ISS:UniProtKB.
GO; GO:0016494; F:C-X-C chemokine receptor activity; IEA:Ensembl.
GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
GO; GO:0005044; F:scavenger receptor activity; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0006935; P:chemotaxis; IEA:InterPro.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
GO; GO:0001570; P:vasculogenesis; IEA:InterPro.
CDD; cd14987; 7tmA_ACKR3_CXCR7; 1.
InterPro; IPR001416; ACKR3.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR44720; PTHR44720; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR00646; RDC1ORPHANR.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
2: Evidence at transcript level;
Cell adhesion; Cell membrane; Complete proteome; Cytoplasm;
Developmental protein; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 362 Atypical chemokine receptor 3.
/FTId=PRO_0000070100.
TOPO_DOM 1 40 Extracellular. {ECO:0000255}.
TRANSMEM 41 61 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 62 81 Cytoplasmic. {ECO:0000255}.
TRANSMEM 82 102 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 103 118 Extracellular. {ECO:0000255}.
TRANSMEM 119 139 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 140 162 Cytoplasmic. {ECO:0000255}.
TRANSMEM 163 183 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 184 213 Extracellular. {ECO:0000255}.
TRANSMEM 214 234 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 235 252 Cytoplasmic. {ECO:0000255}.
TRANSMEM 253 273 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 274 296 Extracellular. {ECO:0000255}.
TRANSMEM 297 319 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 320 362 Cytoplasmic. {ECO:0000255}.
REGION 324 362 C-terminal cytoplasmic tail.
{ECO:0000250}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:P56485}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000250|UniProtKB:P56485}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000250|UniProtKB:P56485}.
CARBOHYD 13 13 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 22 22 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 117 196 {ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 362 AA; 41416 MW; AA1B288DB9674343 CRC64;
MDLHLFDYAE PGNFSDISWP CNSSDCIVVD TVLCPNMPNK SVLLYTLSFI YIFIFVIGMI
ANSVVVWVNI QAKTTGYDTH CYILNLAIAD LWVVVTIPVW VVSLVQHNQW PMGELTCKIT
HLIFSINLFG SIFFLTCMSV DRYLSITYFA STSSRRKKVV RRAVCVLVWL LAFCVSLPDT
YYLKTVTSAS NNETYCRSFY PEHSVKEWLI SMELVSVVLG FAIPFCVIAV FYCLLARAIS
ASSDQEKQSS RKIIFSYVVV FLVCWLPYHV VVLLDIFSIL HYIPFTCQLE NFLFTALHVT
QCLSLVHCCV NPVLYSFINR NYRYELMKAF IFKYSAKTGL TKLIDASRVS ETEYSALEQN
AK


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