ACKR3
entrez
57007
canonical
uniprot
P25106
canonical
ensembl
ENSG00000144476
resolver
ensp
ENSP00000272928
resolver
ensp
ENSP00000599790
resolver
ensp
ENSP00000616152
resolver
ensp
ENSP00000616153
resolver
ensp
ENSP00000616154
resolver
ensp
ENSP00000616155
resolver
ensp
ENSP00000616156
resolver
ensp
ENSP00000616157
resolver
enst
ENST00000272928
resolver
enst
ENST00000929731
resolver
enst
ENST00000946093
resolver
enst
ENST00000946094
resolver
enst
ENST00000946095
resolver
enst
ENST00000946096
resolver
enst
ENST00000946097
resolver
enst
ENST00000946098
resolver
genesymbol
ACKR3
resolver
genesymbol_syn
CMKOR1
resolver
genesymbol_syn
CXCR7
resolver
genesymbol_syn
GPR159
resolver
genesymbol_syn
RDC1
resolver
hgnc
HGNC:23692
resolver
uniprot
A8K6J4
resolver
uniprot
Q53RV4
resolver
uniprot
Q8NE10
resolver
uniprot
Q92938
resolver
uniprot
Q92986
resolver
uniprot_entry
ACKR3_HUMAN
resolver
uniprot_sec
A8K6J4
resolver
uniprot_sec
Q53RV4
resolver
uniprot_sec
Q8NE10
resolver
uniprot_sec
Q92938
resolver
uniprot_sec
Q92986
resolver
amino_acid_sequence
MDLHLFDYSEPGNFSDISWPCNSSDCIVVDTVMCPNMPNKSVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVLTIPVWVVSLVQHNQWPMGELTCKVTHLIFSINLFGSIFFLTCMSVDRYLSITYFTNTPSSRKKMVRRVVCILVWLLAFCVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVVLGFAVPFSIIAVFYFLLARAISASSDQEKHSSRKIIFSYVVVFLVCWLPYHVAVLLDIFSILHYIPFTCRLEHALFTALHVTQCLSLVHCCVNPVLYSFINRNYRYELMKAFIFKYSAKTGLTKLIDASRVSETEYSALEQSTK
uniprot
proteins
disease_involvement
DISEASE: Oculomotor-abducens synkinesis (OCABSN) [MIM:619215]: An autosomal recessive disorder characterized by ptosis and elevation of the eyelid on ipsilateral abduction. OCABSN features are consistent with abnormal innervation of the levator palpebrae superioris muscle, which raises the eyelid, and the lateral rectus muscle, which controls lateral eye movement. {ECO:0000269|PubMed:31211835}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
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 (PubMed:16107333, PubMed:19255243, PubMed:19380869, PubMed:20161793, PubMed:22300987). 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 (PubMed:16940167, PubMed:18653785, PubMed:20018651). Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness (PubMed:16940167, PubMed:18653785). In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival (PubMed:16940167, PubMed:20388803). 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 (PubMed:17804806, PubMed:18653785, PubMed:19641136, PubMed:20887389). Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12 (PubMed:18653785). Required for heart valve development (PubMed:17804806). Regulates axon guidance in the oculomotor system through the regulation of CXCL12 levels (PubMed:31211835). Acts as a receptor for SHLP2, mediating its effects on activation of proopiomelanocortin neurons in the arcuate nucleus of the hypothalamus which leads to suppression of food intake and increased energy expenditure (PubMed:37468558). {ECO:0000269|PubMed:16107333, ECO:0000269|PubMed:16940167, ECO:0000269|PubMed:17804806, ECO:0000269|PubMed:18653785, ECO:0000269|PubMed:19255243, ECO:0000269|PubMed:19380869, ECO:0000269|PubMed:19641136, ECO:0000269|PubMed:20018651, ECO:0000269|PubMed:20161793, ECO:0000269|PubMed:20388803, ECO:0000269|PubMed:20887389, ECO:0000269|PubMed:22300987, ECO:0000269|PubMed:31211835, ECO:0000269|PubMed:37468558}.; FUNCTION: (Microbial infection) Acts as a coreceptor with CXCR4 for a restricted number of HIV isolates. {ECO:0000305|PubMed:23153575}.
uniprot
proteins
mass_dalton
41493
uniprot
proteins
mutagenesis
MUTAGEN 145; /note="S->A: Does not result in CXCL12-inducible chemotaxis, calcium mobilization or ERK activation, and has no effect on CXCR7-mediated CXCL12 degradation; when associated with V-147."; /evidence="ECO:0000269|PubMed:20161793"; MUTAGEN 147; /note="T->V: Does not result in CXCL12-inducible chemotaxis, calcium mobilization or ERK activation, and has no effect on CXCR7-mediated CXCL12 degradation; when associated with A-145."; /evidence="ECO:0000269|PubMed:20161793
uniprot
proteins
post_translational_modification
PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated. {ECO:0000269|PubMed:22457824}.; 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. {ECO:0000269|PubMed:22457824}.
uniprot
proteins
protein_family
Atypical chemokine receptor subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
1315461
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16107333
uniprot
proteins
pubmed
16455976
uniprot
proteins
pubmed
1675791
uniprot
proteins
pubmed
16940167
uniprot
proteins
pubmed
17804806
uniprot
proteins
pubmed
18653785
uniprot
proteins
pubmed
19255243
uniprot
proteins
pubmed
19380869
uniprot
proteins
pubmed
19641136
uniprot
proteins
pubmed
20018651
uniprot
proteins
pubmed
20161793
uniprot
proteins
pubmed
20373092
uniprot
proteins
pubmed
20388803
uniprot
proteins
pubmed
20887389
uniprot
proteins
pubmed
21655198
uniprot
proteins
pubmed
22300987
uniprot
proteins
pubmed
22457824
uniprot
proteins
pubmed
22698181
uniprot
proteins
pubmed
23153575
uniprot
proteins
pubmed
23356288
uniprot
proteins
pubmed
27238288
uniprot
proteins
pubmed
31211835
uniprot
proteins
pubmed
37468558
uniprot
proteins
sequence_length
362
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31211835}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:22457824}. Recycling endosome {ECO:0000269|PubMed:22457824}. 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. {ECO:0000269|PubMed:22457824}.
uniprot
proteins
transmembrane_region
TRANSMEM 41..61; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 82..102; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 119..139; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 163..183; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 214..234; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 253..273; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 297..319; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins