FY
entrez
2532
canonical
uniprot
Q16570
canonical
ensembl
ENSG00000213088
resolver
ensp
ENSP00000357103
resolver
ensp
ENSP00000357104
resolver
genesymbol
ACKR1
resolver
genesymbol
FY
resolver
genesymbol_syn
DARC
resolver
genesymbol_syn
FY
resolver
genesymbol_syn
GPD
resolver
hgnc
HGNC:4035
resolver
uniprot
A8YPG5
resolver
uniprot
O75898
resolver
uniprot
Q16300
resolver
uniprot
Q5Y7A1
resolver
uniprot
Q5Y7A2
resolver
uniprot
Q8WWE3
resolver
uniprot
Q9UJP0
resolver
uniprot
Q9UKZ5
resolver
uniprot
Q9UKZ6
resolver
uniprot
Q9UQE1
resolver
uniprot_entry
ACKR1_HUMAN
resolver
uniprot_entry
Q5Y7A1_HUMAN
resolver
uniprot_entry
Q5Y7A2_HUMAN
resolver
uniprot_sec
A8YPG5
resolver
uniprot_sec
O75898
resolver
uniprot_sec
Q16300
resolver
uniprot_sec
Q8WWE3
resolver
uniprot_sec
Q9UJP0
resolver
uniprot_sec
Q9UKZ5
resolver
uniprot_sec
Q9UKZ6
resolver
uniprot_sec
Q9UQE1
resolver
amino_acid_sequence
MGNCLHRAELSPSTENSSQLDFEDVWNSSYGVNDSFPDGDYGANLEAAAPCHSCNLLDDSALPFFILTSVLGILASSTVLFMLFRPLFRWQLCPGWPVLAQLAVGSALFSIVVPVLAPGLGSTRSSALCSLGYCVWYGSAFAQALLLGCHASLGHRLGAGQVPGLTLGLTVGIWGVAALLTLPVTLASGASGGLCTLIYSTELKALQATHTVACLAIFVLLPLGLFGAKGLKKALGMGPGPWMNILWAWFIFWWPHGVVLGLDFLVRSKLLLLSTCLAQQALDLLLNLAEALAILHCVATPLLLALFCHQATRTLLPSLPLPEGWSSHLDTLGSKS
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. Has a promiscuous chemokine-binding profile, interacting with inflammatory chemokines of both the CXC and the CC subfamilies but not with homeostatic chemokines. Acts as a receptor for chemokines including CCL2, CCL5, CCL7, CCL11, CCL13, CCL14, CCL17, CXCL5, CXCL6, IL8/CXCL8, CXCL11, GRO, RANTES, MCP-1 and TARC. May regulate chemokine bioavailability and, consequently, leukocyte recruitment through two distinct mechanisms: when expressed in endothelial cells, it sustains the abluminal to luminal transcytosis of tissue-derived chemokines and their subsequent presentation to circulating leukocytes; when expressed in erythrocytes, serves as blood reservoir of cognate chemokines but also as a chemokine sink, buffering potential surges in plasma chemokine levels.; FUNCTION: (Microbial infection) Acts as a receptor for the malaria parasite Plasmodium vivax. {ECO:0000269|PubMed:38056460}.; FUNCTION: (Microbial infection) Acts as a receptor for the malaria parasite Plasmodium knowlesi. {ECO:0000269|PubMed:28800732}.
uniprot
proteins
mass_dalton
35553
uniprot
proteins
mutagenesis
MUTAGEN 9; /note="E->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 10; /note="L->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 11; /note="S->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 12; /note="P->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 13; /note="S->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 15; /note="E->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 16; /note="N->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 17; /note="S->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 18; /note="S->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 19; /note="Q->A: Modulates the affinity of the interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 20; /note="L->A: Significantly reduces binding with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 21; /note="D->A: Significantly reduces binding with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 22; /note="F->A: Significantly reduces binding with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 23; /note="E->A: Modulates the affinity of the interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 24; /note="D->A: Significantly reduces binding with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 25; /note="V->A: Significantly reduces binding with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 26; /note="W->A: Significantly reduces binding with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 27; /note="N->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 28; /note="S->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 29; /note="S->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 30; /note="Y->A: Does not affect interaction with Plasmodium vivax Duffy receptor (DBP)."; /evidence="ECO:0000269|PubMed:16024106"; MUTAGEN 30; /note="Y->F: Abolishes sulfation. Reduces binding with IL8/CXCL8."; /evidence="ECO:0000269|PubMed:15720550"; MUTAGEN 41; /note="Y->F: Abolishes sulfation. Reduces binding with MGSA/CXCL1, RANTES/CCL5 and MCP-1/CCL2. Reduces binding with Plasmodium vivax Duffy receptor (DBP) and Plasmodium knowlesi Duffy receptor alpha form (DBPalpha)."; /evidence="ECO:0000269|PubMed:15720550
uniprot
proteins
post_translational_modification
PTM: Sulfation at Tyr-41 facilitates interaction with MGSA/CXCL1, RANTES/CCL5 and MCP-1/CCL2 but not IL8/CXCL8 (PubMed:15720550). Sulfation at Tyr-30 facilitates interaction with IL8/CXCL8 (PubMed:15720550). {ECO:0000269|PubMed:15720550}.; PTM: (Microbial infection) Sulfation at Tyr-41 facilitates interaction with Plasmodium vivax Duffy receptor (DBP) (PubMed:15720550). Sulfation at Tyr-30/Tyr-41 and Tyr-41 alone increases binding affinity of Plasmodium vivax parasites and likely promotes invasion of red blood cells (PubMed:37336887). {ECO:0000269|PubMed:15720550, ECO:0000269|PubMed:37336887}.; PTM: (Microbial infection) Sulfation at Tyr-41 facilitates interaction with Plasmodium knowlesi Duffy receptor alpha form (DBPalpha) (PubMed:15720550). Sulfation at Tyr-30/Tyr-41 and Tyr-41 alone increases binding affinity of Plasmodium knowlesi parasites and likely promotes invasion of red blood cells (PubMed:37336887). {ECO:0000269|PubMed:15720550, ECO:0000269|PubMed:37336887}.
uniprot
proteins
protein_family
Atypical chemokine receptor subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10570183
uniprot
proteins
pubmed
11279211
uniprot
proteins
pubmed
12956774
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15720550
uniprot
proteins
pubmed
15720551
uniprot
proteins
pubmed
16024106
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17389925
uniprot
proteins
pubmed
18179887
uniprot
proteins
pubmed
20373092
uniprot
proteins
pubmed
22698181
uniprot
proteins
pubmed
22912641
uniprot
proteins
pubmed
23356288
uniprot
proteins
pubmed
24415938
uniprot
proteins
pubmed
28800732
uniprot
proteins
pubmed
37336887
uniprot
proteins
pubmed
38056460
uniprot
proteins
pubmed
7663520
uniprot
proteins
pubmed
7705836
uniprot
proteins
pubmed
7833467
uniprot
proteins
pubmed
8248172
uniprot
proteins
pubmed
8879225
uniprot
proteins
pubmed
9731074
uniprot
proteins
pubmed
9746760
uniprot
proteins
pubmed
9886340
uniprot
proteins
sequence_length
336
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Early endosome. Recycling endosome. Membrane; Multi-pass membrane protein. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via caveolae. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane.
uniprot
proteins
transmembrane_region
TRANSMEM 64..84; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 96..116; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 130..153; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 167..187; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 208..228; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 245..265; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 288..308; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins