ADGRF1
entrez
266977
canonical
uniprot
Q5T601
canonical
ensembl
ENSG00000153292
resolver
ensp
ENSP00000283297
resolver
ensp
ENSP00000360289
resolver
ensp
ENSP00000360299
resolver
genesymbol
ADGRF1
resolver
genesymbol
GPR110
resolver
genesymbol_syn
GPR110
resolver
genesymbol_syn
PGR19
resolver
hgnc
HGNC:18990
resolver
uniprot
Q3SXM8
resolver
uniprot
Q5KU15
resolver
uniprot
Q5T5Z9
resolver
uniprot
Q5T600
resolver
uniprot
Q86SM1
resolver
uniprot
Q8IXE3
resolver
uniprot
Q8IZF8
resolver
uniprot
Q96DQ1
resolver
uniprot
Q9H615
resolver
uniprot_entry
AGRF1_HUMAN
resolver
uniprot_entry
Q3SXM8_HUMAN
resolver
uniprot_sec
Q5KU15
resolver
uniprot_sec
Q5T5Z9
resolver
uniprot_sec
Q5T600
resolver
uniprot_sec
Q86SM1
resolver
uniprot_sec
Q8IXE3
resolver
uniprot_sec
Q8IZF8
resolver
uniprot_sec
Q96DQ1
resolver
uniprot_sec
Q9H615
resolver
activity_regulation
ACTIVITY REGULATION: Forms a heterodimer of 2 chains generated by proteolytic processing that remain associated through non-covalent interactions mediated by the GAIN-B domain (By similarity). In the inactivated receptor, the Stachel sequence (also named stalk) is embedded in the GAIN-B domain, where it adopts a beta-strand conformation (PubMed:35418679). On activation, the Stachel moves into the 7 transmembrane region and adopts a twisted hook-shaped configuration that forms contacts within the receptor, leading to coupling of a G-alpha protein, which activates signaling (PubMed:35418679). The cleaved GAIN-B and N-terminal domains can then dissociate from the rest of the receptor (PubMed:35418679). {ECO:0000255|PROSITE-ProRule:PRU00098, ECO:0000269|PubMed:35418679}.
uniprot
proteins
amino_acid_sequence
MKVGVLWLISFFTFTDGHGGFLGKNDGIKTKKELIVNKKKHLGPVEEYQLLLQVTYRDSKEKRDLRNFLKLLKPPLLWSHGLIRIIRAKATTDCNSLNGVLQCTCEDSYTWFPPSCLDPQNCYLHTAGALPSCECHLNNLSQSVNFCERTKIWGTFKINERFTNDLLNSSSAIYSKYANGIEIQLKKAYERIQGFESVQVTQFRNGSIVAGYEVVGSSSASELLSAIEHVAEKAKTALHKLFPLEDGSFRVFGKAQCNDIVFGFGSKDDEYTLPCSSGYRGNITAKCESSGWQVIRETCVLSLLEELNKNFSMIVGNATEAAVSSFVQNLSVIIRQNPSTTVGNLASVVSILSNISSLSLASHFRVSNSTMEDVISIADNILNSASVTNWTVLLREEKYASSRLLETLENISTLVPPTALPLNFSRKFIDWKGIPVNKSQLKRGYSYQIKMCPQNTSIPIRGRVLIGSDQFQRSLPETIISMASLTLGNILPVSKNGNAQVNGPVISTVIQNYSINEVFLFFSKIESNLSQPHCVFWDFSHLQWNDAGCHLVNETQDIVTCQCTHLTSFSILMSPFVPSTIFPVVKWITYVGLGISIGSLILCLIIEALFWKQIKKSQTSHTRRICMVNIALSLLIADVWFIVGATVDTTVNPSGVCTAAVFFTHFFYLSLFFWMLMLGILLAYRIILVFHHMAQHLMMAVGFCLGYGCPLIISVITIAVTQPSNTYKRKDVCWLNWSNGSKPLLAFVVPALAIVAVNFVVVLLVLTKLWRPTVGERLSRDDKATIIRVGKSLLILTPLLGLTWGFGIGTIVDSQNLAWHVIFALLNAFQGFFILCFGILLDSKLRQLLFNKLSALSSWKQTEKQNSSDLSAKPKFSKPFNPLQNKGHYAFSHTGDSSDNIMLTQFVSNE
uniprot
proteins
function
FUNCTION: Adhesion G protein-coupled receptor (aGPCR) for N-docosahexaenoylethanolamine (synaptamide), an omega-3 fatty acid lipid highly enriched in the brain (PubMed:27759003, PubMed:32144388). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:35418679, PubMed:36127364, PubMed:37120430). ADGRF1 is coupled to G(s) G proteins and mediates activation of adenylate cyclase activity (PubMed:35418679). Also able to couple to G(q), G(i) and G(12)/G(13) G proteins; additional evidence is however required to confirm this result in vivo (PubMed:36127364, PubMed:37120430). Involved in the development of neurons and cognitive function (By similarity). In liver, involved in fat accumulation (By similarity). {ECO:0000250|UniProtKB:Q8VEC3, ECO:0000269|PubMed:27759003, ECO:0000269|PubMed:32144388, ECO:0000269|PubMed:35418679, ECO:0000269|PubMed:36127364, ECO:0000269|PubMed:37120430}.
uniprot
proteins
mass_dalton
101365
uniprot
proteins
mutagenesis
MUTAGEN 310; /note="N->Q: No effect."; /evidence="ECO:0000269|PubMed:36716818"; MUTAGEN 389; /note="N->S: Decreased expression."; /evidence="ECO:0000269|PubMed:36716818"; MUTAGEN 565..567; /note="HLT->ALA: Abolished autprocessing, impairing G protein-coupled signaling."; /evidence="ECO:0000269|PubMed:27759003"; MUTAGEN 569; /note="F->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679, ECO:0000269|PubMed:36127364, ECO:0000269|PubMed:37120430"; MUTAGEN 570; /note="S->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36127364"; MUTAGEN 572; /note="L->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679, ECO:0000269|PubMed:36127364, ECO:0000269|PubMed:37120430"; MUTAGEN 573; /note="M->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679, ECO:0000269|PubMed:36127364, ECO:0000269|PubMed:37120430"; MUTAGEN 589; /note="T->A: Decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36127364"; MUTAGEN 627; /note="M->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 630; /note="I->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36127364"; MUTAGEN 672; /note="F->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 675; /note="M->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679, ECO:0000269|PubMed:36127364"; MUTAGEN 678; /note="L->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 681; /note="L->A,H: Retains G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 682; /note="L->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 683; /note="A->G: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 729; /note="R->A: Decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36127364"; MUTAGEN 755; /note="V->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 761; /note="V->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 764; /note="L->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 765; /note="V->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 798; /note="P->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 799; /note="L->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679, ECO:0000269|PubMed:36127364"; MUTAGEN 800; /note="L->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679, ECO:0000269|PubMed:36127364"; MUTAGEN 801; /note="G->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 804; /note="W->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 820; /note="H->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36127364"; MUTAGEN 830; /note="Q->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 831; /note="G->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:35418679"; MUTAGEN 834; /note="I->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36127364
uniprot
proteins
post_translational_modification
PTM: Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity. {ECO:0000255|PROSITE-ProRule:PRU00098}.; PTM: Glycosylated (PubMed:20149256). Glycosylation at Asn-389 is required for secretion or folding (PubMed:36716818). {ECO:0000269|PubMed:20149256, ECO:0000269|PubMed:36716818}.
uniprot
proteins
protein_family
Adhesion G protein-coupled receptor (ADGR) subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
12435584
uniprot
proteins
pubmed
12679517
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
20149256
uniprot
proteins
pubmed
25713288
uniprot
proteins
pubmed
27759003
uniprot
proteins
pubmed
32144388
uniprot
proteins
pubmed
35418679
uniprot
proteins
pubmed
36127364
uniprot
proteins
pubmed
36716818
uniprot
proteins
pubmed
37120430
uniprot
proteins
sequence_length
910
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20149256, ECO:0000269|PubMed:27759003}; Multi-pass membrane protein {ECO:0000269|PubMed:35418679}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:20149256}.
uniprot
proteins
transmembrane_region
TRANSMEM 584..609; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:35418679, ECO:0007744|PDB:7WU3, ECO:0007744|PDB:7WU4, ECO:0007744|PDB:7WU5"; TRANSMEM 622..646; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:35418679, ECO:0007744|PDB:7WU3, ECO:0007744|PDB:7WU4, ECO:0007744|PDB:7WU5"; TRANSMEM 659..684; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:35418679, ECO:0007744|PDB:7WU3, ECO:0007744|PDB:7WU4, ECO:0007744|PDB:7WU5"; TRANSMEM 697..719; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:35418679, ECO:0007744|PDB:7WU3, ECO:0007744|PDB:7WU4, ECO:0007744|PDB:7WU5"; TRANSMEM 743..767; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:35418679, ECO:0007744|PDB:7WU3, ECO:0007744|PDB:7WU4, ECO:0007744|PDB:7WU5"; TRANSMEM 785..813; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:35418679, ECO:0007744|PDB:7WU3, ECO:0007744|PDB:7WU4, ECO:0007744|PDB:7WU5"; TRANSMEM 817..842; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:35418679, ECO:0007744|PDB:7WU3, ECO:0007744|PDB:7WU4, ECO:0007744|PDB:7WU5
uniprot
proteins