ADGRF5
entrez
221395
canonical
uniprot
Q8IZF2
canonical
ensembl
ENSG00000069122
resolver
ensp
ENSP00000265417
resolver
ensp
ENSP00000283296
resolver
ensp
ENSP00000559004
resolver
ensp
ENSP00000559014
resolver
ensp
ENSP00000559018
resolver
ensp
ENSP00000639061
resolver
ensp
ENSP00000643208
resolver
ensp
ENSP00000643209
resolver
genesymbol
ADGRF5
resolver
genesymbol_syn
GPR116
resolver
genesymbol_syn
KIAA0758
resolver
hgnc
HGNC:19030
resolver
uniprot
O94858
resolver
uniprot
Q5TF06
resolver
uniprot
Q6RGN2
resolver
uniprot
Q86SP0
resolver
uniprot
Q9Y3Z2
resolver
uniprot_entry
AGRF5_HUMAN
resolver
uniprot_sec
O94858
resolver
uniprot_sec
Q5TF06
resolver
uniprot_sec
Q6RGN2
resolver
uniprot_sec
Q86SP0
resolver
uniprot_sec
Q9Y3Z2
resolver
activity_regulation
ACTIVITY REGULATION: As an adhesion G protein-coupled receptor (aGPCR) exhibits a large N-terminal extracellular domain containing highly conserved GPCR autoproteolysis-inducing (GAIN) domain. During synthesis, intracellular autoproteolytic processing of nascent chain within the GAIN domain generates a mature protein, consisting of an N-terminal fragment that is non-covalently linked to the C-terminal fragment. The mature protein is routed to the plasma membrane where the N- and C-terminal fragments remain associated, forming the holoreceptor. Dissociation of the aGPCR fragments stimulates G protein signaling through the action of the tethered-peptide agonist stalk that is occluded within the GAIN domain in the holoreceptor form. This dissociation might be induced by ligand binding, such as that of sFNDC4. {ECO:0000305}.
uniprot
proteins
amino_acid_sequence
MKSPRRTTLCLMFIVIYSSKAALNWNYESTIHPLSLHEHEPAGEEALRQKRAVATKSPTAEEYTVNIEISFENASFLDPIKAYLNSLSFPIHGNNTDQITDILSINVTTVCRPAGNEIWCSCETGYGWPRERCLHNLICQERDVFLPGHHCSCLKELPPNGPFCLLQEDVTLNMRVRLNVGFQEDLMNTSSALYRSYKTDLETAFRKGYGILPGFKGVTVTGFKSGSVVVTYEVKTTPPSLELIHKANEQVVQSLNQTYKMDYNSFQAVTINESNFFVTPEIIFEGDTVSLVCEKEVLSSNVSWRYEEQQLEIQNSSRFSIYTALFNNMTSVSKLTIHNITPGDAGEYVCKLILDIFEYECKKKIDVMPIQILANEEMKVMCDNNPVSLNCCSQGNVNWSKVEWKQEGKINIPGTPETDIDSSCSRYTLKADGTQCPSGSSGTTVIYTCEFISAYGARGSANIKVTFISVANLTITPDPISVSEGQNFSIKCISDVSNYDEVYWNTSAGIKIYQRFYTTRRYLDGAESVLTVKTSTREWNGTYHCIFRYKNSYSIATKDVIVHPLPLKLNIMVDPLEATVSCSGSHHIKCCIEEDGDYKVTFHTGSSSLPAAKEVNKKQVCYKHNFNASSVSWCSKTVDVCCHFTNAANNSVWSPSMKLNLVPGENITCQDPVIGVGEPGKVIQKLCRFSNVPSSPESPIGGTITYKCVGSQWEEKRNDCISAPINSLLQMAKALIKSPSQDEMLPTYLKDLSISIDKAEHEISSSPGSLGAIINILDLLSTVPTQVNSEMMTHVLSTVNVILGKPVLNTWKVLQQQWTNQSSQLLHSVERFSQALQSGDSPPLSFSQTNVQMSSMVIKSSHPETYQQRFVFPYFDLWGNVVIDKSYLENLQSDSSIVTMAFPTLQAILAQDIQENNFAESLVMTTTVSHNTTMPFRISMTFKNNSPSGGETKCVFWNFRLANNTGGWDSSGCYVEEGDGDNVTCICDHLTSFSILMSPDSPDPSSLLGILLDIISYVGVGFSILSLAACLVVEAVVWKSVTKNRTSYMRHTCIVNIAASLLVANTWFIVVAAIQDNRYILCKTACVAATFFIHFFYLSVFFWMLTLGLMLFYRLVFILHETSRSTQKAIAFCLGYGCPLAISVITLGATQPREVYTRKNVCWLNWEDTKALLAFAIPALIIVVVNITITIVVITKILRPSIGDKPCKQEKSSLFQISKSIGVLTPLLGLTWGFGLTTVFPGTNLVFHIIFAILNVFQGLFILLFGCLWDLKVQEALLNKFSLSRWSSQHSKSTSLGSSTPVFSMSSPISRRFNNLFGKTGTYNVSTPEATSSSLENSSSASSLLN
uniprot
proteins
function
FUNCTION: Adhesion G protein-coupled receptor (PubMed:28570277). In alveolar type II (ATII or AT2) cells, required for normal lung surfactant homeostasis (PubMed:28570277). Modulation of both surfactant secretion and uptake by ATII cells is mediated by the downstream activation of GNAQ/GNA11 proteins and may be a consequence of increased cortical F-actin assembly induced by ADGRF5 activation (PubMed:28570277). In the kidney, may play a role in the regulation of acid excretion into the primary urine, possibly by regulating the surface expression of V-ATPase proton pump (By similarity). As a receptor for soluble FNDC4 (sFNDC4), required for proper systemic glucose tolerance, specifically sensitizing white adipose tissue to insulin. Also plays a role in sFNDC4-induced decrease of local inflammation in white adipose tissue (PubMed:34016966). {ECO:0000250|UniProtKB:G5E8Q8, ECO:0000269|PubMed:28570277, ECO:0000269|PubMed:34016966}.
uniprot
proteins
mass_dalton
149457
uniprot
proteins
mutagenesis
MUTAGEN 991..996; /note="Missing: No effect on activation by exogenous ligands, nor on subcellular location. Loss of activation by exogenous ligands; when associated with 1240-I--S-1243. Increased activation by exogenous agonists; when associated with K-l009 or with T-1252 or A-1256."; /evidence="ECO:0000269|PubMed:36073784"; MUTAGEN 1009; /note="G->K: No effect on activation by exogenous agonist. Increased activation by exogenous agonist; when associated with 991-T--L-996 del."; /evidence="ECO:0000269|PubMed:36073784"; MUTAGEN 1075..1077; /note="QDN->HDG: No effect on activation by exogenous agonist."; /evidence="ECO:0000269|PubMed:36073784"; MUTAGEN 1080..1083; /note="ILCK->PLNE: No effect on activation by exogenous agonist."; /evidence="ECO:0000269|PubMed:36073784"; MUTAGEN 1153; /note="R->Q: No effect on activation by exogenous agonist; when associated with M-1157 and A-1161."; /evidence="ECO:0000269|PubMed:36073784"; MUTAGEN 1157; /note="T->M: No effect on activation by exogenous agonist; when associated with Q-1153 and A-1161."; /evidence="ECO:0000269|PubMed:36073784"; MUTAGEN 1161; /note="V->A: No effect on activation by exogenous agonist; when associated with Q-1153 and M-1157."; /evidence="ECO:0000269|PubMed:36073784"; MUTAGEN 1240..1243; /note="FPGT->IQGS: Loss of activation by exogenous ligand; when associated with 991-T--L-996 del."; /evidence="ECO:0000269|PubMed:36073784"; MUTAGEN 1252; /note="A->T: Increased activation by exogenous agonists; when associated with 991-T--L-996 del."; /evidence="ECO:0000269|PubMed:36073784"; MUTAGEN 1256; /note="V->A: Increased activation by exogenous agonists; when associated with 991-T--L-996 del."; /evidence="ECO:0000269|PubMed:36073784
uniprot
proteins
post_translational_modification
PTM: Highly glycosylated. {ECO:0000250|UniProtKB:Q9WVT0}.; PTM: Proteolytically cleaved at multiple sites: one in the GPS region of the GAIN-B domain (S1 site) and the other in the SEA domain (S2 site). The proteolytic cleavage at S1 site generates an extracellular subunit and a seven-transmembrane subunit. The proteolytic cleavage at S2 site generates a fragment that undergoes proteolytic cleavage by the processing enzyme furin. {ECO:0000250|UniProtKB:Q9WVT0}.
uniprot
proteins
protein_family
Adhesion G protein-coupled receptor (ADGR) subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
10048485
uniprot
proteins
pubmed
12435584
uniprot
proteins
pubmed
12679517
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
23590306
uniprot
proteins
pubmed
23684610
uniprot
proteins
pubmed
25713288
uniprot
proteins
pubmed
28570277
uniprot
proteins
pubmed
34016966
uniprot
proteins
pubmed
36073784
uniprot
proteins
sequence_length
1346
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23590306, ECO:0000269|PubMed:23684610}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 1007..1027; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 1054..1074; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 1091..1111; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 1129..1149; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 1174..1194; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 1221..1241; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 1245..1265; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins