Adgrf5
entrez
245977
canonical
uniprot
Q9WVT0
canonical
ensembl
ENSRNOG00000011154
resolver
ensembl
ENSRNOG00055020095
resolver
ensembl
ENSRNOG00060021816
resolver
ensembl
ENSRNOG00065023255
resolver
ensp
ENSRNOP00000015223
resolver
ensp
ENSRNOP00000071238
resolver
ensp
ENSRNOP00000096657
resolver
ensp
ENSRNOP00000102120
resolver
ensp
ENSRNOP00055027807
resolver
ensp
ENSRNOP00060031267
resolver
ensp
ENSRNOP00065032401
resolver
enst
ENSRNOT00000015223
resolver
enst
ENSRNOT00000082904
resolver
enst
ENSRNOT00000118179
resolver
enst
ENSRNOT00000135806
resolver
enst
ENSRNOT00055034326
resolver
enst
ENSRNOT00060037919
resolver
enst
ENSRNOT00065039830
resolver
genesymbol
Adgrf5
resolver
genesymbol_syn
Gpr116
resolver
genesymbol_syn
Gprhep
resolver
uniprot
A0A0G2JZZ0
resolver
uniprot
A0A8I6AR34
resolver
uniprot
A0ABK0LF95
resolver
uniprot_entry
A0A0G2JZZ0_RAT
resolver
uniprot_entry
A0A8I6AR34_RAT
resolver
uniprot_entry
A0ABK0LF95_RAT
resolver
uniprot_entry
AGRF5_RAT
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
MKSSRTVTLYFVLIVICSSEATWSRPAEPIVHPLILQEHELAGEELLRPKRAVAVGGPVAEEYTVDVEISFENVSFLESIRAHLNSLRFPVQGNGTDILSMAMTTVCTPTGNDLLCFCEKGYQWPEERCLSSLTCQEHDSALPGRYCNCLKGLPPQGPFCQLPETYITLKIKVRLNIGFQEDLENTSSALYRSYKTDLERAFRAGYRTLPGFRSVTVTQFTKGSVVVDYIVEVASAPLPGSIHKANEQVIQNLNQTYKMDYNSFQGTPSNETKFTVTPEFIFEGDNVTLECESEFVSSNTSWFYGEKRSDIQNSDKFSIHTSIINNISLVTRLTIFNFTQHDAGLYGCNVTLDIFEYGTVRKLDVTPIRILAKEERKVVCDNNPISLNCCSENIANWSRIEWKQEGKINIEGTPETDLESSCSTYTLKADGTQCPSGSSGTTVIYTCEFVSVYGAKGSKNIAVTFTSVANLTITPDPISVSEGQSFSITCLSDVSSFDEVYWNTSAGIKIHPRFYTMRRYRDGAESVLTVKTSTREWNGTYHCIFRYKNSYSIATKDVTVHPLPLESDIMMDPLEASGLCTSSHQFKCCIEENDGEEYIVTFHVDSSSFPAEREVIGKQACYTYSLPGKLPSRCPKDIDVFCHFTNAANSSVRSPSMKLTLVPGKNITCQDPIIGIGEPGKVIQKLCQFAGVSRSPGQTIGGTVTYKCVGSQWKEETRACISAPINGLLQLAKALIKSPSQDQKLPKYLRDLSVSTGKEEQDIRSSPGSLGAIISILDLLSTVPTQVNSEMMRDILATINVILDKSTLNSWEKLLQQQSNQSSQFLQSVERFSKALELGDSTPPFLFHPNVQMKSMVIKRGHAQMYQQKFVFTDSDLWGDVAIDECQLGSLQPDSSIVTVAFPTLKAILAQDGQRKTPSNSLVMTTTVSHNIVKPFRISMTFKNNHRSGGKPQCVFWNFSLANNTGGWDSSGCTVEDDGRDNRDRVFCKCNHLTSFSILMSPDSPDPGSLLKILLDIISYIGLGFSIVSLAACLVVEAMVWKSVTKNRTSYMRHICIVNIALCLLIADIWFIVAGAIHDGHYPLNETACVAATFFIHFFYLSVFFWMLTLGLMLFYRLIFILHDASKSTQKAIAFSLGYGCPLIISSITVGVTQPQEVYMRKNACWLNWEDTRALLAFAIPALIIVVVNVSITVVVITKILRPSVGDKPGKQEKSSLFQISKSIGVLTPLLGLTWGFGLATVIQGSNAVFHIIFTLLNAFQGLFILLFGCLWDQKVQEALLHKFSLSRWSSQHSKSTSLGSSTPVFSMSSPISRRFNNLFGKTGTYNVSTPETTSSSVENSSSAYSLLN
uniprot
proteins
function
FUNCTION: Receptor that plays a critical role in lung surfactant homeostasis. May play a role in controlling adipocyte function. {ECO:0000250|UniProtKB:G5E8Q8}.; FUNCTION: Adhesion G protein-coupled receptor. In alveolar type II (ATII or AT2) cells, required for normal lung surfactant homeostasis. 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. 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. 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. {ECO:0000250|UniProtKB:G5E8Q8}.
uniprot
proteins
mass_dalton
149446
uniprot
proteins
mutagenesis
MUTAGEN 994; /note="T->A: Abolishes cleavage."; /evidence="ECO:0000269|PubMed:11973329
uniprot
proteins
post_translational_modification
PTM: Highly glycosylated. {ECO:0000269|PubMed:10391944, ECO:0000269|PubMed:11973329, ECO:0000269|PubMed:16882675}.; 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:0000269|PubMed:11973329, ECO:0000269|PubMed:16882675}.
uniprot
proteins
protein_family
Adhesion G protein-coupled receptor (ADGR) subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
10391944
uniprot
proteins
pubmed
11973329
uniprot
proteins
pubmed
16641100
uniprot
proteins
pubmed
16882675
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
36073784
uniprot
proteins
sequence_length
1349
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10391944, ECO:0000269|PubMed:16882675}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 1017..1036; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 1056..1078; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 1098..1120; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 1132..1154; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 1174..1196; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 1217..1239; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 1249..1271; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins