ADGRG5
entrez
221188
canonical
uniprot
Q8IZF4
canonical
ensembl
ENSG00000159618
resolver
ensp
ENSP00000290823
resolver
ensp
ENSP00000342981
resolver
ensp
ENSP00000567168
resolver
ensp
ENSP00000757126
resolver
enst
ENST00000340339
resolver
enst
ENST00000349457
resolver
enst
ENST00000897109
resolver
genesymbol
ADGRG5
resolver
genesymbol_syn
GPR114
resolver
genesymbol_syn
PGR27
resolver
hgnc
HGNC:19010
resolver
uniprot
A0A024R6S3
resolver
uniprot
A8K9R8
resolver
uniprot
B3KXZ5
resolver
uniprot
B4E148
resolver
uniprot
Q6ZMH7
resolver
uniprot
Q6ZML4
resolver
uniprot
Q86SL8
resolver
uniprot
Q8IZ14
resolver
uniprot_entry
AGRG5_HUMAN
resolver
uniprot_entry
B4E148_HUMAN
resolver
uniprot_sec
A0A024R6S3
resolver
uniprot_sec
A8K9R8
resolver
uniprot_sec
B3KXZ5
resolver
uniprot_sec
Q6ZMH7
resolver
uniprot_sec
Q6ZML4
resolver
uniprot_sec
Q86SL8
resolver
uniprot_sec
Q8IZ14
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 (PubMed:35418678). 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:35418678). 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:35418678). The cleaved GAIN-B and N-terminal domains can then dissociate from the rest of the receptor (PubMed:35418678). {ECO:0000269|PubMed:35418678}.
uniprot
proteins
amino_acid_sequence
MDHCGALFLCLCLLTLQNATTETWEELLSYMENMQVSRGRSSVFSSRQLHQLEQMLLNTSFPGYNLTLQTPTIQSLAFKLSCDFSGLSLTSATLKRVPQAGGQHARGQHAMQFPAELTRDACKTRPRELRLICIYFSNTHFFKDENNSSLLNNYVLGAQLSHGHVNNLRDPVNISFWHNQSLEGYTLTCVFWKEGARKQPWGGWSPEGCRTEQPSHSQVLCRCNHLTYFAVLMQLSPALVPAELLAPLTYISLVGCSISIVASLITVLLHFHFRKQSDSLTRIHMNLHASVLLLNIAFLLSPAFAMSPVPGSACTALAAALHYALLSCLTWMAIEGFNLYLLLGRVYNIYIRRYVFKLGVLGWGAPALLVLLSLSVKSSVYGPCTIPVFDSWENGTGFQNMSICWVRSPVVHSVLVMGYGGLTSLFNLVVLAWALWTLRRLRERADAPSVRACHDTVTVLGLTVLLGTTWALAFFSFGVFLLPQLFLFTILNSLYGFFLFLWFCSQRCRSEAEAKAQIEAFSSSQTTQ
uniprot
proteins
function
FUNCTION: Orphan adhesion G protein-coupled receptor (aGPCR) (PubMed:37673336). 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:37673336). ADGRG5 is specifically coupled to G(s) G proteins and mediates activation of adenylate cyclase activity (PubMed:37673336). {ECO:0000269|PubMed:37673336}.
uniprot
proteins
mass_dalton
59000
uniprot
proteins
mutagenesis
MUTAGEN 225; /note="H->S: Abolished autoproteolytically processing."; /evidence="ECO:0000269|PubMed:37673336"; MUTAGEN 230; /note="A->M: Impaired G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:37673336
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, ECO:0000269|PubMed:37673336}.; PTM: N-glycsylated. {ECO:0000269|PubMed:37673336}.
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
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21724806
uniprot
proteins
pubmed
25713288
uniprot
proteins
pubmed
35418678
uniprot
proteins
pubmed
37673336
uniprot
proteins
sequence_length
528
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q3V3Z3}; Multi-pass membrane protein {ECO:0000269|PubMed:35418678}.
uniprot
proteins
transmembrane_region
TRANSMEM 246..271; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:35418678, ECO:0007744|PDB:7EQ1"; TRANSMEM 281..304; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:35418678, ECO:0007744|PDB:7EQ1"; TRANSMEM 315..340; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:35418678, ECO:0007744|PDB:7EQ1"; TRANSMEM 354..377; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:35418678, ECO:0007744|PDB:7EQ1"; TRANSMEM 411..435; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:35418678, ECO:0007744|PDB:7EQ1"; TRANSMEM 456..477; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:35418678, ECO:0007744|PDB:7EQ1"; TRANSMEM 482..505; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:35418678, ECO:0007744|PDB:7EQ1
uniprot
proteins