Adgrg6
entrez
215798
canonical
uniprot
Q6F3F9
canonical
ensembl
ENSMUSG00000039116
resolver
ensp
ENSMUSP00000043055
resolver
ensp
ENSMUSP00000146821
resolver
ensp
ENSMUSP00000158717
resolver
ensp
ENSMUSP00000282993
resolver
enst
ENSMUST00000041168
resolver
enst
ENSMUST00000238680
resolver
genesymbol
Adgrg6
resolver
genesymbol_syn
Dreg
resolver
genesymbol_syn
Gm222
resolver
genesymbol_syn
Gpr126
resolver
uniprot
A0A571BEJ4
resolver
uniprot
Q811E4
resolver
uniprot_entry
A0A571BEJ4_MOUSE
resolver
uniprot_entry
AGRG6_MOUSE
resolver
uniprot_sec
Q811E4
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. In the inactivated receptor, the Stachel sequence (also named stalk) is embedded in the GAIN-B domain, where it adopts a beta-strand conformation. 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. The cleaved GAIN-B and N-terminal domains can then dissociate from the rest of the receptor. {ECO:0000250|UniProtKB:Q8IZF4}.
uniprot
proteins
amino_acid_sequence
MMFDTLGKRCCPWRLKPSALLFLFVLCVTCVPLSVCGCGSCRLVLSNPSGTFTSPCYPNDYPNTQSCSWTLRAPAGYIIQITFNDFDIEEAPNCIYDSLSLDNGESQTKFCGATAKGLSFNSSVNEMHVSFSSDFSIQKKGFNASYIRVAVSLRNQKVILPQTLDAYQVSVAKSISIPELKAFTLCFEASKVGNEGGDWTAFSYSDESLTQLLSLEKASNGYFLSISGSRCLLNNALPVKDKEDIFTENLEQLCLVWNNSWGSIGINFKKNYETVPCDSTISAVVPGDGTLLLGSDRDEVASLRGSIYNFRLWNFTMDLKALSNLSCSVSGNVIDWHNDFWSISTQALKAEGNLSCGSYLIQLPAAELTNCSELGTLCQDGIMYRISVVIHNDFNHPEVKVQTKVAEWLNSTFQNWNYTVYVVNISFHQKVGEDRMKVKRDIMDDDKRLVLWALLVYNATNNVSLNEEKIKQKLMTNNASLEDGLRLCEVDVNQLGMCSALEDPDGFSWPATLPSVYKQPCPNKPGFFMTRACLSNGTSTFWGPVDTSNCSRQSNEVANEILNQTGDGQNLTSANINSIVEKVKRIVNKEENIDITLGSTLMNIFSNILSSSDSDLLESSTEALKTIDELAFKIDLNSTPHVNIETQNLALGVSSLIPGTNAPSNFSIGLPSNNESYFQMDFGNGQTDPLASVILPPNLLENLSPEDSVLVRRAQFTFFNKTGLFQDVGSQRKVLVSYVMACSIGNITIQNLKDPVQIKIKHTRTQEVHHPICAFWDMNKNKSFGGWNTSGCVAHSDLDAGETICLCSHFTHFGVLMDLPRSASQIDGRNTKVLTFITYIGCGISAIFSAATLLTYVAFEKLRRDYPSKILMNLSSALLFLNLIFLLDGWVTSFGVAGLCTAVAALLHFFLLATFTWMGLEAIHMYIALVKVFNTYIHRYILKFCIIGWGLPALVVSIILVSRRQNEVYGKESYGKDQDDEFCWIQDPVVFYVSCAGYFGVMFFLNVAMFIVVMVQICGRNGKRSNRTLREEVLRNLRSVVSLTFLLGMTWGFAFFAWGPLNIPFMYLFSIFNSLQGLFIFIFHCAMKENVQKQWRRHLCCGRFRLADNSDWSKTATNIIKKSSDNLGKSLSSSSIGSNSTYLTSKSKSSSTTYFKRNSHSDNFS
uniprot
proteins
function
FUNCTION: Adhesion G protein-coupled receptor (aGPCR) for steroid hormones, such as progesterone and 17alpha-hydroxyprogesterone (17OHP) (By similarity). Involved in many biological processes, such as myelination, sprouting angiogenesis, placenta, ear and cartilage development (PubMed:21613327, PubMed:24082093, PubMed:24227709, PubMed:25217645, PubMed:25695270, PubMed:25954032, PubMed:27501152, PubMed:34767447). 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 (By similarity). ADGRG6 is coupled to G(i) G alpha proteins and mediates inhibition of adenylate cyclase (By similarity). Also able to couple to G(q) G proteins (By similarity). Involved in myelination of the peripheral nervous system: required for differentiation of promyelinating Schwann cells and for normal myelination of axons (PubMed:21613327, PubMed:24227709, PubMed:27927955). Also acts as a regulator of body length and bone mass (PubMed:32219165). Acts as a regulator of blood-brain barrier formation in the central nervous system vie its association with LRP1 and ITGB1 (PubMed:39087467). {ECO:0000250|UniProtKB:Q86SQ4, ECO:0000269|PubMed:21613327, ECO:0000269|PubMed:24082093, ECO:0000269|PubMed:24227709, ECO:0000269|PubMed:25217645, ECO:0000269|PubMed:25695270, ECO:0000269|PubMed:25954032, ECO:0000269|PubMed:27501152, ECO:0000269|PubMed:27927955, ECO:0000269|PubMed:32219165, ECO:0000269|PubMed:34767447, ECO:0000269|PubMed:39087467}.
uniprot
proteins
mass_dalton
129721
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved into 2 conserved sites: one in the GPS region of the GAIN-B domain (S1 site) and the other in the middle of the extracellular domain (S2 site). The proteolytic cleavage at S1 site generates an extracellular subunit and a seven-transmembrane subunit. Furin is involved in the cleavage of the S2 site generating a soluble fragment. Processing at the GPS region occurred independent of and probably prior to the cleavage at the S2 site. Proteolytic cleavage is required for activation of the receptor. {ECO:0000250|UniProtKB:Q86SQ4}.
uniprot
proteins
protein_family
Adhesion G protein-coupled receptor (ADGR) subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
15189448
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19656770
uniprot
proteins
pubmed
21124978
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21613327
uniprot
proteins
pubmed
24082093
uniprot
proteins
pubmed
24227709
uniprot
proteins
pubmed
25217645
uniprot
proteins
pubmed
25695270
uniprot
proteins
pubmed
25954032
uniprot
proteins
pubmed
27501152
uniprot
proteins
pubmed
27927955
uniprot
proteins
pubmed
32219165
uniprot
proteins
pubmed
34767447
uniprot
proteins
pubmed
39087467
uniprot
proteins
sequence_length
1165
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:39087467}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 833..853; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 874..894; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 900..920; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 941..961; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 995..1015; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 1040..1060; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 1063..1083; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins