Adgra2
entrez
78560
canonical
uniprot
Q91ZV8
canonical
ensembl
ENSMUSG00000031486
resolver
ensp
ENSMUSP00000033876
resolver
ensp
ENSMUSP00000340014
resolver
enst
ENSMUST00000033876
resolver
genesymbol
Adgra2
resolver
genesymbol_syn
Gpr124
resolver
genesymbol_syn
Tem5
resolver
uniprot
B2RRK0
resolver
uniprot_entry
AGRA2_MOUSE
resolver
uniprot_sec
B2RRK0
resolver
amino_acid_sequence
MGAGGRRMPVPPARLLLLPLLPCLLLLAPGTRGAPGCPVPIRGCKCSGERPKGLSGGAHNPARRRVVCGGGDLPEPPDPGLLPNGTITLLLSNNKITGLRNGSFLGLSLLEKLDLRSNVISTVQPGAFLGLGELKRLDLSNNRIGCLTSETFQGLPRLLRLNISGNIYSSLQPGVFDELPALKIVDFGTEFLTCDCRLRWLLPWARNHSLQLSERTLCAYPSALHAHALSSLQESQLRCEGALELHTHYLIPSLRQVVFQGDRLPFQCSASYLGNDTRIHWYHNGAPMESDEQAGIVLAENLIHDCTFITSELTLSHIGVWASGEWECSVSTVQGNTSKKVEIVVLETSASYCPAERVTNNRGDFRWPRTLAGITAYQSCLQYPFTSVPLSGGAPGTRASRRCDRAGRWEPGDYSHCLYTNDITRVLYTFVLMPINASNALTLAHQLRVYTAEAASFSDMMDVVYVAQMIQKFLGYVDQIKELVEVMVDMASNLMLVDEHLLWLAQREDKACSGIVGALERIGGAALSPHAQHISVNSRNVALEAYLIKPHSYVGLTCTAFQRREVGVSGAQPSSVGQDAPVEPEPLADQQLRFRCTTGRPNISLSSFHIKNSVALASIQLPPSLFSTLPAALAPPVPPDCTLQLLVFRNGRLFRSHGNNTSRPGAAGPGKRRGVATPVIFAGTSGCGVGNLTEPVAVSLRHWAEGADPMAAWWNQDGPGGWSSEGCRLRYSQPNVSSLYCQHLGNVAVLMELNAFPREAGGSGAGLHPVVYPCTALLLLCLFSTIITYILNHSSIHVSRKGWHMLLNLCFHMAMTSAVFVGGVTLTNYQMVCQAVGITLHYSSLSSLLWMGVKARVLHKELSWRAPPLEEGEAAPPGPRPMLRFYLIAGGIPLIICGITAAVNIHNYRDHSPYCWLVWRPSLGAFYIPVALILPITWIYFLCAGLHLRSHVAQNPKQGNRISLEPGEELRGSTRLRSSGVLLNDSGSLLATVSAGVGTPAPPEDGDGVYSPGVQLGALMTTHFLYLAMWACGALAVSQRWLPRVVCSCLYGVAASALGLFVFTHHCARRRDVRASWRACCPPASPSASHVPARALPTATEDGSPVLGEGPASLKSSPSGSSGRAPPPPCKLTNLQVAQSQVCEASVAARGDGEPEPTGSRGSLAPRHHNNLHHGRRVHKSRAKGHRAGETGGKSRLKALRAGTSPGAPELLSSESGSLHNSPSDSYPGSSRNSPGDGLPLEGEPMLTPSEGSDTSAAPIAETGRPGQRRSASRDNLKGSGSALERESKRRSYPLNTTSLNGAPKGGKYEDASVTGAEAIAGGSMKTGLWKSETTV
uniprot
proteins
function
FUNCTION: Endothelial receptor which functions together with RECK to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B) (PubMed:25373781, PubMed:25558062, PubMed:28803732). Plays a key role in Wnt7-specific responses, such as endothelial cell sprouting and migration in the forebrain and neural tube, and establishment of the blood-brain barrier (PubMed:21071672, PubMed:21282641, PubMed:21421844, PubMed:25373781, PubMed:28288111). Acts as a Wnt7-specific coactivator of canonical Wnt signaling: required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex (By similarity). ADGRA2-tethering function does not rely on its G protein-coupled receptor (GPCR) structure but instead on its combined capacity to interact with RECK extracellularly and recruit the Dishevelled scaffolding protein intracellularly (By similarity). Binds to the glycosaminoglycans heparin, heparin sulfate, chondroitin sulfate and dermatan sulfate (By similarity). {ECO:0000250|UniProtKB:Q96PE1, ECO:0000269|PubMed:21071672, ECO:0000269|PubMed:21282641, ECO:0000269|PubMed:21421844, ECO:0000269|PubMed:25373781, ECO:0000269|PubMed:25558062, ECO:0000269|PubMed:28288111, ECO:0000269|PubMed:28803732}.
uniprot
proteins
mass_dalton
143170
uniprot
proteins
mutagenesis
MUTAGEN 364; /note="D->E: No effect on potentiation of WNT7A signaling."; /evidence="ECO:0000269|PubMed:25558062"; MUTAGEN 1333..1336; /note="Missing: Fails to interact with DLG1. No effect on cell surface localization."; /evidence="ECO:0000269|PubMed:25558062
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000250|UniProtKB:Q96PE1}.; PTM: Proteolytically cleaved into two subunits, an extracellular subunit and a seven-transmembrane subunit. Cleaved by thrombin (F2) and MMP1. Also cleaved by MMP9, with lower efficiency. Presence of the protein disulfide-isomerase P4HB at the cell surface is additionally required for shedding of the extracellular subunit, suggesting that the subunits are linked by disulfide bonds. Shedding is enhanced by the growth factor FGF2 and may promote cell survival during angiogenesis. {ECO:0000250|UniProtKB:Q96PE1}.
uniprot
proteins
protein_family
Adhesion G protein-coupled receptor (ADGR) subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
11559528
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18848646
uniprot
proteins
pubmed
21071672
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21282641
uniprot
proteins
pubmed
21421844
uniprot
proteins
pubmed
25373781
uniprot
proteins
pubmed
25558062
uniprot
proteins
pubmed
28288111
uniprot
proteins
pubmed
28803732
uniprot
proteins
sequence_length
1336
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25558062, ECO:0000269|PubMed:28803732}; Multi-pass membrane protein {ECO:0000255}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q96PE1}. Note=Enriched at lateral cell borders and also at sites of cell-ECM (extracellular matrix) contact. {ECO:0000250|UniProtKB:Q96PE1}.
uniprot
proteins
transmembrane_region
TRANSMEM 770..790; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 806..826; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 831..851; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 885..905; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 923..943; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 1017..1037; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 1045..1065; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins