GPR56
entrez
9289
canonical
uniprot
Q9Y653
canonical
ensembl
ENSG00000205336
resolver
ensp
ENSP00000373465
resolver
ensp
ENSP00000398034
resolver
ensp
ENSP00000444911
resolver
ensp
ENSP00000454933
resolver
ensp
ENSP00000455215
resolver
ensp
ENSP00000455351
resolver
ensp
ENSP00000456620
resolver
ensp
ENSP00000456794
resolver
ensp
ENSP00000457456
resolver
ensp
ENSP00000500185
resolver
ensp
ENSP00000500676
resolver
ensp
ENSP00000530595
resolver
ensp
ENSP00000530599
resolver
ensp
ENSP00000530600
resolver
ensp
ENSP00000530601
resolver
ensp
ENSP00000530602
resolver
ensp
ENSP00000530603
resolver
ensp
ENSP00000530607
resolver
ensp
ENSP00000530608
resolver
ensp
ENSP00000530613
resolver
ensp
ENSP00000530614
resolver
ensp
ENSP00000530616
resolver
ensp
ENSP00000530620
resolver
ensp
ENSP00000530621
resolver
ensp
ENSP00000530622
resolver
ensp
ENSP00000530623
resolver
ensp
ENSP00000642453
resolver
ensp
ENSP00000642454
resolver
ensp
ENSP00000642456
resolver
ensp
ENSP00000642463
resolver
ensp
ENSP00000642464
resolver
genesymbol
ADGRG1
resolver
genesymbol
GPR56
resolver
genesymbol_syn
GPR56
resolver
genesymbol_syn
TM7LN4
resolver
genesymbol_syn
TM7XN1
resolver
hgnc
HGNC:4512
resolver
uniprot
A0A024R6U7
resolver
uniprot
A0A0S2Z517
resolver
uniprot
A6NIT7
resolver
uniprot
A6NJV9
resolver
uniprot
B0M0K4
resolver
uniprot
B3KQN7
resolver
uniprot
B3KQV4
resolver
uniprot
B4DM06
resolver
uniprot
B4DR54
resolver
uniprot
O95966
resolver
uniprot
Q6ZMP1
resolver
uniprot
Q8NGB3
resolver
uniprot
Q96HB4
resolver
uniprot_entry
A0A024R6U7_HUMAN
resolver
uniprot_entry
A0A0S2Z517_HUMAN
resolver
uniprot_entry
AGRG1_HUMAN
resolver
uniprot_entry
B3KQN7_HUMAN
resolver
uniprot_entry
B3KQV4_HUMAN
resolver
uniprot_entry
B4DM06_HUMAN
resolver
uniprot_sec
A6NIT7
resolver
uniprot_sec
A6NJV9
resolver
uniprot_sec
B0M0K4
resolver
uniprot_sec
B4DR54
resolver
uniprot_sec
O95966
resolver
uniprot_sec
Q6ZMP1
resolver
uniprot_sec
Q8NGB3
resolver
uniprot_sec
Q96HB4
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:35418682). 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:35418682). 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:35418682). The cleaved GAIN-B and N-terminal domains can then dissociate from the rest of the receptor (PubMed:25918380, PubMed:35418682). {ECO:0000269|PubMed:25918380, ECO:0000269|PubMed:35418682}.
uniprot
proteins
amino_acid_sequence
MTPQSLLQTTLFLLSLLFLVQGAHGRGHREDFRFCSQRNQTHRSSLHYKPTPDLRISIENSEEALTVHAPFPAAHPASRSFPDPRGLYHFCLYWNRHAGRLHLLYGKRDFLLSDKASSLLCFQHQEESLAQGPPLLATSVTSWWSPQNISLPSAASFTFSFHSPPHTAAHNASVDMCELKRDLQLLSQFLKHPQKASRRPSAAPASQQLQSLESKLTSVRFMGDMVSFEEDRINATVWKLQPTAGLQDLHIHSRQEEEQSEIMEYSVLLPRTLFQRTKGRSGEAEKRLLLVDFSSQALFQDKNSSQVLGEKVLGIVVQNTKVANLTEPVVLTFQHQLQPKNVTLQCVFWVEDPTLSSPGHWSSAGCETVRRETQTSCFCNHLTYFAVLMVSSVEVDAVHKHYLSLLSYVGCVVSALACLVTIAAYLCSRVPLPCRRKPRDYTIKVHMNLLLAVFLLDTSFLLSEPVALTGSEAGCRASAIFLHFSLLTCLSWMGLEGYNLYRLVVEVFGTYVPGYLLKLSAMGWGFPIFLVTLVALVDVDNYGPIILAVHRTPEGVIYPSMCWIRDSLVSYITNLGLFSLVFLFNMAMLATMVVQILRLRPHTQKWSHVLTLLGLSLVLGLPWALIFFSFASGTFQLVVLYLFSIITSFQGFLIFIWYWSMRLQARGGPSPLKSNSDSARLPISSGSTSSSRI
uniprot
proteins
disease_involvement
DISEASE: Cortical dysplasia, complex, with other brain malformations 14A (bilateral frontoparietal) (CDCBM14A) [MIM:606854]: An autosomal recessive disorder characterized by global developmental delay with impaired intellectual development, motor delay, poor speech, cerebellar and pyramidal signs, truncal ataxia, and early-onset seizures. Brain imaging shows bilateral frontoparietal polymicrogyria, a malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. Polymicrogyria is considered to be the result of postmigratory abnormal cortical organization. {ECO:0000269|PubMed:15044805, ECO:0000269|PubMed:16240336, ECO:0000269|PubMed:21349848, ECO:0000269|PubMed:21723461, ECO:0000269|PubMed:22238662, ECO:0000269|PubMed:24949629, ECO:0000269|PubMed:28424266, ECO:0000269|PubMed:29707406, ECO:0000269|PubMed:30511534, ECO:0000269|PubMed:34513772, ECO:0000269|PubMed:36524291}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cortical dysplasia, complex, with other brain malformations 14B (bilateral perisylvian) (CDCBM14B) [MIM:615752]: An autosomal recessive disorder characterized by strikingly restricted polymicrogyria limited to the cortex surrounding the Sylvian fissure. Affected individuals have intellectual and language difficulty and seizures, but no motor disability. Polymicrogyria is a malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. It is considered to be the result of postmigratory abnormal cortical organization. {ECO:0000269|PubMed:24531968}. Note=The disease is caused by variants affecting the gene represented in this entry. Homozygous deletion of 1 of 2 tandem 15-bp repeats located 144 bp upstream of the ADGRG1 non-coding exon 1m transcription start site, results in impaired perisylvian ADGRG1 expression and disruption of perisylvian gyri (PubMed:24531968). {ECO:0000269|PubMed:24531968}.
uniprot
proteins
function
FUNCTION: Adhesion G protein-coupled receptor (aGPCR) for steroid hormone 17alpha-hydroxypregnenolone (17-OH), which is involved in cell adhesion and cell-cell interactions (PubMed:39389061). 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 RhoA pathway (PubMed:28874577, PubMed:35418682, PubMed:39389061). ADGRG1 is coupled to G(12) and/or G(13) G proteins (GNA12 and GNA13, respectively) and mediates the activation Rho small GTPases (PubMed:22238662, PubMed:28424266, PubMed:35418682, PubMed:39389061). Acts as a potent suppressor of ferroptosis: binding to 17-OH-binding initiates signaling that down-regulates CD36 and alleviates ferroptosis-induced liver injury (By similarity). Ligand-binding also induces cell adhesion activity via association with proteins such as collagen III/COL3A1 and TGM2 (By similarity). Mediates cell matrix adhesion in developing neurons and hematopoietic stem cells (By similarity). Involved in cortical development, specifically in maintenance of the pial basement membrane integrity and in cortical lamination: association with COL3A1 in the developing brain inhibits neuronal migration via activation of the RhoA pathway (PubMed:24531968). Together with TGM2, acts as a regulator of myelination and myelin repair in oligodendrocyte precursor cells (By similarity). Acts as a hemostatic sensor of shear force: G protein-coupled receptor signaling is activated in response to shear force in platelets, promoting G(13) G protein signaling, and platelet shape change and aggregation in a COL3A1-dependent manner (PubMed:33097663). Acts as an inhibitor of VEGFA production thereby inhibiting angiogenesis through a signaling pathway mediated by PRKCA (PubMed:16757564, PubMed:19572147, PubMed:21724588). Plays a role in the maintenance of hematopoietic stem cells in bone marrow niche (By similarity). Plays an essential role in testis development (By similarity). {ECO:0000250|UniProtKB:Q8K209, ECO:0000269|PubMed:16757564, ECO:0000269|PubMed:19572147, ECO:0000269|PubMed:21724588, ECO:0000269|PubMed:22238662, ECO:0000269|PubMed:24531968, ECO:0000269|PubMed:28424266, ECO:0000269|PubMed:28874577, ECO:0000269|PubMed:33097663, ECO:0000269|PubMed:35418682, ECO:0000269|PubMed:39389061}.; FUNCTION: [Isoform 5]: Adhesion G protein-coupled receptor (aGPCR) for phosphatidylserine, which is involved in microglia-mediated synapse pruning during development (By similarity). Required to maintain appropriate synaptic numbers in several brain regions in a time- and circuit-dependent fashion: phosphatidylserine-binding acts as a 'eat-me' signal for apoptotic cells, leading to microglial engulfment of phosphatidylserine-positive synapses (By similarity). {ECO:0000250|UniProtKB:Q8K209}.
uniprot
proteins
mass_dalton
77738
uniprot
proteins
mutagenesis
MUTAGEN 28; /note="H->A: Abolishes heparin-binding; when associated with A-29 and A-33."; /evidence="ECO:0000269|PubMed:27068534"; MUTAGEN 29; /note="R->A: Abolishes heparin-binding; when associated with A-28 and A-33."; /evidence="ECO:0000269|PubMed:27068534"; MUTAGEN 33; /note="R->A: Reduces heparin-binding. Abolishes heparin-binding; when associated with A-28 and A-29."; /evidence="ECO:0000269|PubMed:27068534"; MUTAGEN 381; /note="H->S: Abolishes cleavage."; /evidence="ECO:0000269|PubMed:22333914"; MUTAGEN 383; /note="T->G: Abolishes cleavage but does not affect cell membrane localization or signaling activity."; /evidence="ECO:0000269|PubMed:21349848, ECO:0000269|PubMed:22333914, ECO:0000269|PubMed:26710850"; MUTAGEN 384; /note="Y->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418682"; MUTAGEN 385; /note="F->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418682"; MUTAGEN 386; /note="A->M: Impaired G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:37673336"; MUTAGEN 389; /note="M->A: Abolished G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418682"; MUTAGEN 454; /note="F->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418682"; MUTAGEN 482; /note="L->A: Impaired G protein-coupled receptor activity in response to 17alpha-hydroxypregnenolone-binding."; /evidence="ECO:0000269|PubMed:39389061"; MUTAGEN 486; /note="L->A: Impaired G protein-coupled receptor activity in response to 17alpha-hydroxypregnenolone-binding."; /evidence="ECO:0000269|PubMed:39389061"; MUTAGEN 563; /note="W->A: Impaired G protein-coupled receptor activity in response to 17alpha-hydroxypregnenolone-binding."; /evidence="ECO:0000269|PubMed:35418682, ECO:0000269|PubMed:39389061"; MUTAGEN 570; /note="S->A,V: Impaired G protein-coupled receptor activity in response to 17alpha-hydroxypregnenolone-binding."; /evidence="ECO:0000269|PubMed:39389061"; MUTAGEN 571; /note="Y->F: Impaired G protein-coupled receptor activity in response to 17alpha-hydroxypregnenolone-binding."; /evidence="ECO:0000269|PubMed:39389061"; MUTAGEN 574; /note="N->A: Impaired G protein-coupled receptor activity in response to 17alpha-hydroxypregnenolone-binding."; /evidence="ECO:0000269|PubMed:39389061"; MUTAGEN 623; /note="W->A: Impaired G protein-coupled receptor activity in response to 17alpha-hydroxypregnenolone-binding."; /evidence="ECO:0000269|PubMed:35418682, ECO:0000269|PubMed:39389061"; MUTAGEN 643; /note="F->A: Impaired G protein-coupled receptor activity in response to 17alpha-hydroxypregnenolone-binding."; /evidence="ECO:0000269|PubMed:35418682, ECO:0000269|PubMed:39389061
uniprot
proteins
post_translational_modification
PTM: Autoproteolytically cleaved into 2 fragments; the large extracellular N-terminal fragment (ADGRG1 NT) and the membrane-bound C-terminal fragment (ADGRG1 CT) predominantly remain associated and non-covalently linked (PubMed:22333914, PubMed:37673336). Shedding to yield the secreted ADGRG1 N-terminal fragment seems to involve metalloprotease(s) (PubMed:22333914). {ECO:0000269|PubMed:22333914, ECO:0000269|PubMed:37673336}.; PTM: N-glycosylated. Contains sialic acid residues. {ECO:0000269|PubMed:21349848}.; PTM: Ubiquitinated. Undergoes polyubiquitination upon activation. {ECO:0000269|PubMed:21708946}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
protein_family
LN-TM7 subfamily
uniprot
proteins
pubmed
10049584
uniprot
proteins
pubmed
10100861
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15004227
uniprot
proteins
pubmed
15044805
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
16240336
uniprot
proteins
pubmed
16757564
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19572147
uniprot
proteins
pubmed
21349848
uniprot
proteins
pubmed
21708946
uniprot
proteins
pubmed
21723461
uniprot
proteins
pubmed
21724588
uniprot
proteins
pubmed
22238662
uniprot
proteins
pubmed
22333914
uniprot
proteins
pubmed
24531968
uniprot
proteins
pubmed
24949629
uniprot
proteins
pubmed
25918380
uniprot
proteins
pubmed
26710850
uniprot
proteins
pubmed
27068534
uniprot
proteins
pubmed
28258187
uniprot
proteins
pubmed
28424266
uniprot
proteins
pubmed
28874577
uniprot
proteins
pubmed
29707406
uniprot
proteins
pubmed
30511534
uniprot
proteins
pubmed
33097663
uniprot
proteins
pubmed
34513772
uniprot
proteins
pubmed
35418682
uniprot
proteins
pubmed
36524291
uniprot
proteins
pubmed
37673336
uniprot
proteins
pubmed
39389061
uniprot
proteins
sequence_length
693
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21349848, ECO:0000269|PubMed:24949629, ECO:0000269|PubMed:28424266}; Multi-pass membrane protein {ECO:0000269|PubMed:35418682}.; SUBCELLULAR LOCATION: [Adhesion G protein-coupled receptor G1, N-terminal fragment]: Secreted {ECO:0000269|PubMed:21349848}. Note=Activation of the G protein-coupled receptor and interaction with COL3A1 leads to the release of ADGRG1 NT from the membrane. {ECO:0000269|PubMed:21349848, ECO:0000269|PubMed:24949629}.; SUBCELLULAR LOCATION: [Adhesion G protein-coupled receptor G1, C-terminal fragment]: Membrane raft {ECO:0000269|PubMed:24949629}. Note=Interaction with its ligand COL3A1 leads to the release of ADGRG1 NT from the membrane and triggers the association of ADGRG1 CT with lipid rafts. {ECO:0000269|PubMed:24949629}.
uniprot
proteins
transmembrane_region
TRANSMEM 402..424; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF8"; TRANSMEM 438..460; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF8"; TRANSMEM 466..495; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF8"; TRANSMEM 511..533; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF8"; TRANSMEM 563..588; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF8"; TRANSMEM 603..624; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF8"; TRANSMEM 629..654; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF8
uniprot
proteins