GPR56 Antibody - #DF2753

Receptor involved in cell adhesion and probably in cell-cell interactions. Mediates cell matrix adhesion in developing neurons and hematopoietic stem cells. Receptor for collagen III/COL3A1 in the developing brain and involved in regulation of cortical development, specifically in maintenance of the pial basement membrane integrity and in cortical lamination (By similarity). Binding to the COL3A1 ligand inhibits neuronal migration and activates the RhoA pathway by coupling to GNA13 and possibly GNA12. Plays a role in the maintenance of hematopoietic stem cells and/or leukemia stem cells in bone marrow niche (By similarity). Plays a critical role in cancer progression by inhibiting VEGFA production threreby inhibiting angiogenesis through a signaling pathway mediated by PRKCA. Plays an essential role in testis development (By similarity).

Plays a critical role in cancer progression by activating VEGFA production and angiogenesis through a signaling pathway mediated by PRKCA.

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. Shedding to yield the secreted ADGRG1 N-terminal fragment seems to involve metalloprotease(s).

N-glycosylated. Contains sialic acid residues.

Ubiquitinated. Undergoes polyubiquitination upon activation.

Cell membrane>Multi-pass membrane protein.

Secreted.

Membrane raft.
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.

Widely distributed with highest levels found in thyroid gland, brain and heart. Expressed in a great number of tumor cells. Expression is down-regulated in different tumors from highly metastatic cells.

Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment (ADGRG1 NT) and the membrane-bound C-terminal fragment (ADGRG1-CT) predominantly remain associated and non-covalently linked. ADGRG1 NT self-associates in a trans-trans manner; the homophilic interaction enhances receptor signaling. ADGRG1-CT interacts with ARRB2; the interaction is impaired by ADGRG1 NT. Interacts with TGM2; TGM2 probably is not a ADGRG1 ligand and the interaction is reported controversial. Part of a GPCR-tetraspanin complex at least consisting of ADGRG1, CD81, eventually CD9, and GNA11 in which CD81 is enhancing the association of ADGRG1 with GNA11. Interacts with heparin; leading to the reduction of ADGRG1 shedding. Interacts with COL3A1.

Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily.