Secretin receptor family

Protein family From Wikipedia, the free encyclopedia

Secretin receptor family (class B GPCR subfamily[1]) consists of secretin receptors regulated by peptide hormones from the glucagon hormone family. The family is different from adhesion G protein-coupled receptors.[2]

Quick facts Identifiers, Symbol ...
Secretin family of 7 transmembrane receptors
Identifiers
Symbol7tm_2
PfamPF00002
InterProIPR000832
PROSITEPDOC00559
TCDB9.A.14
OPM superfamily6
OPM protein4k5y
CDDcd13952
Available protein structures:
PDB  IPR000832 PF00002 (ECOD; PDBsum)  
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The secretin-receptor family of GPCRs include vasoactive intestinal peptide receptors and receptors for secretin, calcitonin and parathyroid hormone/parathyroid hormone-related peptides. These receptors activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. The receptors in this family have seven transmembrane helices,[3][4] like rhodopsin-like GPCRs. However, there is no significant sequence identity between these two GPCR families and the secretin-receptor family has its own characteristic 7TM signature.[5]

The secretin-receptor family GPCRs exist in many animal species. Data mining with the Pfam signature has identified members in fungi, although due to their presumed non-hormonal function they are more commonly referred to as Adhesion G protein-coupled receptors, making the Adhesion subfamily the more basal group.[6] Three distinct sub-families (B1-B3) are recognized.

Subfamily B1

Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways.

Subfamily B2

Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin[7] and brain-specific angiogenesis inhibitor receptors[8] amongst others. They are otherwise known as Adhesion G protein-coupled receptors.

Subfamily B3

Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteristic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.

Unclassified members

HCTR-5; HCTR-6; KPG 006; KPG 008

References

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