Biology:Secretin receptor family

From HandWiki
Short description: Protein family
Secretin family of 7 transmembrane receptors
Identifiers
Symbol7tm_2
PfamPF00002
InterProIPR000832
PROSITEPDOC00559
TCDB9.A.14
OPM superfamily6
OPM protein4k5y
CDDcd13952

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]

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 7 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

  1. ↑ "Family-B G-protein-coupled receptors". Genome Biology 2 (12): REVIEWS3013. 2001. doi:10.1186/gb-2001-2-12-reviews3013. PMID 11790261. 
  2. ↑ "International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G protein-coupled receptors". Pharmacological Reviews 67 (2): 338–67. 2015. doi:10.1124/pr.114.009647. PMID 25713288. 
  3. ↑ PDB: 4L6R​; "Structure of the human glucagon class B G-protein-coupled receptor". Nature 499 (7459): 444–9. July 2013. doi:10.1038/nature12393. PMID 23863937. Bibcode: 2013Natur.499..444S. 
  4. ↑ PDB: 5VEX​; "Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators". Nature 546 (7657): 312–315. June 2017. doi:10.1038/nature22378. PMID 28514449. Bibcode: 2017Natur.546..312S. 
  5. ↑ "Insights into the structure of class B GPCRs". Trends in Pharmacological Sciences 35 (1): 12–22. January 2014. doi:10.1016/j.tips.2013.11.001. PMID 24359917. 
  6. ↑ "The origin of GPCRs: identification of mammalian like Rhodopsin, Adhesion, Glutamate and Frizzled GPCRs in fungi". PLOS ONE 7 (1): e29817. 2012. doi:10.1371/journal.pone.0029817. PMID 22238661. Bibcode: 2012PLoSO...729817K. 
  7. ↑ Universal protein resource accession number O94910 at UniProt.
  8. ↑ Universal protein resource accession number O14514 at UniProt.



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