In molecular biology, the amylin protein family or calcitonin/CGRP/IAPP protein family is a family of proteins, which includes the precursors of calcitonin/calcitonin gene-related peptide (CGRP), islet amyloid polypeptide (IAPP) and adrenomedullin.
| Calc_CGRP_IAPP | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 solution conformation of salmon calcitonin in sodium dodecyl sulfate micelles | |||||||||
| Identifiers | |||||||||
| Symbol | Calc_CGRP_IAPP | ||||||||
| Pfam | PF00214 | ||||||||
| InterPro | IPR021116 | ||||||||
| PROSITE | PDOC00231 | ||||||||
| SCOP2 | 1bzb / SCOPe / SUPFAM | ||||||||
| TCDB | 1.C.49 | ||||||||
| OPM superfamily | 243 | ||||||||
| OPM protein | 2jxz | ||||||||
| |||||||||
Calcitonin[1] is a 32 amino acid polypeptide hormone that causes a rapid but short-lived drop in the level of calcium and phosphate in the blood, by promoting the incorporation of these ions in the bones, alpha type. Alternative splicing of the gene coding for calcitonin produces a distantly related peptide of 37 amino acids, called calcitonin gene-related peptide (CGRP), beta type. CGRP induces vasodilatation in a variety of vessels, including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role.
Islet amyloid polypeptide (IAPP)[2] (also known as diabetes-associated peptide (DAP), or amylin) is a peptide of 37 amino acids that selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. Structurally, IAPP is closely related to CGRP.
Two conserved cysteines in the N-terminal of these peptides are known to be involved in a disulfide bond. The C-terminal amino acid of all three peptides is amidated.[3][4]
xCxxxxxCxxxxxxxxxxxxxxxxxxxxxxxxxxxx-NH(2)
| | Amide group
+-----+
Subfamilies
editHuman proteins containing this domain
editReferences
edit- ^ Breimer LH, Zaidi M, MacIntyre I (1988). "Peptides from the calcitonin genes: molecular genetics, structure and function". Biochem. J. 255 (2): 377–390. doi:10.1042/bj2550377. PMC 1135239. PMID 3060108.
- ^ Bell GI, Steiner DF, Nishi M, Sanke T, Nagamatsu S (1990). "Islet amyloid polypeptide. A new beta cell secretory product related to islet amyloid deposits". J. Biol. Chem. 265 (8): 4173–4176. doi:10.1016/S0021-9258(19)39539-0. PMID 2407732.
- ^ Breimer LH, MacIntyre I, Zaidi M (October 1988). "Peptides from the calcitonin genes: molecular genetics, structure and function". Biochem. J. 255 (2): 377–90. doi:10.1042/bj2550377. PMC 1135239. PMID 3060108.
- ^ Nishi M, Sanke T, Nagamatsu S, Bell GI, Steiner DF (March 1990). "Islet amyloid polypeptide. A new beta cell secretory product related to islet amyloid deposits". J. Biol. Chem. 265 (8): 4173–6. doi:10.1016/S0021-9258(19)39539-0. PMID 2407732.