Guanylate cyclase-C
| Receptor of heat-stable enterotoxins | ||
|---|---|---|
| other names |
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| Properties of human protein | ||
| Mass / length primary structure | 1050 amino acids | |
| Secondary to quaternary structure | Membrane receptor | |
| Identifier | ||
| Gene name | GUCY2C | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 4.6.1.2 , lyase | |
| Substrate | GTP | |
| Products | 3 ', 5'-cGMP + diphosphate | |
| Orthologue | ||
| human | House mouse | |
| Entrez | 2984 | 14917 |
| Ensemble | ENSG00000070019 | ENSMUSG00000042638 |
| UniProt | P25092 | Q3UWA6 |
| Refseq (mRNA) | NM_004963 | NM_001127318 |
| Refseq (protein) | NP_004954 | NP_001120790 |
| Gene locus | Chr 12: 14.61 - 14.7 Mb | Chr 6: 136.7 - 136.78 Mb |
| PubMed search | 2984 |
14917
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Guanylate cyclase-C ( GC-C , also: hSTAR ) is the protein in the cell membrane of intestinal cells that functions on the outside of the membrane as a receptor for the two peptide hormones guanyline and uroguanyline . In the case of such a bond the fitting to the membrane inner side is enzyme - domain activated. It catalyzes the biosynthesis of cGMP from GTP , whereupon cGMP triggers a signal cascade inside the cell , which leads to increased excretion of water and chloride from the cell. GC-C is thus significantly involved in the regulation of the fluid and electrolyte balance . In addition, the heat-stable enterotoxins (STa) of E. coli bind to the receptor and lead to uncontrolled excretion and thus diarrhea.
The GC-C receptor consists of three subunits, also called domains :
- the extracellular ligand binding domain, consisting of approximately 410 amino acids
- a transmembrane domain of about 25 residues and
- an intracellular domain of approximately 620 amino acids.
Individual evidence
- ↑ guanylate cyclase-C. In: Online Mendelian Inheritance in Man . (English).
- ^ LR Forte, RH Freeman, WJ Krause, RM London: Guanylin peptides: cyclic GMP signaling mechanisms . Braz: J. Med. Biol. Res., 32, 1999, pp. 1329-1336.