Guanylin

Guanylin precursor
Identifiers
Symbol	Guanylin
Pfam	PF02058
InterPro	IPR000879
SCOP2	1uyb / SCOPe / SUPFAM
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1gnb :103-115 1gna :103-115 1o8rA:22-115 1uya :97-111 1uyb :97-111

Search for
Structures	Swiss-model
Domains	InterPro

guanylate cyclase activator 2A (guanylin)
	Solution structure of human proguanylin.[1]
Identifiers
Symbol	GUCA2A
Alt. symbols	GUCA2
NCBI gene	2980
HGNC	4682
OMIM	139392
PDB	1O8R
RefSeq	NM_033553
UniProt	Q02747
Other data
Locus	Chr. 1 p35-p34
Search for
Structures	Swiss-model
Domains	InterPro

Guanylin is a 15 amino acid polypeptide that is secreted by goblet cells in the colon. Guanylin acts as an agonist of the guanylyl cyclase receptor GC-C and regulates electrolyte and water transport in intestinal and renal epithelia.[2][3] Upon receptor binding, guanylin increases the intracellular concentration of cGMP, induces chloride secretion and decreases intestinal fluid absorption, ultimately causing diarrhoea.[4] The peptide stimulates the enzyme through the same receptor binding region as the heat-stable enterotoxins.[3]

Human proteins containing this domain

GUCA2A; GUCA2B;

Structure

This peptide has two topogies,[5] both isoforms are shown below:

Structure of the A-form of human uroguanylin.[5]

Structure of the B-form of human uroguanylin.[5]

References

PDB: 1O8R; Lauber T, Neudecker P, Rösch P, Marx UC (June 2003). "Solution structure of human proguanylin: the role of a hormone prosequence". J. Biol. Chem. 278 (26): 24118–24. doi:10.1074/jbc.M300370200. PMID 12707255.
Sciaky D, Kosiba JL, Cohen MB (1994). "Genomic sequence of the murine guanylin gene". Genomics. 24 (3): 583–587. doi:10.1006/geno.1994.1670. PMID 7713512.
Goeddel DV, Kuang WJ, Henzel W, Keshav S, Gillett N, de Sauvage FJ (1992). "Precursor structure, expression, and tissue distribution of human guanylin". Proc. Natl. Acad. Sci. U.S.A. 89 (19): 9089–9093. doi:10.1073/pnas.89.19.9089. PMC 50070. PMID 1409606.
Smith CE, Currie MG, Fok KF, Kato J, Moore RJ, Hamra FK, Duffin KL (1992). "Guanylin: an endogenous activator of intestinal guanylate cyclase". Proc. Natl. Acad. Sci. U.S.A. 89 (3): 947–951. doi:10.1073/pnas.89.3.947. PMC 48362. PMID 1346555.
Marx UC, Klodt J, Meyer M, et al. (September 1998). "One peptide, two topologies: structure and interconversion dynamics of human uroguanylin isomers". J. Pept. Res. 52 (3): 229–40. doi:10.1111/j.1399-3011.1998.tb01480.x. PMID 9774236.

External links

guanylin at the US National Library of Medicine Medical Subject Headings (MeSH)

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[pmid12707255-1] PDB: 1O8R; Lauber T, Neudecker P, Rösch P, Marx UC (June 2003). "Solution structure of human proguanylin: the role of a hormone prosequence". J. Biol. Chem. 278 (26): 24118–24. doi:10.1074/jbc.M300370200. PMID 12707255.

[PUB00001960-2] Sciaky D, Kosiba JL, Cohen MB (1994). "Genomic sequence of the murine guanylin gene". Genomics. 24 (3): 583–587. doi:10.1006/geno.1994.1670. PMID 7713512.

[PUB00004802-3] Goeddel DV, Kuang WJ, Henzel W, Keshav S, Gillett N, de Sauvage FJ (1992). "Precursor structure, expression, and tissue distribution of human guanylin". Proc. Natl. Acad. Sci. U.S.A. 89 (19): 9089–9093. doi:10.1073/pnas.89.19.9089. PMC 50070. PMID 1409606.

[PUB00004805-4] Smith CE, Currie MG, Fok KF, Kato J, Moore RJ, Hamra FK, Duffin KL (1992). "Guanylin: an endogenous activator of intestinal guanylate cyclase". Proc. Natl. Acad. Sci. U.S.A. 89 (3): 947–951. doi:10.1073/pnas.89.3.947. PMC 48362. PMID 1346555.

[pmid9774236-5] Marx UC, Klodt J, Meyer M, et al. (September 1998). "One peptide, two topologies: structure and interconversion dynamics of human uroguanylin isomers". J. Pept. Res. 52 (3): 229–40. doi:10.1111/j.1399-3011.1998.tb01480.x. PMID 9774236.