GUCY1B3

From Wikipedia, the free encyclopedia

Guanylate cyclase 1, soluble, beta 3

Identifiers

GUCY1B3; GC-S-beta-1; GC-SB3; GUC1B3; GUCB3; GUCSB3

External IDs

OMIM: 139397 MGI: 1860604 HomoloGene: 664

Gene ontology
Molecular Function:	• guanylate cyclase activity • receptor activity • iron ion binding • heme binding • metal ion binding
Cellular Component:	• cytoplasm • guanylate cyclase complex, soluble
Biological Process:	• cGMP biosynthetic process • nitric oxide mediated signal transduction • circulation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000857 (mRNA)
NP_000848 (protein)

NM_017469 (mRNA)
NP_059497 (protein)

Location

Chr 4: 156.9 - 156.95 Mb

Chr 3: 82.12 - 82.16 Mb

Pubmed search

[1]

[2]

Guanylate cyclase 1, soluble, beta 3, also known as GUCY1B3, is a human gene.^[1]

Soluble guanylate cyclase (sGC), a heterodimeric protein consisting of an alpha and a beta subunit, catalyzes the conversion of GTP to the second messenger cGMP and functions as the main receptor for nitric oxide and nitrovasodilator drugs (Zabel et al., 1998).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: GUCY1B3 guanylate cyclase 1, soluble, beta 3.

[edit] Further reading

Lucas KA, Pitari GM, Kazerounian S, et al. (2000). "Guanylyl cyclases and signaling by cyclic GMP.". Pharmacol. Rev. 52 (3): 375–414. PMID 10977868.
Giuili G, Scholl U, Bulle F, Guellaën G (1992). "Molecular cloning of the cDNAs coding for the two subunits of soluble guanylyl cyclase from human brain.". FEBS Lett. 304 (1): 83–8. PMID 1352257.
Chhajlani V, Frändberg PA, Ahlner J, et al. (1991). "Heterogeneity in human soluble guanylate cyclase due to alternative splicing.". FEBS Lett. 290 (1-2): 157–8. PMID 1680753.
Giuili G, Roechel N, Scholl U, et al. (1993). "Colocalization of the genes coding for the alpha 3 and beta 3 subunits of soluble guanylyl cyclase to human chromosome 4 at q31.3-q33.". Hum. Genet. 91 (3): 257–60. PMID 8097486.
Papapetropoulos A, Cziraki A, Rubin JW, et al. (1996). "cGMP accumulation and gene expression of soluble guanylate cyclase in human vascular tissue.". J. Cell. Physiol. 167 (2): 213–21. doi:10.1002/(SICI)1097-4652(199605)167:2<213::AID-JCP4>3.0.CO;2-S. PMID 8613461.
Zabel U, Weeger M, La M, Schmidt HH (1998). "Human soluble guanylate cyclase: functional expression and revised isoenzyme family.". Biochem. J. 335 ( Pt 1): 51–7. PMID 9742212.
Russwurm M, Wittau N, Koesling D (2002). "Guanylyl cyclase/PSD-95 interaction: targeting of the nitric oxide-sensitive alpha2beta1 guanylyl cyclase to synaptic membranes.". J. Biol. Chem. 276 (48): 44647–52. doi:10.1074/jbc.M105587200. PMID 11572861.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Venema RC, Venema VJ, Ju H, et al. (2003). "Novel complexes of guanylate cyclase with heat shock protein 90 and nitric oxide synthase.". Am. J. Physiol. Heart Circ. Physiol. 285 (2): H669–78. doi:10.1152/ajpheart.01025.2002. PMID 12676772.
Meurer S, Pioch S, Wagner K, et al. (2005). "AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl cyclase.". J. Biol. Chem. 279 (47): 49346–54. doi:10.1074/jbc.M410565200. PMID 15381706.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Mateos-Cáceres PJ, Garcia-Cardoso J, Lapuente L, et al. (2006). "Soluble guanylate cyclase beta1-subunit expression is increased in mononuclear cells from patients with erectile dysfunction.". Int. J. Impot. Res. 18 (5): 432–7. doi:10.1038/sj.ijir.3901461. PMID 16528291.