GUCY2F

GUCY2F
Identifiers
Aliases	GUCY2F, CYGF, GC-F, GUC2DL, GUC2F, RETGC-2, ROS-GC2, guanylate cyclase 2F, retinal
External IDs	MGI: 105119 HomoloGene: 37491 GeneCards: GUCY2F
Gene ontology Molecular function • protein kinase activity • nucleotide binding • protein homodimerization activity • guanylate cyclase activity • GTP binding • lyase activity • protein heterodimerization activity • adenylate cyclase activity • phosphorus-oxygen lyase activity • ATP binding • receptor activity Cellular component • integral component of membrane • membrane • integral component of plasma membrane • photoreceptor disc membrane • guanylate cyclase complex, soluble • nuclear outer membrane Biological process • intracellular signal transduction • response to stimulus • regulation of rhodopsin mediated signaling pathway • cyclic nucleotide biosynthetic process • detection of light stimulus involved in visual perception • cGMP biosynthetic process • protein phosphorylation • receptor guanylyl cyclase signaling pathway • visual perception Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2986	245650
Ensembl	ENSG00000101890	ENSMUSG00000042282
UniProt	P51841	Q5SDA5
RefSeq (mRNA)	NM_001522	NM_001007576
RefSeq (protein)	NP_001513.2	NP_001007577.1
Location (UCSC)	Chr X: 109.37 – 109.48 Mb	Chr X: 142.08 – 142.2 Mb
PubMed search	[1]	[2]
Wikidata

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Retinal guanylyl cyclase 2 also known as guanylate cyclase F (GUCY2F) is a protein that in humans is encoded by the GUCY2F gene.^[3]

Function

The protein encoded by this gene is a guanylyl cyclase found predominantly in photoreceptors in the retina. The encoded protein is thought to be involved in resynthesis of cGMP after light activation of the visual signal transduction cascade, allowing a return to the dark state. This protein is a single-pass type I membrane protein.^[3]

Clinical significance

Defects in this gene may be a cause of X-linked retinitis pigmentosa.^[3]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: Guanylate cyclase 2F, retinal".

Further reading

• Blackford A, Parmigiani G, Kensler TW, Wolfgang C, Jones S, Zhang X, Parsons DW, Lin JC, Leary RJ, Eshleman JR, Goggins M, Jaffee EM, Iacobuzio-Donahue CA, Maitra A, Klein A, Cameron JL, Olino K, Schulick R, Winter J, Vogelstein B, Velculescu VE, Kinzler KW, Hruban RH (April 2009). "Genetic mutations associated with cigarette smoking in pancreatic cancer". Cancer Res. 69 (8): 3681–8. doi:10.1158/0008-5472.CAN-09-0015. PMC 2669837. PMID 19351817.
• Lowe DG, Dizhoor AM, Liu K, Gu Q, Spencer M, Laura R, Lu L, Hurley JB (June 1995). "Cloning and expression of a second photoreceptor-specific membrane retina guanylyl cyclase (RetGC), RetGC-2". Proc. Natl. Acad. Sci. U.S.A. 92 (12): 5535–9. doi:10.1073/pnas.92.12.5535. PMC 41730. PMID 7777544.
• Yang RB, Fülle HJ, Garbers DL (February 1996). "Chromosomal localization and genomic organization of genes encoding guanylyl cyclase receptors expressed in olfactory sensory neurons and retina". Genomics. 31 (3): 367–72. doi:10.1006/geno.1996.0060. PMID 8838319.
• Yang RB, Garbers DL (May 1997). "Two eye guanylyl cyclases are expressed in the same photoreceptor cells and form homomers in preference to heteromers". J. Biol. Chem. 272 (21): 13738–42. doi:10.1074/jbc.272.21.13738. PMID 9153227.
• Wood LD, Calhoun ES, Silliman N, Ptak J, Szabo S, Powell SM, Riggins GJ, Wang TL, Yan H, Gazdar A, Kern SE, Pennacchio L, Kinzler KW, Vogelstein B, Velculescu VE (October 2006). "Somatic mutations of GUCY2F, EPHA3, and NTRK3 in human cancers". Hum. Mutat. 27 (10): 1060–1. doi:10.1002/humu.9452. PMID 16941478.
• Laura RP, Hurley JB (August 1998). "The kinase homology domain of retinal guanylyl cyclases 1 and 2 specifies the affinity and cooperativity of interaction with guanylyl cyclase activating protein-2". Biochemistry. 37 (32): 11264–71. doi:10.1021/bi9809674. PMID 9698373.
• Helten A, Säftel W, Koch KW (November 2007). "Expression level and activity profile of membrane bound guanylate cyclase type 2 in rod outer segments". J. Neurochem. 103 (4): 1439–46. doi:10.1111/j.1471-4159.2007.04923.x. PMID 17868328.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.