GUCA1B

Guanylyl cyclase-activating protein 2 is an enzyme that in humans is encoded by the GUCA1B gene. Alternative names:

• Guanylate cyclase activator 1B
• Retinal guanylyl cyclase activator protein p24

GUCA1B
Identifiers
Aliases	GUCA1B, GCAP2, GUCA2, RP48, guanylate cyclase activator 1B, GCAP 2
External IDs	OMIM: 602275; MGI: 1194489; HomoloGene: 1586; GeneCards: GUCA1B; OMA:GUCA1B - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p21.1 Start 42,183,284 bp End 42,194,956 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 C Start 47,696,318 bp End 47,703,892 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle cerebellar hemisphere granulocyte right hemisphere of cerebellum tibialis anterior muscle gastrocnemius muscle stromal cell of endometrium tibial nerve trabecular bone right uterine tube Top expressed in layer of retina neural layer of retina embryo embryo quadriceps femoris muscle outer nuclear layer islet of Langerhans bone marrow zone of skin lens More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding guanylate cyclase regulator activity metal ion binding calcium sensitive guanylate cyclase activator activity Cellular component photoreceptor inner segment membrane plasma membrane photoreceptor outer segment photoreceptor disc membrane Biological process phototransduction response to stimulus cell-cell signaling positive regulation of guanylate cyclase activity regulation of guanylate cyclase activity receptor guanylyl cyclase signaling pathway body fluid secretion visual perception regulation of rhodopsin mediated signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2979 107477 Ensembl ENSG00000112599 ENSMUSG00000023979 UniProt Q9UMX6 Q8VBV8 RefSeq (mRNA) NM_002098 NM_146079 RefSeq (protein) NP_002089 NP_666191 Location (UCSC) Chr 6: 42.18 – 42.19 Mb Chr 17: 47.7 – 47.7 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Biological Role

Guanylyl cyclase-activating protein 2 is proposed to play a role in dark adaptation. Under scotopic conditions, calcium ions bind to three putative EF-hand calcium binding motifs which reduces the protein's ability to stimulate guanylyl cyclase. This contributes to the maintained responsiveness of rod photoreceptors through hyperpolarizing them during sustained darkness.

Further reading

• Wiegand RC, Kato J, Huang MD, Fok KF, Kachur JF, Currie MG (October 1992). "Human guanylin: cDNA isolation, structure, and activity". FEBS Letters. 311 (2): 150–4. doi:10.1016/0014-5793(92)81387-2. PMID 1327879. S2CID 39983596.
• de Sauvage FJ, Keshav S, Kuang WJ, Gillett N, Henzel W, Goeddel DV (October 1992). "Precursor structure, expression, and tissue distribution of human guanylin". Proceedings of the National Academy of Sciences of the United States of America. 89 (19): 9089–93. Bibcode:1992PNAS...89.9089D. doi:10.1073/pnas.89.19.9089. PMC 50070. PMID 1409606.
• Otto-Bruc A, Fariss RN, Haeseleer F, Huang J, Buczyłko J, Surgucheva I, et al. (April 1997). "Localization of guanylate cyclase-activating protein 2 in mammalian retinas". Proceedings of the National Academy of Sciences of the United States of America. 94 (9): 4727–32. Bibcode:1997PNAS...94.4727O. doi:10.1073/pnas.94.9.4727. PMC 20792. PMID 9114059.
• 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.
• Sokal I, Haeseleer F, Arendt A, Adman ET, Hargrave PA, Palczewski K (February 1999). "Identification of a guanylyl cyclase-activating protein-binding site within the catalytic domain of retinal guanylyl cyclase 1". Biochemistry. 38 (5): 1387–93. doi:10.1021/bi982512k. PMID 9931003.
• Payne AM, Downes SM, Bessant DA, Plant C, Moore T, Bird AC, Bhattacharya SS (September 1999). "Genetic analysis of the guanylate cyclase activator 1B (GUCA1B) gene in patients with autosomal dominant retinal dystrophies". Journal of Medical Genetics. 36 (9): 691–3. doi:10.1136/jmg.36.9.691. PMC 1734430. PMID 10507726.
• Wistow G, Bernstein SL, Wyatt MK, Ray S, Behal A, Touchman JW, et al. (June 2002). "Expressed sequence tag analysis of human retina for the NEIBank Project: retbindin, an abundant, novel retinal cDNA and alternative splicing of other retina-preferred gene transcripts". Molecular Vision. 8: 196–204. PMID 12107411.
• Sato M, Nakazawa M, Usui T, Tanimoto N, Abe H, Ohguro H (March 2005). "Mutations in the gene coding for guanylate cyclase-activating protein 2 (GUCA1B gene) in patients with autosomal dominant retinal dystrophies". Graefe's Archive for Clinical and Experimental Ophthalmology = Albrecht von Graefes Archiv für Klinische und Experimentelle Ophthalmologie. 243 (3): 235–42. doi:10.1007/s00417-004-1015-7. PMID 15452722. S2CID 23347858.

External links

• GeneReviews/NCBI/NIH/UW entry on Retinitis Pigmentosa Overview