GUCA1B

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

Guanylyl cyclase-activating protein 2 is an enzyme that in humans is encoded by the GUCA1B gene.{{cite journal | vauthors = Surguchov A, Bronson JD, Banerjee P, Knowles JA, Ruiz C, Subbaraya I, Palczewski K, Baehr W | display-authors = 6 | title = The human GCAP1 and GCAP2 genes are arranged in a tail-to-tail array on the short arm of chromosome 6 (p21.1) | journal = Genomics | volume = 39 | issue = 3 | pages = 312–22 | date = February 1997 | pmid = 9119368 | doi = 10.1006/geno.1996.4513 | doi-access = free }}{{cite web | title = Entrez Gene: GUCA1B guanylate cyclase activator 1B (retina)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2979}} Alternative names:{{Cite web|url=https://www.uniprot.org/uniprot/P51177|title=GUCA1B - Guanylyl cyclase-activating protein 2 - Bos taurus (Bovine) - GUCA1B gene & protein|website=www.uniprot.org|language=en|access-date=2017-10-09}}

Biological Role

Guanylyl cyclase-activating protein 2 is proposed to play a role in dark adaptation.{{cite journal | vauthors = Gorczyca WA, Gray-Keller MP, Detwiler PB, Palczewski K | title = Purification and physiological evaluation of a guanylate cyclase activating protein from retinal rods | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 91 | issue = 9 | pages = 4014–8 | date = April 1994 | pmid = 7909609 | doi = 10.1073/pnas.91.9.4014 | pmc = 43713 | bibcode = 1994PNAS...91.4014G | doi-access = free }} 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.

References

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Further reading

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  • {{cite journal | vauthors = Wiegand RC, Kato J, Huang MD, Fok KF, Kachur JF, Currie MG | title = Human guanylin: cDNA isolation, structure, and activity | journal = FEBS Letters | volume = 311 | issue = 2 | pages = 150–4 | date = October 1992 | pmid = 1327879 | doi = 10.1016/0014-5793(92)81387-2 | s2cid = 39983596 | doi-access = free }}
  • {{cite journal | vauthors = de Sauvage FJ, Keshav S, Kuang WJ, Gillett N, Henzel W, Goeddel DV | title = Precursor structure, expression, and tissue distribution of human guanylin | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 89 | issue = 19 | pages = 9089–93 | date = October 1992 | pmid = 1409606 | pmc = 50070 | doi = 10.1073/pnas.89.19.9089 | bibcode = 1992PNAS...89.9089D | doi-access = free }}
  • {{cite journal | vauthors = Otto-Bruc A, Fariss RN, Haeseleer F, Huang J, Buczyłko J, Surgucheva I, Baehr W, Milam AH, Palczewski K | display-authors = 6 | title = Localization of guanylate cyclase-activating protein 2 in mammalian retinas | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 9 | pages = 4727–32 | date = April 1997 | pmid = 9114059 | pmc = 20792 | doi = 10.1073/pnas.94.9.4727 | bibcode = 1997PNAS...94.4727O | doi-access = free }}
  • {{cite journal | vauthors = Laura RP, Hurley JB | title = The kinase homology domain of retinal guanylyl cyclases 1 and 2 specifies the affinity and cooperativity of interaction with guanylyl cyclase activating protein-2 | journal = Biochemistry | volume = 37 | issue = 32 | pages = 11264–71 | date = August 1998 | pmid = 9698373 | doi = 10.1021/bi9809674 }}
  • {{cite journal | vauthors = Sokal I, Haeseleer F, Arendt A, Adman ET, Hargrave PA, Palczewski K | title = Identification of a guanylyl cyclase-activating protein-binding site within the catalytic domain of retinal guanylyl cyclase 1 | journal = Biochemistry | volume = 38 | issue = 5 | pages = 1387–93 | date = February 1999 | pmid = 9931003 | doi = 10.1021/bi982512k }}
  • {{cite journal | vauthors = Payne AM, Downes SM, Bessant DA, Plant C, Moore T, Bird AC, Bhattacharya SS | title = Genetic analysis of the guanylate cyclase activator 1B (GUCA1B) gene in patients with autosomal dominant retinal dystrophies | journal = Journal of Medical Genetics | volume = 36 | issue = 9 | pages = 691–3 | date = September 1999 | pmid = 10507726 | pmc = 1734430 | doi = 10.1136/jmg.36.9.691 }}
  • {{cite journal | vauthors = Wistow G, Bernstein SL, Wyatt MK, Ray S, Behal A, Touchman JW, Bouffard G, Smith D, Peterson K | display-authors = 6 | title = 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 | journal = Molecular Vision | volume = 8 | pages = 196–204 | date = June 2002 | pmid = 12107411 }}
  • {{cite journal | vauthors = Sato M, Nakazawa M, Usui T, Tanimoto N, Abe H, Ohguro H | title = Mutations in the gene coding for guanylate cyclase-activating protein 2 (GUCA1B gene) in patients with autosomal dominant retinal dystrophies | journal = Graefe's Archive for Clinical and Experimental Ophthalmology = Albrecht von Graefes Archiv für Klinische und Experimentelle Ophthalmologie | volume = 243 | issue = 3 | pages = 235–42 | date = March 2005 | pmid = 15452722 | doi = 10.1007/s00417-004-1015-7 | s2cid = 23347858 }}

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