Difference between revisions of "Phosphatase Family OCA"

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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_Cys-based_I|Superfamily Cys-based I]]:  [[Phosphatase_Family_OCA|OCA]]
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__NOTOC__
  
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OCA family is named after the five member genes in yeast. OCA stands for Oxidant-induced Cell-cycle Arrest. The physiological substrates of OCAs are still unclear. But, [[Gene_OCA3|OCA3]] has been shown to control intracellular localization of Gln3 (a phosphorylated transcriptional activator), in cooperation with Npr1 kinase <cite>Harashima08</cite>. OCAs also have been shown to be involved in telomere capping and uncapping <cite>lydall08</cite>.
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]:  [[Phosphatase_Family_OCA|Family OCA]]
  
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It is found in most if not all of eukaryotes except eumetazoan (i.e. fungi, plants, protists, monosiga, and sponge).
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The OCA family is named after the five member genes in yeast (OCA1-4, OCA6 = Oxidant-induced Cell-cycle Arrest). The family is also called Plant and Fungi Atypical (PFA)-DSPs <cite>Pulido07 Pulido11</cite>.  
  
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The family is also called as plant and fungi atypical (PFA)-DSPs <cite>Pulido07 Pulido11</cite>.
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=== Evolution ===
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The OCA family is found in many eukaryotes, including fungi, plants, protists, choanoflagellates (''Monosiga''), and sponge. It is absent from most eumetazoa, but is found in several invertebrate deuterostomes (the urchin (''Strongylocentrotus purpuratus''), lancelet (''Branchiostoma floridae'')) and even an early-branching vertebrate, the ghostshark (''Callorhinchus milii'') and a few protostomes: ''Capitella teleta'', the owl limpet (''Lottia gigantea''), and the leech (''Helobdella robusta'').
  
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===== Reference =====
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=== Domain ===
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<biblio>
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OCA has a single domain, a phosphatase domain of fold CC1.
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#Harashima08 pmid=18166280
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</biblio>
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=== Functions ===
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=== Reference ===
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Yeast OCA members are involved in cell cycle arrest in response to oxidative damage<cite>Alic</cite>, in telomere capping <cite>lydall08</cite>, and in actin organization <cite>Care</cite>. [[Gene_OCA3|OCA3]] has been shown to control intracellular localization of Gln3 (a phosphorylated transcriptional activator), in cooperation with Npr1 kinase <cite>Harashima08</cite>.
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=== References ===
 
<biblio>
 
<biblio>
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#Alic pmid=11408586
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#Care pmid=15020461
 
#Pulido07 pmid=17976645
 
#Pulido07 pmid=17976645
 
#Pulido11 pmid=21409566
 
#Pulido11 pmid=21409566

Latest revision as of 20:13, 14 August 2016


Phosphatase Classification: Fold CC1: Superfamily CC1: Family OCA

The OCA family is named after the five member genes in yeast (OCA1-4, OCA6 = Oxidant-induced Cell-cycle Arrest). The family is also called Plant and Fungi Atypical (PFA)-DSPs [1, 2].

Evolution

The OCA family is found in many eukaryotes, including fungi, plants, protists, choanoflagellates (Monosiga), and sponge. It is absent from most eumetazoa, but is found in several invertebrate deuterostomes (the urchin (Strongylocentrotus purpuratus), lancelet (Branchiostoma floridae)) and even an early-branching vertebrate, the ghostshark (Callorhinchus milii) and a few protostomes: Capitella teleta, the owl limpet (Lottia gigantea), and the leech (Helobdella robusta).

Domain

OCA has a single domain, a phosphatase domain of fold CC1.

Functions

Yeast OCA members are involved in cell cycle arrest in response to oxidative damage[3], in telomere capping [4], and in actin organization [5]. OCA3 has been shown to control intracellular localization of Gln3 (a phosphorylated transcriptional activator), in cooperation with Npr1 kinase [6].

References

  1. Romá-Mateo C, Ríos P, Tabernero L, Attwood TK, and Pulido R. A novel phosphatase family, structurally related to dual-specificity phosphatases, that displays unique amino acid sequence and substrate specificity. J Mol Biol. 2007 Dec 7;374(4):899-909. DOI:10.1016/j.jmb.2007.10.008 | PubMed ID:17976645 | HubMed [Pulido07]
  2. Romá-Mateo C, Sacristán-Reviriego A, Beresford NJ, Caparrós-Martín JA, Culiáñez-Macià FA, Martín H, Molina M, Tabernero L, and Pulido R. Phylogenetic and genetic linkage between novel atypical dual-specificity phosphatases from non-metazoan organisms. Mol Genet Genomics. 2011 Apr;285(4):341-54. DOI:10.1007/s00438-011-0611-6 | PubMed ID:21409566 | HubMed [Pulido11]
  3. Alic N, Higgins VJ, and Dawes IW. Identification of a Saccharomyces cerevisiae gene that is required for G1 arrest in response to the lipid oxidation product linoleic acid hydroperoxide. Mol Biol Cell. 2001 Jun;12(6):1801-10. DOI:10.1091/mbc.12.6.1801 | PubMed ID:11408586 | HubMed [Alic]
  4. Addinall SG, Downey M, Yu M, Zubko MK, Dewar J, Leake A, Hallinan J, Shaw O, James K, Wilkinson DJ, Wipat A, Durocher D, and Lydall D. A genomewide suppressor and enhancer analysis of cdc13-1 reveals varied cellular processes influencing telomere capping in Saccharomyces cerevisiae. Genetics. 2008 Dec;180(4):2251-66. DOI:10.1534/genetics.108.092577 | PubMed ID:18845848 | HubMed [lydall08]
  5. Care A, Vousden KA, Binley KM, Radcliffe P, Trevethick J, Mannazzu I, and Sudbery PE. A synthetic lethal screen identifies a role for the cortical actin patch/endocytosis complex in the response to nutrient deprivation in Saccharomyces cerevisiae. Genetics. 2004 Feb;166(2):707-19. DOI:10.1534/genetics.166.2.707 | PubMed ID:15020461 | HubMed [Care]
  6. Hirasaki M, Kaneko Y, and Harashima S. Protein phosphatase Siw14 controls intracellular localization of Gln3 in cooperation with Npr1 kinase in Saccharomyces cerevisiae. Gene. 2008 Feb 15;409(1-2):34-43. DOI:10.1016/j.gene.2007.11.005 | PubMed ID:18166280 | HubMed [Harashima08]
All Medline abstracts: PubMed | HubMed
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