Difference between revisions of "Phosphatase Family OCA"

From PhosphataseWiki
Jump to: navigation, search
 
(5 intermediate revisions by 2 users not shown)
Line 1: Line 1:
 
__NOTOC__
 
__NOTOC__
  
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]:  [[Phosphatase_Family_OCA|OCA]]
+
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]:  [[Phosphatase_Family_OCA|Family OCA]]
  
The OCA family is named after the five member genes in yeast (OCA1-5 = Oxidant-induced Cell-cycle Arrest). The family is also called plant and fungi atypical (PFA)-DSPs <cite>Pulido07 Pulido11</cite>.  
+
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>.  
  
 
=== Evolution ===
 
=== Evolution ===
OCA is found in most eukaryotes other than eumetazoa. We have seen it in fungi, plants, protists, monosiga, and sponge.
+
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 ===
 
=== Domain ===
Line 12: Line 12:
  
 
=== Functions ===
 
=== Functions ===
Yeast OCA members are involved in cell cycle arrest in response to oxidative damage<cite>Alic</cite>, in telomere capping <cite>lydall08</cite>, 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>.
+
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>.
  
 
=== References ===
 
=== References ===

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