Probable cation-transporting ATPase 13A2 is an enzyme that in humans is encoded by the ATP13A2 gene that is involved in the transport of divalent transition metal cations.[5][6][7] It appears to protect cells from manganese[8] and zinc toxicity,[9] possibly by causing cellular efflux and/or lysosomal sequestration; and from iron toxicity, possibly by preserving lysosome integrity against iron-induced lipid peroxidation.[10] However, it potentiates the toxic effects of cadmium and nickel on developing neurites,[11] and of the widely used herbicide paraquat[12] possibly by increasing polyamine uptake.[13]

ATP13A2
Identifiers
AliasesATP13A2, CLN12, HSA9947, KRPPD, PARK9, ATPase 13A2, SPG78, ATPase cation transporting 13A2
External IDsMGI: 1922022 HomoloGene: 56940 GeneCards: ATP13A2
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for ATP13A2
Genomic location for ATP13A2
Band1p36.13Start16,985,958 bp[1]
End17,011,928 bp[1]
RNA expression pattern
PBB GE ATP13A2 218608 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001141973
NM_001141974
NM_022089

NM_001164366
NM_029097

RefSeq (protein)

NP_001135445
NP_001135446
NP_071372
NP_001135445.1
NP_001135446.1

NP_001157838
NP_083373

Location (UCSC)Chr 1: 16.99 – 17.01 MbChr 4: 140.99 – 141.01 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Deficiency is associated with spastic paraplegia and Kufor-Rakeb syndrome, in which there is progressive parkinsonism with dementia.[14]

ReferencesEdit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000159363 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036622 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:".
  4. ^ "Mouse PubMed Reference:".
  5. ^ Schultheis PJ, Hagen TT, O'Toole KK, Tachibana A, Burke CR, McGill DL, Okunade GW, Shull GE (October 2004). "Characterization of the P5 subfamily of P-type transport ATPases in mice". Biochemical and Biophysical Research Communications. 323 (3): 731–8. doi:10.1016/j.bbrc.2004.08.156. PMID 15381061.
  6. ^ Ramirez A, Heimbach A, Gründemann J, Stiller B, Hampshire D, Cid LP, Goebel I, Mubaidin AF, Wriekat AL, Roeper J, Al-Din A, Hillmer AM, Karsak M, Liss B, Woods CG, Behrens MI, Kubisch C (October 2006). "Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase". Nature Genetics. 38 (10): 1184–91. doi:10.1038/ng1884. PMID 16964263.
  7. ^ "Entrez Gene: ATP13A2 ATPase type 13A2".
  8. ^ Tan J, Zhang T, Jiang L, Chi J, Hu D, Pan Q, Wang D, Zhang Z (August 2011). "Regulation of intracellular manganese homeostasis by Kufor-Rakeb syndrome-associated ATP13A2 protein". The Journal of Biological Chemistry. 286 (34): 29654–62. doi:10.1074/jbc.M111.233874. PMC 3191006. PMID 21724849.
  9. ^ Tsunemi T, Krainc D (June 2014). "Zn²⁺ dyshomeostasis caused by loss of ATP13A2/PARK9 leads to lysosomal dysfunction and alpha-synuclein accumulation". Human Molecular Genetics. 23 (11): 2791–801. doi:10.1093/hmg/ddt572. PMC 4014186. PMID 24334770.
  10. ^ Rinaldi DE, Corradi GR, Cuesta LM, Adamo HP, de Tezanos Pinto F (August 2015). "The Parkinson-associated human P5B-ATPase ATP13A2 protects against the iron-induced cytotoxicity". Biochimica et Biophysica Acta. 1848 (8): 1646–55. doi:10.1016/j.bbamem.2015.04.008. PMID 25912790.
  11. ^ Podhajska A, Musso A, Trancikova A, Stafa K, Moser R, Sonnay S, Glauser L, Moore DJ (2012-06-29). "Common pathogenic effects of missense mutations in the P-type ATPase ATP13A2 (PARK9) associated with early-onset parkinsonism". PLoS One. 7 (6): e39942. doi:10.1371/journal.pone.0039942. PMC 3386943. PMID 22768177.
  12. ^ Pinto F, Corradi GR, Hera DP, Adamo HP (February 2012). "CHO cells expressing the human P₅-ATPase ATP13A2 are more sensitive to the toxic effects of herbicide paraquat". Neurochemistry International. 60 (3): 243–8. doi:10.1016/j.neuint.2012.01.002. PMID 22265822.
  13. ^ De La Hera DP, Corradi GR, Adamo HP, De Tezanos Pinto F (February 2013). "Parkinson's disease-associated human P5B-ATPase ATP13A2 increases spermidine uptake". The Biochemical Journal. 450 (1): 47–53. doi:10.1042/BJ20120739. PMID 23205587.
  14. ^ Online Mendelian Inheritance in Man (OMIM) ATPase, TYPE 13A2; ATP13A2 -610513

External linksEdit

Further readingEdit