ATP13A2

Protein-coding gene found in humans

ATP13A2

Identifiers

Aliases

ATP13A2, CLN12, HSA9947, KRPPD, PARK9, ATPase 13A2, SPG78, ATPase cation transporting 13A2

External IDs

OMIM: 610513; MGI: 1922022; HomoloGene: 56940; GeneCards: ATP13A2; OMA:ATP13A2 - orthologs

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	1p36.13	Start	16,985,958 bp^[1]
Band	1p36.13	End	17,011,928 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	4\|4 D3	Start	140,714,184 bp^[2]
Band	4\|4 D3	End	140,734,641 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

right frontal lobe

right hemisphere of cerebellum

prefrontal cortex

anterior cingulate cortex

pons

Brodmann area 9

anterior pituitary

amygdala

hypothalamus

nucleus accumbens

Top expressed in

external carotid artery

internal carotid artery

stroma of bone marrow

dorsal tegmental nucleus

perirhinal cortex

neural layer of retina

motor neuron

entorhinal cortex

superior colliculus

superior frontal gyrus

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	nucleotide binding metal ion binding ATPase activity protein binding hydrolase activity ATP binding cupric ion binding phosphatidic acid binding zinc ion binding phosphatidylinositol-3,5-bisphosphate binding manganese ion binding P-type calcium transporter activity ATPase-coupled cation transmembrane transporter activity
Cellular component	integral component of membrane membrane vesicle membrane integral component of plasma membrane transport vesicle lysosomal lumen lysosome vesicle multivesicular body neuron projection integral component of lysosomal membrane multivesicular body membrane autophagosome late endosome neuronal cell body lysosomal membrane
Biological process	cellular cation homeostasis cation transport ion transmembrane transport regulation of autophagy of mitochondrion regulation of autophagosome size regulation of endopeptidase activity regulation of mitochondrion organization cellular response to oxidative stress cellular calcium ion homeostasis cellular response to manganese ion cellular iron ion homeostasis protein autophosphorylation cellular zinc ion homeostasis autophagosome organization regulation of glucosylceramidase activity regulation of chaperone-mediated autophagy negative regulation of neuron death zinc ion homeostasis regulation of macroautophagy regulation of intracellular protein transport positive regulation of protein secretion positive regulation of exosomal secretion peptidyl-aspartic acid autophosphorylation negative regulation of lysosomal protein catabolic process cellular response to zinc ion calcium ion transmembrane transport regulation of lysosomal protein catabolic process extracellular exosome biogenesis polyamine transmembrane transport
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


23400


74772

Ensembl


ENSG00000159363


ENSMUSG00000036622

UniProt


Q9NQ11 Q8N4D4


Q9CTG6

RefSeq (mRNA)


NM_001141973 NM_001141974 NM_022089

NM_001164366 NM_029097 NM_001379619 NM_001379620 NM_001379621
NM_001379622

RefSeq (protein)


NP_001135445 NP_001135446 NP_071372 NP_001135445.1 NP_001135446.1

NP_001157838 NP_083373 NP_001366548 NP_001366549 NP_001366550
NP_001366551

Location (UCSC)

Chr 1: 16.99 – 17.01 Mb

Chr 4: 140.71 – 140.73 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

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]

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

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000159363 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000036622 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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. S2CID 6502952.
^ "Entrez Gene: ATP13A2 ATPase type 13A2".
^ 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.
^ 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.
^ 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 (BBA) - Biomembranes. 1848 (8): 1646–55. doi:10.1016/j.bbamem.2015.04.008. hdl:11336/82017. PMID 25912790.
^ 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. Bibcode:2012PLoSO...739942P. doi:10.1371/journal.pone.0039942. PMC 3386943. PMID 22768177.
^ 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. S2CID 25893162.
^ 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. hdl:11336/18027. PMID 23205587.
^ Online Mendelian Inheritance in Man (OMIM): ATPase, TYPE 13A2; ATP13A2 - 610513