ATPase ASNA1

ArsA arsenite transporter, ATP-binding, homolog 1 (bacterial)
Identifiers
Symbols	ASNA1 ; ARSA-I; ARSA1; ASNA-I; GET3; TRC40; hASNA-I
External IDs	OMIM: 601913 MGI: 1928379 HomoloGene: 31513 GeneCards: ASNA1 Gene
EC number	3.6.3.16
Gene ontology Molecular function • transporter activity • protein binding • ATP binding • arsenite transmembrane transporter activity • ATPase activity • metal ion binding Cellular component • nucleus • nucleolus • cytoplasm • endoplasmic reticulum membrane • extracellular exosome Biological process • transport • inorganic anion transport • endoplasmic reticulum unfolded protein response • IRE1-mediated unfolded protein response • cellular protein metabolic process • protein insertion into ER membrane Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	439	56495
Ensembl	ENSG00000198356	ENSMUSG00000052456
UniProt	O43681	O54984
RefSeq (mRNA)	NM_004317	NM_019652
RefSeq (protein)	NP_004308	NP_062626
Location (UCSC)	Chr 19: 12.74 – 12.75 Mb	Chr 8: 85.02 – 85.03 Mb
PubMed search

ATPase ASNA1 also known as arsenical pump-driving ATPase and arsenite-stimulated ATPase is an enzyme that in humans is encoded by the ASNA1 gene.^[1][2]

Function

ASNA1 is the human homolog of the bacterial arsA gene. In E. coli, arsA ATPase is the catalytic component of a multisubunit oxyanion pump that is responsible for resistance to arsenicals and antimonials.^[2]

Interactions

ASNA1 is found to interact with FAM71D according to STRING ^[3]

References

1. Kurdi-Haidar B, Aebi S, Heath D, Enns RE, Naredi P, Hom DK, Howell SB (Feb 1997). "Isolation of the ATP-binding human homolog of the arsA component of the bacterial arsenite transporter". Genomics 36 (3): 486–91. doi:10.1006/geno.1996.0494. PMID 8884272.
2. "Entrez Gene: ASNA1 arsA arsenite transporter, ATP-binding, homolog 1 (bacterial)".
3. "STRING 10".

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Kurdi-Haidar B, Heath D, Aebi S, Howell SB (1998). "Biochemical characterization of the human arsenite-stimulated ATPase (hASNA-I).". J. Biol. Chem. 273 (35): 22173–6. doi:10.1074/jbc.273.35.22173. PMID 9712828.
• Kurdi-Haidar B, Hom DK, Flittner DE; et al. (1998). "Dual cytoplasmic and nuclear distribution of the novel arsenite-stimulated human ATPase (hASNA-I).". J. Cell. Biochem. 71 (1): 1–10. doi:10.1002/(SICI)1097-4644(19981001)71:1<1::AID-JCB1>3.0.CO;2-#. PMID 9736449.
• Kurdi-Haidar B, Heath D, Lennon G, Howell SB (2000). "Chromosomal localization and genomic structure of the human arsenite-stimulated ATPase (hASNA-I).". Somat. Cell Mol. Genet. 24 (5): 307–11. doi:10.1023/B:SCAM.0000007134.16744.8b. PMID 10696239.
• Kao G, Nordenson C, Still M; et al. (2007). "ASNA-1 positively regulates insulin secretion in C. elegans and mammalian cells.". Cell 128 (3): 577–87. doi:10.1016/j.cell.2006.12.031. PMID 17289575.
• Stefanovic S, Hegde RS (2007). "Identification of a targeting factor for posttranslational membrane protein insertion into the ER.". Cell 128 (6): 1147–59. doi:10.1016/j.cell.2007.01.036. PMID 17382883.