ATPase ASNA1

ASNA1
Identifiers
Aliases	ASNA1 , ARSA-I, ARSA1, ASNA-I, GET3, TRC40, hASNA-I, arsA arsenite transporter, ATP-binding, homolog 1 (bacterial)
External IDs	OMIM: 601913 MGI: 1928379 HomoloGene: 31513 GeneCards: ASNA1
Gene location (Human)
Chr.	Chromosome 19 (human)
End	12,748,323 bp
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)
End	85,751,910 bp
RNA expression pattern
	Top expressed in
	monocyte; ; stromal cell of endometrium; ; prefrontal cortex; ; Right adrenal gland; ; Left adrenal gland; ; islet of Langerhans; ; cingulate gyrus; ; left ventricle; ; body of stomach; ; nucleus accumbens;
	Top expressed in
	yolk sac; ; superior frontal gyrus; ; medulla oblongata; ; lip; ; entorhinal cortex; ; medial vestibular nucleus; ; cerebellar cortex; ; inferior colliculus; ; spermatid; ; maxillary prominence;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	nucleotide binding ; ATPase activity ; protein binding ; hydrolase activity ; ATP binding ; arsenite transmembrane transporter activity ; metal ion binding ; transporter activity ; ATPase-coupled transmembrane transporter activity ;
Cellular component	cytoplasm ; nucleolus ; extracellular exosome ; endoplasmic reticulum membrane ; nucleus ; endoplasmic reticulum ; GET complex ;
Biological process	IRE1-mediated unfolded protein response ; inorganic anion transport ; transport ; posttranslational protein targeting to endoplasmic reticulum membrane ; arsenite transport ; protein insertion into ER membrane ; tail-anchored membrane protein insertion into ER membrane ;
	Sources:Amigo / QuickGO
Orthologs
	439
	56495
	ENSG00000198356
	ENSMUSG00000052456
	O43681
	O54984
	NM_004317
	NM_019652 ; NM_001357202 ; NM_001357203
	NP_004308 ; NP_001358417 ; NP_001358418
	NP_062626 ; NP_001344131 ; NP_001344132
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated September 30, 2022

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.^[5]^[6]

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.^[6]

Interactions

ASNA1 is found to interact with FAM71D according to STRING ^[7]

Related Research Articles

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In molecular biology, the ars operon is an operon found in several bacterial taxon. It is required for the detoxification of arsenate, arsenite, and antimonite. This system transports arsenite and antimonite out of the cell. The pump is composed of two polypeptides, the products of the arsA and arsB genes. This two-subunit enzyme produces resistance to arsenite and antimonite. Arsenate, however, must first be reduced to arsenite before it is extruded. A third gene, arsC, expands the substrate specificity to allow for arsenate pumping and resistance. ArsC is an approximately 150-residue arsenate reductase that uses reduced glutathione (GSH) to convert arsenate to arsenite with a redox active cysteine residue in the active site. ArsC forms an active quaternary complex with GSH, arsenate, and glutaredoxin 1 (Grx1). The three ligands must be present simultaneously for reduction to occur.

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Arsenite-antimonite transporters are membrane transporters that pump arsenite or antimonite out of a cell. Antimonite is the salt of antimony and has been found to significantly impact the toxicity of arsenite. The similar structure of As(III) and Sb(III) makes it plausible that certain transporters function in the efflux of both substrates. Arsenic efflux transporters exist in almost every organism and serve to remove this toxic compound from the cell.

Arsenite resistance (Ars) efflux pumps of bacteria may consist of two proteins, ArsB and ArsA, or of one protein. ArsA proteins have two ATP binding domains and probably arose by a tandem gene duplication event. ArsB proteins all possess twelve transmembrane spanners and may also have arisen by a tandem gene duplication event. Structurally, the Ars pumps resemble ABC-type efflux pumps, but there is no significant sequence similarity between the Ars and ABC pumps. When only ArsB is present, the system operates by a pmf-dependent mechanism, and consequently belongs in TC subclass 2.A. When ArsA is also present, ATP hydrolysis drives efflux, and consequently the system belongs in TC subclass 3.A. ArsB therefore appears twice in the TC system but ArsA appears only once. These pumps actively expel both arsenite and antimonite.

The arsenical resistance-3 (ACR3) family is a member of the BART superfamily. Based on operon analyses, ARC3 homologues may function either as secondary carriers or as primary active transporters, similarly to the ArsB and ArsAB families. In the latter case ATP hydrolysis again energizes transport. ARC3 homologues transport the same anions as ArsA/AB homologues, though ArsB homologues are members of the IT Superfamily and homologues of the ARC3 family are within the BART Superfamily suggesting they may not be evolutionarily related.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000198356 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000052456 - 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.
↑ 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.
1 2 "Entrez Gene: ASNA1 arsA arsenite transporter, ATP-binding, homolog 1 (bacterial)".
↑ "STRING 10".

External links

Human ASNA1 genome location and ASNA1 gene details page in the UCSC Genome Browser .