vha-13 V-type proton ATPase catalytic subunit A [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: vha-13
Official Full Name: V-type proton ATPase catalytic subunit A
Primary source: WormBase:WBGene00013025
Locus tag: CELE_Y49A3A.2
See related: AllianceGenome:WB:WBGene00013025
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Predicted to enable proton-transporting ATPase activity, rotational mechanism. Involved in lysosomal lumen acidification. Predicted to be part of proton-transporting V-type ATPase, V1 domain. Is expressed in body wall musculature; excretory cell; head; and intestine. Human ortholog(s) of this gene implicated in autosomal recessive cutis laxa type IID and developmental and epileptic encephalopathy 93. Orthologous to human ATP6V1A (ATPase H+ transporting V1 subunit A). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See vha-13 in Genome Data Viewer

Location:: chromosome: V

Exon count:: 3

Sequence:: Chromosome: V; NC_003283.11 (14351709..14354422)

Chromosome V - NC_003283.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003283.11

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

miR-1 coordinately regulates lysosomal v-ATPase and biogenesis to impact proteotoxicity and muscle function during aging.
Title: miR-1 coordinately regulates lysosomal v-ATPase and biogenesis to impact proteotoxicity and muscle function during aging.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Y49A3A.1 (e-PCR)
- UniSTS:317315

Y49A3A.2 (e-PCR)
- UniSTS:317316

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables proton-transporting ATP synthase activity, rotational mechanism	IEA Inferred from Electronic Annotation more info
enables proton-transporting ATPase activity, rotational mechanism	IBA Inferred from Biological aspect of Ancestor more info
enables proton-transporting ATPase activity, rotational mechanism	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in ATP metabolic process	IEA Inferred from Electronic Annotation more info
involved_in lysosomal lumen acidification	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in proton motive force-driven ATP synthesis	IEA Inferred from Electronic Annotation more info
involved_in proton transmembrane transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in proton transmembrane transport	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of proton-transporting V-type ATPase, V1 domain	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: V-type proton ATPase catalytic subunit A

NP_506559.1

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003283.11 Reference assembly

Range

14351709..14354422

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_074158.8 → NP_506559.1 V-type proton ATPase catalytic subunit A [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_506559.1

Status: REVIEWED

UniProtKB/Swiss-Prot

Q9XW92

Conserved Domains (4) summary

cd01134
Location:74 → 446

V_A-ATPase_A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. The Vacuolar (V-type) ATPase is found in the membranes of vacuoles, the golgi ...

TIGR01042
Location:6 → 598

V-ATPase_V1_A; V-type (H+)-ATPase V1, A subunit

pfam00306
Location:464 → 606

ATP-synt_ab_C; ATP synthase alpha/beta chain, C terminal domain

pfam02874
Location:10 → 72

ATP-synt_ab_N; ATP synthase alpha/beta family, beta-barrel domain