Q6AYE4 · VATC2_RAT

  • Protein
    V-type proton ATPase subunit C 2
  • Gene
    Atp6v1c2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

Function

function

Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentvacuolar proton-transporting V-type ATPase, V1 domain
Molecular Functionidentical protein binding
Molecular Functionproton-transporting ATPase activity, rotational mechanism
Biological Processpositive regulation of Wnt signaling pathway
Biological Processproton transmembrane transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    V-type proton ATPase subunit C 2
  • Short names
    V-ATPase subunit C 2
  • Alternative names
    • Vacuolar proton pump subunit C 2

Gene names

    • Name
      Atp6v1c2

Organism names

  • Taxonomic identifier
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q6AYE4
  • Secondary accessions
    • Q53B80

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002856711-425V-type proton ATPase subunit C 2

PTM databases

Expression

Tissue specificity

Lung, kidney and testis. Expressed in both bronchiolar and alveolar lung epithelial cells. Isoform 1 is predominantly expressed in the lung while isoform 2 is strongly expressed in the kidney and testis.

Interaction

Subunit

V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex. The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H. The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region295-318Disordered

Sequence similarities

Belongs to the V-ATPase C subunit family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q6AYE4-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    1
  • Synonyms
    C2-a
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    425
  • Mass (Da)
    48,243
  • Last updated
    2004-09-13 v1
  • Checksum
    698606392087372D
MSEFWLISAPGDKENLQALERMNSVTSKSNLSHNTKFAIPDFKVGTLDSLVGLSDELGKLDTFAESLIKRMAQSVVEVMEDSKGKVHENLLANGVDLTSFVTHFEWDMAKYPAKQPLVSVVDTLAKQLAQIETDLKSRTAAYSVLKANLENLEKKSTGNLFTRTLSDIVSKEDFVLDSEYLITLLVIVPKSSYVQWQKTYESLSDMVVPRSTKLIAEDNEGGLFTVTLFRKVIEDFKVKAKENKFIVREFYYDEKEIKREREEMTRLLSDKKQQYQTSCVALKKGSATYRDHKVKVTPLGNPTRPTAGQNDRESEGEGEGPLLRWLKVNFSEAFIAWIHIKALRVFVESVLRYGLPVNFQAVLLQPHKKSATKRLREVLNSVFRHLDEVAAASILDASVEIPGLQLSNQDYFPYVYFHIDLSLLD

Q6AYE4-2

  • Name
    2
  • Synonyms
    C2-b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0G2JZN3A0A0G2JZN3_RATAtp6v1c2435
M0RBN8M0RBN8_RATAtp6v1c2399

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict49in Ref. 1; AAT44904
Alternative sequenceVSP_024886276-319in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY594319
EMBL· GenBank· DDBJ
AAT44904.1
EMBL· GenBank· DDBJ
mRNA
BC079083
EMBL· GenBank· DDBJ
AAH79083.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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