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Protein

V-type proton ATPase proteolipid subunit

Gene

Atp6v0c

Organism
Mus musculus (Mouse)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transportUniRule annotation, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase proteolipid subunitUniRule annotation
Gene namesi
Name:Atp6v0cImported
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Organism-specific databases

MGIiMGI:88116. Atp6v0c.

Subcellular locationi

  • Vacuole membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3524HelicalUniRule annotationAdd
BLAST
Transmembranei56 – 7722HelicalUniRule annotationAdd
BLAST
Transmembranei89 – 11426HelicalUniRule annotationAdd
BLAST
Transmembranei126 – 15227HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, VacuoleUniRule annotation

PTM / Processingi

Proteomic databases

PaxDbiQ3UK60.
PRIDEiQ3UK60.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024932.

Structurei

3D structure databases

ProteinModelPortaliQ3UK60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 7660ATP-synt_CInterPro annotationAdd
BLAST
Domaini93 – 15260ATP-synt_CInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the V-ATPase proteolipid subunit family.UniRule annotationSAAS annotation

Keywords - Domaini

Transmembrane, Transmembrane helixUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG0232. Eukaryota.
COG0636. LUCA.
HOVERGENiHBG002712.

Family and domain databases

InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
IPR011555. ATPase_proteolipid_su_C_euk.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSiPR00122. VACATPASE.
SUPFAMiSSF81333. SSF81333. 2 hits.
TIGRFAMsiTIGR01100. V_ATP_synt_C. 1 hit.

Sequencei

Sequence statusi: Complete.

Q3UK60-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADIKNNPEY SSFFGVMGAS STMVFSAMGA AYGTAKSGTG IAAMSVMRPE
60 70 80 90 100
LIMKSIIPVV MAGIIAIYGL VVAVLIANSL TDGITLYRSF LQLGAGLSVG
110 120 130 140 150
LSGLAAGFAI GIVGDAGVRG TAQQPRLFVG MILILIFAEV LGLYGLIVAL

ILSTK
Length:155
Mass (Da):15,838
Last modified:October 11, 2005 - v1
Checksum:iC90C281C5BE77D40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146159 mRNA. Translation: BAE26942.1.
UniGeneiMm.294761.
Mm.30155.
Mm.320896.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146159 mRNA. Translation: BAE26942.1.
UniGeneiMm.294761.
Mm.30155.
Mm.320896.

3D structure databases

ProteinModelPortaliQ3UK60.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024932.

Proteomic databases

PaxDbiQ3UK60.
PRIDEiQ3UK60.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:88116. Atp6v0c.

Phylogenomic databases

eggNOGiKOG0232. Eukaryota.
COG0636. LUCA.
HOVERGENiHBG002712.

Miscellaneous databases

ChiTaRSiAtp6v0c. mouse.
SOURCEiSearch...

Family and domain databases

InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
IPR011555. ATPase_proteolipid_su_C_euk.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSiPR00122. VACATPASE.
SUPFAMiSSF81333. SSF81333. 2 hits.
TIGRFAMsiTIGR01100. V_ATP_synt_C. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "High-efficiency full-length cDNA cloning."
    Carninci P., Hayashizaki Y.
    Methods Enzymol. 303:19-44(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BALB/CImported.
  2. "Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes."
    Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.
    Genome Res. 10:1617-1630(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BALB/CImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BALB/CImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BALB/CImported.
  5. "Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs."
    The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team
    Nature 420:563-573(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BALB/CImported.
  6. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BALB/CImported.
  7. "The Transcriptional Landscape of the Mammalian Genome."
    The FANTOM Consortium, Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group)
    Science 309:1559-1563(2005)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BALB/CImported.
  8. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BALB/CImported.

Entry informationi

Entry nameiQ3UK60_MOUSE
AccessioniPrimary (citable) accession number: Q3UK60
Entry historyi
Integrated into UniProtKB/TrEMBL: October 11, 2005
Last sequence update: October 11, 2005
Last modified: May 11, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.