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P27449 (VATL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
V-type proton ATPase 16 kDa proteolipid subunit

Short name=V-ATPase 16 kDa proteolipid subunit
Alternative name(s):
Vacuolar proton pump 16 kDa proteolipid subunit
Gene names
Name:ATP6V0C
Synonyms:ATP6C, ATP6L, ATPL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length155 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_01396

Subunit structure

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein; which is present as a hexamer that forms the proton-conducting pore). Interacts with LASS2. Interacts with HTLV-1 accessory protein p12I. Interacts with RNF182; this interaction leads to ubiquitination and degradation via the proteasome pathway. Ref.6 Ref.7 Ref.8

Subcellular location

Vacuole membrane; Multi-pass membrane protein HAMAP-Rule MF_01396.

Post-translational modification

Ubiquitinated by RNF182, leading to its degradation via the ubiquitin-proteasome pathway. Ref.8

Sequence similarities

Belongs to the V-ATPase proteolipid subunit family.

Ontologies

Keywords
   Biological processHost-virus interaction
Hydrogen ion transport
Ion transport
Transport
   Cellular componentMembrane
Vacuole
   DomainTransmembrane
Transmembrane helix
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: InterPro

cellular iron ion homeostasis

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

interaction with host

Traceable author statement. Source: Reactome

phagosome maturation

Traceable author statement. Source: Reactome

proton transport

Traceable author statement Ref.1. Source: ProtInc

transferrin transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendosome membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of membrane

Traceable author statement Ref.1. Source: ProtInc

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

phagocytic vesicle membrane

Traceable author statement. Source: Reactome

proton-transporting V-type ATPase, V0 domain

Inferred from electronic annotation. Source: InterPro

   Molecular_functionprotein binding

Inferred from physical interaction Ref.7PubMed 1334459PubMed 21988832. Source: IntAct

proton-transporting ATP synthase activity, rotational mechanism

Traceable author statement Ref.1. Source: UniProtKB

proton-transporting ATPase activity, rotational mechanism

Traceable author statement Ref.1. Source: ProtInc

ubiquitin protein ligase binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CERS2Q96G233EBI-721179,EBI-1057080
E5P0CK452EBI-721179,EBI-7015490From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 155155V-type proton ATPase 16 kDa proteolipid subunit HAMAP-Rule MF_01396
PRO_0000071743

Regions

Topological domain1 – 1010Lumenal Potential
Transmembrane11 – 3323Helical; Potential
Topological domain34 – 5522Cytoplasmic Potential
Transmembrane56 – 7621Helical; Potential
Topological domain77 – 9216Lumenal Potential
Transmembrane93 – 11422Helical; Potential
Topological domain115 – 13117Cytoplasmic Potential
Transmembrane132 – 15221Helical; Potential
Topological domain153 – 1553Lumenal Potential

Sites

Site1391Essential for proton translocation By similarity

Sequences

Sequence LengthMass (Da)Tools
P27449 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 91141854A0492A5B

FASTA15515,736
        10         20         30         40         50         60 
MSESKSGPEY ASFFAVMGAS AAMVFSALGA AYGTAKSGTG IAAMSVMRPE QIMKSIIPVV 

        70         80         90        100        110        120 
MAGIIAIYGL VVAVLIANSL NDDISLYKSF LQLGAGLSVG LSGLAAGFAI GIVGDAGVRG 

       130        140        150 
TAQQPRLFVG MILILIFAEV LGLYGLIVAL ILSTK 

« Hide

References

« Hide 'large scale' references
[1]"CpG island in the region of an autosomal dominant polycystic kidney disease locus defines the 5' end of a gene encoding a putative proton channel."
Gillespie G.A.J., Somlo S., Germino G.G., Weinstat-Saslow D., Reeders S.T.
Proc. Natl. Acad. Sci. U.S.A. 88:4289-4293(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Muscle and Skin.
[5]"Vacuolar type H(+)-ATPase genes: presence of four genes including pseudogenes for the 16-kDa proteolipid subunit in the human genome."
Hasebe M., Hanada H., Moriyama Y., Maeda M., Futai M.
Biochem. Biophys. Res. Commun. 183:856-863(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-155.
[6]"Mapping of the intermolecular association of human T cell leukaemia/lymphotropic virus type I p12I and the vacuolar H+-ATPase 16 kDa subunit protein."
Koralnik I.J., Mulloy J.C., Andresson T., Fullen J., Franchini G.
J. Gen. Virol. 76:1909-1916(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I.
[7]"Cloning, mapping, and characterization of a human homologue of the yeast longevity assurance gene LAG1."
Pan H., Qin W.-X., Huo K.-K., Wan D.-F., Yu Y., Xu Z.-G., Hu Q.-D., Gu K.T., Zhou X.-M., Jiang H.-Q., Zhang P.-P., Huang Y., Li Y.-Y., Gu J.-R.
Genomics 77:58-64(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LASS2.
[8]"A novel brain-enriched E3 ubiquitin ligase RNF182 is up regulated in the brains of Alzheimer's patients and targets ATP6V0C for degradation."
Liu Q.Y., Lei J.X., Sikorska M., Liu R.
Mol. Neurodegener. 3:4-4(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF182, UBIQUITINATION.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62762 mRNA. Translation: AAA60039.1.
CR541930 mRNA. Translation: CAG46728.1.
CR541951 mRNA. Translation: CAG46749.1.
BT007155 mRNA. Translation: AAP35819.1.
BC004537 mRNA. Translation: AAH04537.1.
BC007389 mRNA. Translation: AAH07389.1.
BC007759 mRNA. Translation: AAH07759.1.
BC009290 mRNA. Translation: AAH09290.1.
CCDSCCDS10470.1.
PIRA39367.
RefSeqNP_001185498.1. NM_001198569.1.
NP_001685.1. NM_001694.3.
UniGeneHs.389107.

3D structure databases

ProteinModelPortalP27449.
SMRP27449. Positions 14-153.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107010. 4 interactions.
IntActP27449. 6 interactions.
MINTMINT-1414327.
STRING9606.ENSP00000329757.

PTM databases

PhosphoSiteP27449.

Polymorphism databases

DMDM137479.

Proteomic databases

MaxQBP27449.
PaxDbP27449.
PRIDEP27449.

Protocols and materials databases

DNASU527.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330398; ENSP00000329757; ENSG00000185883.
GeneID527.
KEGGhsa:527.
UCSCuc002cqn.3. human.

Organism-specific databases

CTD527.
GeneCardsGC16P002563.
HGNCHGNC:855. ATP6V0C.
MIM108745. gene.
neXtProtNX_P27449.
PharmGKBPA25149.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0636.
HOGENOMHOG000056520.
HOVERGENHBG002712.
InParanoidP27449.
KOK02155.
OMAMATELCP.
OrthoDBEOG7FV3RW.
PhylomeDBP27449.
TreeFamTF300025.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER66-34368.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

BgeeP27449.
CleanExHS_ATP6V0C.
GenevestigatorP27449.

Family and domain databases

HAMAPMF_01396. ATP_synth_c_bact.
InterProIPR002379. ATPase_proteolipid_c_like_dom.
IPR000245. ATPase_proteolipid_csu.
IPR011555. ATPase_proteolipid_su_C_euk.
[Graphical view]
PfamPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSPR00122. VACATPASE.
SUPFAMSSF81333. SSF81333. 2 hits.
TIGRFAMsTIGR01100. V_ATP_synt_C. 1 hit.
ProtoNetSearch...

Other

GeneWikiATP6V0C.
GenomeRNAi527.
NextBio2187.
PROP27449.
SOURCESearch...

Entry information

Entry nameVATL_HUMAN
AccessionPrimary (citable) accession number: P27449
Secondary accession number(s): Q6FH26
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM