P27449 (VATL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	155 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.
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 process	Host-virus interaction Hydrogen ion transport Ion transport Transport
Cellular component	Membrane Vacuole
Domain	Transmembrane Transmembrane helix
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP 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 transferrin transport Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endosome membrane Traceable author statement. Source: Reactome integral to membrane Traceable author statement Ref.1. Source: ProtInc phagocytic vesicle membrane Traceable author statement. Source: Reactome proton-transporting V-type ATPase, V0 domain Inferred from electronic annotation. Source: InterPro vacuolar membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CERS2	Q96G23	3	EBI-721179,EBI-1057080

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 155	155	V-type proton ATPase 16 kDa proteolipid subunit		PRO_0000071743
Regions
	Topological domain	1 – 10	10	Lumenal Potential
	Transmembrane	11 – 33	23	Helical; Potential
	Topological domain	34 – 55	22	Cytoplasmic Potential
	Transmembrane	56 – 76	21	Helical; Potential
	Topological domain	77 – 92	16	Lumenal Potential
	Transmembrane	93 – 114	22	Helical; Potential
	Topological domain	115 – 131	17	Cytoplasmic Potential
	Transmembrane	132 – 152	21	Helical; Potential
	Topological domain	153 – 155	3	Lumenal Potential
Sites
	Site	139	1	Essential for proton translocation By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27449 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 91141854A0492A5B	FASTA	155	15,736
	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

References

	« Hide 'large scale' referencesShow '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.
IPI	IPI00018855.
PIR	A39367.
RefSeq	NP_001185498.1. NM_001198569.1. NP_001685.1. NM_001694.3.
UniGene	Hs.389107.
3D structure databases
ProteinModelPortal	P27449.
ModBase	Search...
Protein-protein interaction databases
IntAct	P27449. 3 interactions.
MINT	MINT-1414327.
STRING	9606.ENSP00000329757.
PTM databases
PhosphoSite	P27449.
Polymorphism databases
DMDM	137479.
Proteomic databases
PaxDb	P27449.
PRIDE	P27449.
Protocols and materials databases
DNASU	527.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000330398; ENSP00000329757; ENSG00000185883. ENST00000568694; ENSP00000454796; ENSG00000185883.
GeneID	527.
KEGG	hsa:527.
UCSC	uc002cqn.3. human.
Organism-specific databases
CTD	527.
GeneCards	GC16P002563.
HGNC	HGNC:855. ATP6V0C.
MIM	108745. gene.
neXtProt	NX_P27449.
PharmGKB	PA25149.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0636.
HOGENOM	HOG000056520.
HOVERGEN	HBG002712.
InParanoid	P27449.
KO	K02155.
OMA	TCFGASY.
OrthoDB	EOG428231.
PhylomeDB	P27449.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_116125. Disease. REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	P27449.
Bgee	P27449.
CleanEx	HS_ATP6V0C.
Genevestigator	P27449.
GermOnline	ENSG00000185883. Homo sapiens.
Family and domain databases
InterPro	IPR002379. ATPase_proteolipid_c_like_dom. IPR000245. ATPase_proteolipid_csu. IPR011555. ATPase_proteolipid_su_C_euk. [Graphical view]
Pfam	PF00137. ATP-synt_C. 2 hits. [Graphical view]
PRINTS	PR00122. VACATPASE.
SUPFAM	SSF81333. ATPase_F0/V0_c. 2 hits.
TIGRFAMs	TIGR01100. V_ATP_synt_C. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	527.
NextBio	2187.
SOURCE	Search...

Entry information

Entry name

VATL_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.