Reviewed, UniProtKB/Swiss-Prot O15342 (VA0E1_HUMAN)

Names and origin

Protein names

Recommended name:
    V-type proton ATPase subunit e 1
      Short name=V-ATPase subunit e 1
Alternative name(s):
    Vacuolar proton pump subunit e 1
    V-ATPase 9.2 kDa membrane accessory protein
    V-ATPase M9.2 subunit

Gene names

Name:	ATP6V0E1
Synonyms:	ATP6H, ATP6V0E

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	81 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subunit structure	Composed of at least 10 subunits.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Tissue specificity	Ubiquitous. Ref.7
Sequence similarities	Belongs to the V-ATPase e subunit family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Membrane
Domain	Transmembrane
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro cell growth Ref.7 Inferred from genetic interaction. Source: UniProtKB vacuolar acidification Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Ref.1 Traceable author statement. Source: ProtInc proton-transporting V-type ATPase, V0 domain Inferred from electronic annotation. Source: InterPro
Molecular function	proton-transporting ATPase activity, rotational mechanism Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 81	80	V-type proton ATPase subunit e 1		PRO_0000071740
Regions
	Transmembrane	8 – 28	21	Potential
	Transmembrane	36 – 56	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	O15342-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9A47F16FDD2B2027	FASTA	81	9,374
	10 20 30 40 50 60 MAYHGLTVPL IVMSVFWGFV GFLVPWFIPK GPNRGVIITM LVTCSVCCYL FWLIAILAQL 70 80 NPLFGPQLKN ETIWYLKYHW P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules." Ludwig J., Kerscher S., Brandt U., Pfeiffer K., Getlawi F., Apps D.K., Schaegger H. J. Biol. Chem. 273:10939-10947(1998) [PubMed: 9556572] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[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 open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Molecular cloning and characterization of a novel form of the human vacuolar H+-ATPase e-subunit: an essential proton pump component." Blake-Palmer K.G., Su Y., Smith A.N., Karet F.E. Gene 393:94-100(2007) [PubMed: 17350184] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y15286 mRNA. Translation: CAA75571.1. Different initiation. CR456856 mRNA. Translation: CAG33137.1. CR542131 mRNA. Translation: CAG46928.1. AK312068 mRNA. Translation: BAG35004.1. CH471062 Genomic DNA. Translation: EAW61417.1. BC119714 mRNA. Translation: AAI19715.1. BC119715 mRNA. Translation: AAI19716.1.
IPI	IPI00217058.
RefSeq	NP_003936.1.
UniGene	Hs.484188
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O15342.
Genome annotation databases
Ensembl	ENST00000265093; ENSP00000265093; ENSG00000113732; Homo sapiens. [Genome view]
GeneID	8992.
KEGG	hsa:8992.
UCSC	uc003mcd.1. human.
Organism-specific databases
CTD	8992.
GeneCards	GC05P172344.
H-InvDB	HIX0032083.
HGNC	HGNC:863. ATP6V0E1.
MIM	603931. gene.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	O15342.
OMA	FVVPWFI
OrthoDB	EOG9F4VWF
Enzyme and pathway databases
BRENDA	3.6.3.14. 247.
Gene expression databases
ArrayExpress	O15342.
Bgee	O15342.
CleanEx	HS_ATP6V0E1.
Genevestigator	O15342.
GermOnline	ENSG00000113732. Homo sapiens.
Family and domain databases
InterPro	IPR008389. ATPase_V0-cplx_esu. IPR017385. ATPase_V0-cplx_esu_met. [Graphical view]
PANTHER	PTHR12263. ATPase_V0_H. 1 hit.
Pfam	PF05493. ATP_synt_H. 1 hit. [Graphical view]
PIRSF	PIRSF038097. V-ATP_synth_e1/e2. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	33719.
SOURCE	Search...

Entry information

Entry name

VA0E1_HUMAN

Accession

Primary (citable) accession number: O15342
Secondary accession number(s): B2R557, Q6IBE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.