Reviewed, UniProtKB/Swiss-Prot Q16864 (VATF_HUMAN)

Names and origin

Protein names

Recommended name:
    V-type proton ATPase subunit F
      Short name=V-ATPase subunit F
Alternative name(s):
    Vacuolar proton pump subunit F
    V-ATPase 14 kDa subunit

Gene names

Name:	ATP6V1F
Synonyms:	ATP6S14, VATF

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	119 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subunit structure	V-ATPase is an heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d).
Sequence similarities	Belongs to the V-ATPase F subunit family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Coding sequence diversity	Polymorphism
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	membrane fraction Non-traceable author statement. Source: UniProtKB proton-transporting V-type ATPase, V1 domain Inferred from electronic annotation. Source: InterPro vacuolar proton-transporting V-type ATPase complex Inferred from direct assay. Source: UniProtKB
Molecular function	ATPase activity, uncoupled Ref.1 Non-traceable author statement. Source: UniProtKB hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: UniProtKB proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 119	119	V-type proton ATPase subunit F		PRO_0000144799
Natural variations
	Natural variant	24	1	G → V: dbSNP rs10958.		VAR_048348
Experimental info
	Sequence conflict	8	1	I → T in BAA08392. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q16864-1 [UniParc]. Last modified February 20, 2007. Version 2. Checksum: 9FE5A8BD249A85FA	FASTA	119	13,370
	10 20 30 40 50 60 MAGRGKLIAV IGDEDTVTGF LLGGIGELNK NRHPNFLVVE KDTTINEIED TFRQFLNRDD 70 80 90 100 110 IGIILINQYI AEMVRHALDA HQQSIPAVLE IPSKEHPYDA AKDSILRRAR GMFTAEDLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing and expression of a novel cDNA encoding human vacuolar ATPase (14-kDa subunit)." Fujiwara T., Kawai A., Shimizu F., Hirano H., Okuno S., Takeda S., Ozaki K., Shimada Y., Nagata M., Watanabe T., Takaichi A., Nakamura Y., Shin S. DNA Res. 2:107-111(1995) [PubMed: 8581736] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[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]	"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]. Tissue: Brain.
[4]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D49400 mRNA. Translation: BAA08392.1. CR456896 mRNA. Translation: CAG33177.1. BC104230 mRNA. Translation: AAI04231.1. BC104231 mRNA. Translation: AAI04232.1. BC107854 mRNA. Translation: AAI07855.1.
IPI	IPI00004488.
PIR	JC4193.
RefSeq	NP_004222.2.
UniGene	Hs.78089
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q16864. 1 interaction.
Protein family/group databases
TCDB	3.A.2.2.4. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.
Proteomic databases
PeptideAtlas	Q16864.
PRIDE	Q16864.
Genome annotation databases
Ensembl	ENSG00000128524. Homo sapiens. [Contig view]
GeneID	9296.
KEGG	hsa:9296.
Organism-specific databases
GeneCards	GC07P128290.
HGNC	HGNC:16832. ATP6V1F.
HPA	CAB009529.
MIM	607160. gene.
PharmGKB	PA38421.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q16864.
HOVERGEN	Q16864.
OMA	Q16864. AILLINQ.
Enzyme and pathway databases
BRENDA	3.6.3.14. 247.
Gene expression databases
Bgee	Q16864.
CleanEx	HS_ATP6V1F.
GermOnline	ENSG00000128524. Homo sapiens.
Family and domain databases
InterPro	IPR005772. ATPase_V1-cplx_fsu_euk. IPR008218. ATPase_V1/A1-cplx_fsu. [Graphical view]
PANTHER	PTHR13861. ATPase_V1_F_euk. 1 hit.
Pfam	PF01990. ATP-synt_F. 1 hit. [Graphical view]
PIRSF	PIRSF015945. ATPase_V1_F_euk. 1 hit.
TIGRFAMs	TIGR01101. V_ATP_synt_F. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	34831.
SOURCE	Search...

Entry information

Entry name

VATF_HUMAN

Accession

Primary (citable) accession number: Q16864
Secondary accession number(s): Q6IBA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 20, 2007
Last modified:	June 16, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)