Q9D1K2 (VATF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
V-type proton ATPase subunit F
Short name=V-ATPase subunit F

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

Gene names

Name:	Atp6v1f
Synonyms:	Atp6s14, Vatf

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	119 AA.
Sequence status	Complete.
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 a 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
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular_component	proton-transporting V-type ATPase, V1 domain Inferred from electronic annotation. Source: InterPro
Molecular_function	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_0000144800
Experimental info
	Sequence conflict	35	1	N → D in BAB22780. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9D1K2 [UniParc]. Last modified May 10, 2004. Version 2. Checksum: 9FFA95BD2667AA2A	FASTA	119	13,370
	10 20 30 40 50 60 MAGRGKLIAV IGDEDTVTGF LLGGIGELNK NRHPNFLVVE KDTTINEIED TFRQFLNRDD 70 80 90 100 110 IGIILINQYI AEMVRHALDA HQRSIPAVLE IPSKEHPYDA AKDSILRRAK GMFTAEDLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow, Embryo and Pancreas.
[2]	"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]. Strain: C57BL/6J. Tissue: Mammary tumor.
[3]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 42-53, MASS SPECTROMETRY. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK003419 mRNA. Translation: BAB22780.1. AK007327 mRNA. Translation: BAB24962.1. AK152153 mRNA. Translation: BAE30988.1. AK152929 mRNA. Translation: BAE31604.1. AK152959 mRNA. Translation: BAE31622.1. BC016553 mRNA. Translation: AAH16553.1.
IPI	IPI00315999.
RefSeq	NP_079657.1. NM_025381.2.
UniGene	Mm.371614.
3D structure databases
ProteinModelPortal	Q9D1K2.
SMR	Q9D1K2. Positions 8-109.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9D1K2. 1 interaction.
PTM databases
PhosphoSite	Q9D1K2.
2D gel databases
REPRODUCTION-2DPAGE	Q9D1K2.
Proteomic databases
PaxDb	Q9D1K2.
PRIDE	Q9D1K2.
Protocols and materials databases
DNASU	66144.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000004396; ENSMUSP00000004396; ENSMUSG00000004285.
GeneID	66144.
KEGG	mmu:66144.
UCSC	uc009bdp.1. mouse.
Organism-specific databases
CTD	9296.
MGI	MGI:1913394. Atp6v1f.
Phylogenomic databases
eggNOG	COG1436.
GeneTree	ENSGT00390000013208.
HOGENOM	HOG000056545.
HOVERGEN	HBG004488.
InParanoid	Q9D1K2.
KO	K02151.
OMA	HPYDPEK.
OrthoDB	EOG408N9G.
Gene expression databases
Bgee	Q9D1K2.
CleanEx	MM_ATP6V1F.
Genevestigator	Q9D1K2.
GermOnline	ENSMUSG00000004285. Mus musculus.
Family and domain databases
InterPro	IPR008218. ATPase_V1-cplx_f_g_su. IPR005772. ATPase_V1-cplx_fsu_euk. [Graphical view]
PANTHER	PTHR13861. PTHR13861. 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
ChiTaRS	ATP6V1F. mouse.
NextBio	320762.
SOURCE	Search...

Entry information

Entry name

VATF_MOUSE

Accession

Primary (citable) accession number: Q9D1K2
Secondary accession number(s): Q3U6X0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 10, 2004
Last modified:	May 1, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program