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Protein

V-type proton ATPase subunit F

Gene

Atp6v1f

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_290403. Transferrin endocytosis and recycling.
REACT_299823. Ion channel transport.
REACT_324664. Insulin receptor recycling.

Protein family/group databases

TCDBi3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Atp6v1f
Synonyms:Atp6s14, Vatf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1913394. Atp6v1f.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 119119V-type proton ATPase subunit FPRO_0000144800Add
BLAST

Proteomic databases

MaxQBiQ9D1K2.
PaxDbiQ9D1K2.
PRIDEiQ9D1K2.

2D gel databases

REPRODUCTION-2DPAGEQ9D1K2.

PTM databases

PhosphoSiteiQ9D1K2.

Expressioni

Gene expression databases

BgeeiQ9D1K2.
CleanExiMM_ATP6V1F.
GenevisibleiQ9D1K2. MM.

Interactioni

Subunit structurei

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).

Protein-protein interaction databases

IntActiQ9D1K2. 4 interactions.
MINTiMINT-4139820.
STRINGi10090.ENSMUSP00000004396.

Structurei

3D structure databases

ProteinModelPortaliQ9D1K2.
SMRiQ9D1K2. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase F subunit family.Curated

Phylogenomic databases

eggNOGiCOG1436.
GeneTreeiENSGT00390000013208.
HOGENOMiHOG000056545.
HOVERGENiHBG004488.
InParanoidiQ9D1K2.
KOiK02151.
OMAiRAKGMFN.
OrthoDBiEOG7JMGGM.
PhylomeDBiQ9D1K2.
TreeFamiTF300080.

Family and domain databases

Gene3Di3.40.50.10580. 1 hit.
InterProiIPR008218. ATPase_V1-cplx_f_g_su.
IPR005772. ATPase_V1-cplx_fsu_euk.
[Graphical view]
PANTHERiPTHR13861. PTHR13861. 1 hit.
PfamiPF01990. ATP-synt_F. 1 hit.
[Graphical view]
PIRSFiPIRSF015945. ATPase_V1_F_euk. 1 hit.
SUPFAMiSSF159468. SSF159468. 1 hit.
TIGRFAMsiTIGR01101. V_ATP_synt_F. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9D1K2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGRGKLIAV IGDEDTVTGF LLGGIGELNK NRHPNFLVVE KDTTINEIED
60 70 80 90 100
TFRQFLNRDD IGIILINQYI AEMVRHALDA HQRSIPAVLE IPSKEHPYDA
110
AKDSILRRAK GMFTAEDLR
Length:119
Mass (Da):13,370
Last modified:May 10, 2004 - v2
Checksum:i9FFA95BD2667AA2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351N → D in BAB22780 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19960.1.
RefSeqiNP_079657.1. NM_025381.2.
UniGeneiMm.371614.

Genome annotation databases

EnsembliENSMUST00000004396; ENSMUSP00000004396; ENSMUSG00000004285.
GeneIDi66144.
KEGGimmu:66144.
UCSCiuc009bdp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19960.1.
RefSeqiNP_079657.1. NM_025381.2.
UniGeneiMm.371614.

3D structure databases

ProteinModelPortaliQ9D1K2.
SMRiQ9D1K2. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D1K2. 4 interactions.
MINTiMINT-4139820.
STRINGi10090.ENSMUSP00000004396.

Protein family/group databases

TCDBi3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteiQ9D1K2.

2D gel databases

REPRODUCTION-2DPAGEQ9D1K2.

Proteomic databases

MaxQBiQ9D1K2.
PaxDbiQ9D1K2.
PRIDEiQ9D1K2.

Protocols and materials databases

DNASUi66144.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004396; ENSMUSP00000004396; ENSMUSG00000004285.
GeneIDi66144.
KEGGimmu:66144.
UCSCiuc009bdp.1. mouse.

Organism-specific databases

CTDi9296.
MGIiMGI:1913394. Atp6v1f.

Phylogenomic databases

eggNOGiCOG1436.
GeneTreeiENSGT00390000013208.
HOGENOMiHOG000056545.
HOVERGENiHBG004488.
InParanoidiQ9D1K2.
KOiK02151.
OMAiRAKGMFN.
OrthoDBiEOG7JMGGM.
PhylomeDBiQ9D1K2.
TreeFamiTF300080.

Enzyme and pathway databases

ReactomeiREACT_290403. Transferrin endocytosis and recycling.
REACT_299823. Ion channel transport.
REACT_324664. Insulin receptor recycling.

Miscellaneous databases

NextBioi320762.
PROiQ9D1K2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1K2.
CleanExiMM_ATP6V1F.
GenevisibleiQ9D1K2. MM.

Family and domain databases

Gene3Di3.40.50.10580. 1 hit.
InterProiIPR008218. ATPase_V1-cplx_f_g_su.
IPR005772. ATPase_V1-cplx_fsu_euk.
[Graphical view]
PANTHERiPTHR13861. PTHR13861. 1 hit.
PfamiPF01990. ATP-synt_F. 1 hit.
[Graphical view]
PIRSFiPIRSF015945. ATPase_V1_F_euk. 1 hit.
SUPFAMiSSF159468. SSF159468. 1 hit.
TIGRFAMsiTIGR01101. V_ATP_synt_F. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.

Entry informationi

Entry nameiVATF_MOUSE
AccessioniPrimary (citable) accession number: Q9D1K2
Secondary accession number(s): Q3U6X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: June 24, 2015
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.