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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

ReactomeiR-MMU-1222556. ROS, RNS production in response to bacteria.
R-MMU-77387. Insulin receptor recycling.
R-MMU-917977. Transferrin endocytosis and recycling.
R-MMU-983712. Ion channel transport.

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
Proteomesi
  • UP000000589 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

EPDiQ9D1K2.
MaxQBiQ9D1K2.
PaxDbiQ9D1K2.
PeptideAtlasiQ9D1K2.
PRIDEiQ9D1K2.
TopDownProteomicsiQ9D1K2.

2D gel databases

REPRODUCTION-2DPAGEQ9D1K2.

PTM databases

iPTMnetiQ9D1K2.
PhosphoSiteiQ9D1K2.

Expressioni

Gene expression databases

BgeeiENSMUSG00000004285.
CleanExiMM_ATP6V1F.
ExpressionAtlasiQ9D1K2. baseline and differential.
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

eggNOGiKOG3432. Eukaryota.
COG1436. LUCA.
GeneTreeiENSGT00390000013208.
HOGENOMiHOG000056545.
HOVERGENiHBG004488.
InParanoidiQ9D1K2.
KOiK02151.
OMAiQNVAEMI.
OrthoDBiEOG091G0ZUA.
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

iPTMnetiQ9D1K2.
PhosphoSiteiQ9D1K2.

2D gel databases

REPRODUCTION-2DPAGEQ9D1K2.

Proteomic databases

EPDiQ9D1K2.
MaxQBiQ9D1K2.
PaxDbiQ9D1K2.
PeptideAtlasiQ9D1K2.
PRIDEiQ9D1K2.
TopDownProteomicsiQ9D1K2.

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

eggNOGiKOG3432. Eukaryota.
COG1436. LUCA.
GeneTreeiENSGT00390000013208.
HOGENOMiHOG000056545.
HOVERGENiHBG004488.
InParanoidiQ9D1K2.
KOiK02151.
OMAiQNVAEMI.
OrthoDBiEOG091G0ZUA.
PhylomeDBiQ9D1K2.
TreeFamiTF300080.

Enzyme and pathway databases

ReactomeiR-MMU-1222556. ROS, RNS production in response to bacteria.
R-MMU-77387. Insulin receptor recycling.
R-MMU-917977. Transferrin endocytosis and recycling.
R-MMU-983712. Ion channel transport.

Miscellaneous databases

PROiQ9D1K2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000004285.
CleanExiMM_ATP6V1F.
ExpressionAtlasiQ9D1K2. baseline and differential.
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...

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: September 7, 2016
This is version 121 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

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 one 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.