Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9D1K2

- VATF_MOUSE

UniProt

Q9D1K2 - VATF_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

V-type proton ATPase subunit F

Gene

Atp6v1f

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. proton-transporting ATPase activity, rotational mechanism Source: InterPro

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198515. Transferrin endocytosis and recycling.
REACT_233181. 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: Chromosome 6

Organism-specific databases

MGIiMGI:1913394. Atp6v1f.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. proton-transporting V-type ATPase, V1 domain Source: InterPro
  3. vacuolar proton-transporting V-type ATPase complex Source: Ensembl
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.
GenevestigatoriQ9D1K2.

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.

Structurei

3D structure databases

ProteinModelPortaliQ9D1K2.
SMRiQ9D1K2. Positions 7-91.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase F subunit family.Curated

Phylogenomic databases

eggNOGiCOG1436.
GeneTreeiENSGT00390000013208.
HOGENOMiHOG000056545.
HOVERGENiHBG004488.
InParanoidiQ9D1K2.
KOiK02151.
OMAiRHVIDAH.
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 .
CCDSi CCDS19960.1.
RefSeqi NP_079657.1. NM_025381.2.
UniGenei Mm.371614.

3D structure databases

ProteinModelPortali Q9D1K2.
SMRi Q9D1K2. Positions 7-91.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9D1K2. 4 interactions.
MINTi MINT-4139820.

Protein family/group databases

TCDBi 3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSitei Q9D1K2.

2D gel databases

REPRODUCTION-2DPAGE Q9D1K2.

Proteomic databases

MaxQBi Q9D1K2.
PaxDbi Q9D1K2.
PRIDEi Q9D1K2.

Protocols and materials databases

DNASUi 66144.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004396 ; ENSMUSP00000004396 ; ENSMUSG00000004285 .
GeneIDi 66144.
KEGGi mmu:66144.
UCSCi uc009bdp.1. mouse.

Organism-specific databases

CTDi 9296.
MGIi MGI:1913394. Atp6v1f.

Phylogenomic databases

eggNOGi COG1436.
GeneTreei ENSGT00390000013208.
HOGENOMi HOG000056545.
HOVERGENi HBG004488.
InParanoidi Q9D1K2.
KOi K02151.
OMAi RHVIDAH.
OrthoDBi EOG7JMGGM.
PhylomeDBi Q9D1K2.
TreeFami TF300080.

Enzyme and pathway databases

Reactomei REACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198515. Transferrin endocytosis and recycling.
REACT_233181. Insulin receptor recycling.

Miscellaneous databases

NextBioi 320762.
PROi Q9D1K2.
SOURCEi Search...

Gene expression databases

Bgeei Q9D1K2.
CleanExi MM_ATP6V1F.
Genevestigatori Q9D1K2.

Family and domain databases

Gene3Di 3.40.50.10580. 1 hit.
InterProi IPR008218. ATPase_V1-cplx_f_g_su.
IPR005772. ATPase_V1-cplx_fsu_euk.
[Graphical view ]
PANTHERi PTHR13861. PTHR13861. 1 hit.
Pfami PF01990. ATP-synt_F. 1 hit.
[Graphical view ]
PIRSFi PIRSF015945. ATPase_V1_F_euk. 1 hit.
SUPFAMi SSF159468. SSF159468. 1 hit.
TIGRFAMsi TIGR01101. V_ATP_synt_F. 1 hit.
ProtoNeti Search...

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: November 26, 2014
This is version 107 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