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Protein

V-type proton ATPase subunit E 2

Gene

Atp6v1e2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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. This isoform is essential for energy coupling involved in acidification of acrosome.1 Publication

GO - Molecular functioni

  1. hydrogen-exporting ATPase activity, phosphorylative mechanism Source: MGI
  2. proton-transporting ATPase activity, rotational mechanism Source: InterPro

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: MGI
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 E 2
Short name:
V-ATPase subunit E 2
Alternative name(s):
Vacuolar proton pump subunit E 2
Gene namesi
Name:Atp6v1e2
Synonyms:Atp6e1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1922165. Atp6v1e2.

Subcellular locationi

GO - Cellular componenti

  1. acrosomal vesicle Source: MGI
  2. proton-transporting two-sector ATPase complex, catalytic domain Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 226226V-type proton ATPase subunit E 2PRO_0000282345Add
BLAST

Proteomic databases

MaxQBiQ9D593.
PaxDbiQ9D593.
PRIDEiQ9D593.

PTM databases

PhosphoSiteiQ9D593.

Expressioni

Tissue specificityi

Testis specific.1 Publication

Gene expression databases

BgeeiQ9D593.
CleanExiMM_ATP6V1E2.
GenevestigatoriQ9D593.

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

BioGridi217076. 1 interaction.
IntActiQ9D593. 3 interactions.
MINTiMINT-4127094.

Structurei

3D structure databases

ProteinModelPortaliQ9D593.
SMRiQ9D593. Positions 2-217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase E subunit family.Curated

Phylogenomic databases

eggNOGiCOG1390.
GeneTreeiENSGT00390000002730.
HOGENOMiHOG000202506.
HOVERGENiHBG002309.
InParanoidiQ9D593.
KOiK02150.
OMAiSGNQRIK.
OrthoDBiEOG70PC01.
PhylomeDBiQ9D593.
TreeFamiTF313479.

Family and domain databases

HAMAPiMF_00311. ATP_synth_E_arch.
InterProiIPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view]
PfamiPF01991. vATP-synt_E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D593-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALTDIDVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR
60 70 80 90 100
LKIMDYFEKK EKQIEQQKKI QLSTMRNQAR ITVLRARDNL ILELLKDAKM
110 120 130 140 150
RLSRIVSDEE IYQDLLDKLV LQALLRLLEP VMIVRCRPQD LHLVESAVLR
160 170 180 190 200
AIPQYMRLCQ KHLEVQVDQT EHLPSNAAGG VEVYSSDQKI KVSNTLESRL
210 220
NLAAMQKMPE IRGILFGDNT SRKFFT
Length:226
Mass (Da):26,307
Last modified:June 1, 2001 - v1
Checksum:iAE5F501F02B8F98F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551D → G in AAH61059 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB074757 mRNA. Translation: BAB92083.1.
AK015654 mRNA. Translation: BAB29919.1.
BC049547 mRNA. Translation: AAH49547.2.
BC061059 mRNA. Translation: AAH61059.1.
CCDSiCCDS29009.1.
RefSeqiNP_083397.3. NM_029121.3.
UniGeneiMm.159369.

Genome annotation databases

EnsembliENSMUST00000065758; ENSMUSP00000065285; ENSMUSG00000053375.
GeneIDi74915.
KEGGimmu:74915.
UCSCiuc008dul.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB074757 mRNA. Translation: BAB92083.1.
AK015654 mRNA. Translation: BAB29919.1.
BC049547 mRNA. Translation: AAH49547.2.
BC061059 mRNA. Translation: AAH61059.1.
CCDSiCCDS29009.1.
RefSeqiNP_083397.3. NM_029121.3.
UniGeneiMm.159369.

3D structure databases

ProteinModelPortaliQ9D593.
SMRiQ9D593. Positions 2-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217076. 1 interaction.
IntActiQ9D593. 3 interactions.
MINTiMINT-4127094.

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

PhosphoSiteiQ9D593.

Proteomic databases

MaxQBiQ9D593.
PaxDbiQ9D593.
PRIDEiQ9D593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065758; ENSMUSP00000065285; ENSMUSG00000053375.
GeneIDi74915.
KEGGimmu:74915.
UCSCiuc008dul.1. mouse.

Organism-specific databases

CTDi90423.
MGIiMGI:1922165. Atp6v1e2.

Phylogenomic databases

eggNOGiCOG1390.
GeneTreeiENSGT00390000002730.
HOGENOMiHOG000202506.
HOVERGENiHBG002309.
InParanoidiQ9D593.
KOiK02150.
OMAiSGNQRIK.
OrthoDBiEOG70PC01.
PhylomeDBiQ9D593.
TreeFamiTF313479.

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198515. Transferrin endocytosis and recycling.
REACT_233181. Insulin receptor recycling.

Miscellaneous databases

NextBioi341799.
PROiQ9D593.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D593.
CleanExiMM_ATP6V1E2.
GenevestigatoriQ9D593.

Family and domain databases

HAMAPiMF_00311. ATP_synth_E_arch.
InterProiIPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view]
PfamiPF01991. vATP-synt_E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidification."
    Sun-Wada G.H., Imai-Senga Y., Yamamoto A., Murata Y., Hirata T., Wada Y., Futai M.
    J. Biol. Chem. 277:18098-18105(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  2. "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: Testis.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiVATE2_MOUSE
AccessioniPrimary (citable) accession number: Q9D593
Secondary accession number(s): Q6P8U8, Q810S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.