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Q9D593

- VATE2_MOUSE

UniProt

Q9D593 - VATE2_MOUSE

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Protein

V-type proton ATPase subunit E 2

Gene
Atp6v1e2, Atp6e1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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.

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 2UniRule annotationPRO_0000282345Add
BLAST

Proteomic databases

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.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1390.
GeneTreeiENSGT00390000002730.
HOGENOMiHOG000202506.
HOVERGENiHBG002309.
InParanoidiQ9D593.
KOiK02150.
OMAiDVGKQIQ.
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

MALTDIDVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR    50
LKIMDYFEKK EKQIEQQKKI QLSTMRNQAR ITVLRARDNL ILELLKDAKM 100
RLSRIVSDEE IYQDLLDKLV LQALLRLLEP VMIVRCRPQD LHLVESAVLR 150
AIPQYMRLCQ KHLEVQVDQT EHLPSNAAGG VEVYSSDQKI KVSNTLESRL 200
NLAAMQKMPE IRGILFGDNT SRKFFT 226
Length:226
Mass (Da):26,307
Last modified:June 1, 2001 - v1
Checksum:iAE5F501F02B8F98F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551D → G in AAH61059. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AB074757 mRNA. Translation: BAB92083.1 .
AK015654 mRNA. Translation: BAB29919.1 .
BC049547 mRNA. Translation: AAH49547.2 .
BC061059 mRNA. Translation: AAH61059.1 .
CCDSi CCDS29009.1.
RefSeqi NP_083397.3. NM_029121.3.
UniGenei Mm.159369.

3D structure databases

ProteinModelPortali Q9D593.
SMRi Q9D593. Positions 2-217.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 217076. 1 interaction.
IntActi Q9D593. 3 interactions.
MINTi MINT-4127094.

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 Q9D593.

Proteomic databases

PaxDbi Q9D593.
PRIDEi Q9D593.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000065758 ; ENSMUSP00000065285 ; ENSMUSG00000053375 .
GeneIDi 74915.
KEGGi mmu:74915.
UCSCi uc008dul.1. mouse.

Organism-specific databases

CTDi 90423.
MGIi MGI:1922165. Atp6v1e2.

Phylogenomic databases

eggNOGi COG1390.
GeneTreei ENSGT00390000002730.
HOGENOMi HOG000202506.
HOVERGENi HBG002309.
InParanoidi Q9D593.
KOi K02150.
OMAi DVGKQIQ.
OrthoDBi EOG70PC01.
PhylomeDBi Q9D593.
TreeFami TF313479.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi 341799.
PROi Q9D593.
SOURCEi Search...

Gene expression databases

Bgeei Q9D593.
CleanExi MM_ATP6V1E2.
Genevestigatori Q9D593.

Family and domain databases

HAMAPi MF_00311. ATP_synth_E_arch.
InterProi IPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view ]
Pfami PF01991. vATP-synt_E. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 98 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

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