Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9D593 (VATE2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Atp6v1e2
Synonyms:Atp6e1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 isessential for energy coupling involved in acidification of acrosome. Ref.1

Subunit structure

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).

Tissue specificity

Testis specific. Ref.1

Sequence similarities

Belongs to the V-ATPase E subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 226226V-type proton ATPase subunit E 2 HAMAP-Rule MF_00311
PRO_0000282345

Experimental info

Sequence conflict551D → G in AAH61059. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9D593 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: AE5F501F02B8F98F

FASTA22626,307
        10         20         30         40         50         60 
MALTDIDVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMDYFEKK 

        70         80         90        100        110        120 
EKQIEQQKKI QLSTMRNQAR ITVLRARDNL ILELLKDAKM RLSRIVSDEE IYQDLLDKLV 

       130        140        150        160        170        180 
LQALLRLLEP VMIVRCRPQD LHLVESAVLR AIPQYMRLCQ KHLEVQVDQT EHLPSNAAGG 

       190        200        210        220 
VEVYSSDQKI KVSNTLESRL NLAAMQKMPE IRGILFGDNT SRKFFT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB074757 mRNA. Translation: BAB92083.1.
AK015654 mRNA. Translation: BAB29919.1.
BC049547 mRNA. Translation: AAH49547.2.
BC061059 mRNA. Translation: AAH61059.1.
CCDSCCDS29009.1.
RefSeqNP_083397.3. NM_029121.3.
UniGeneMm.159369.

3D structure databases

ProteinModelPortalQ9D593.
SMRQ9D593. Positions 2-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid217076. 1 interaction.
IntActQ9D593. 3 interactions.
MINTMINT-4127094.

Protein family/group databases

TCDB3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteQ9D593.

Proteomic databases

PaxDbQ9D593.
PRIDEQ9D593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000065758; ENSMUSP00000065285; ENSMUSG00000053375.
GeneID74915.
KEGGmmu:74915.
UCSCuc008dul.1. mouse.

Organism-specific databases

CTD90423.
MGIMGI:1922165. Atp6v1e2.

Phylogenomic databases

eggNOGCOG1390.
GeneTreeENSGT00390000002730.
HOGENOMHOG000202506.
HOVERGENHBG002309.
InParanoidQ9D593.
KOK02150.
OMADVGKQIQ.
OrthoDBEOG70PC01.
PhylomeDBQ9D593.
TreeFamTF313479.

Gene expression databases

BgeeQ9D593.
CleanExMM_ATP6V1E2.
GenevestigatorQ9D593.

Family and domain databases

HAMAPMF_00311. ATP_synth_E_arch.
InterProIPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view]
PfamPF01991. vATP-synt_E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio341799.
PROQ9D593.
SOURCESearch...

Entry information

Entry nameVATE2_MOUSE
AccessionPrimary (citable) accession number: Q9D593
Secondary accession number(s): Q6P8U8, Q810S5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot