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Protein

V-type proton ATPase subunit E 1

Gene

Atp6v1e1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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

  • ATP hydrolysis coupled proton transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-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 E 1
Short name:
V-ATPase subunit E 1
Alternative name(s):
V-ATPase 31 kDa subunit
Short name:
p31
Vacuolar proton pump subunit E 1
Gene namesi
Name:Atp6v1e1
Synonyms:Atp6e, Atp6e2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:894326. Atp6v1e1.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • endosome Source: UniProtKB
  • extracellular exosome Source: MGI
  • lysosomal membrane Source: MGI
  • microvillus Source: UniProtKB
  • mitochondrion Source: MGI
  • proton-transporting two-sector ATPase complex, catalytic domain Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 226225V-type proton ATPase subunit E 1PRO_0000117296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei56 – 561PhosphotyrosineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP50518.
MaxQBiP50518.
PaxDbiP50518.
PRIDEiP50518.

PTM databases

iPTMnetiP50518.
PhosphoSiteiP50518.

Expressioni

Tissue specificityi

Expressed within the midpiece of sperm tail (at protein level). Ubiquitous.2 Publications

Gene expression databases

BgeeiP50518.
CleanExiMM_ATP6V1E1.
ExpressionAtlasiP50518. baseline and differential.
GenevisibleiP50518. 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). Interacts with ALDOC. Interacts with RAB11B (By similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiP50518. 7 interactions.
MINTiMINT-4139807.
STRINGi10090.ENSMUSP00000019354.

Structurei

3D structure databases

ProteinModelPortaliP50518.
SMRiP50518. Positions 2-217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase E subunit family.Curated

Phylogenomic databases

eggNOGiKOG1664. Eukaryota.
COG1390. LUCA.
GeneTreeiENSGT00390000002730.
HOGENOMiHOG000202506.
HOVERGENiHBG002309.
InParanoidiP50518.
KOiK02150.
OMAiEYQTVLT.
OrthoDBiEOG70PC01.
PhylomeDBiP50518.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P50518-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR
60 70 80 90 100
LKIMEYYEKK EKQIEQQKKI QMSNLMNQAR LKVLRARDDL ITDLLNEAKQ
110 120 130 140 150
RLSKVVKDTT RYQVLLDGLV LQGLYQLLEP RMIVRCRKQD FPLVKAAVQK
160 170 180 190 200
AIPMYKIATK KDVDVQIDQE AYLPEEIAGG VEIYNGDRKI KVSNTLESRL
210 220
DLIAQQMMPE VRGALFGANA NRKFLD
Length:226
Mass (Da):26,157
Last modified:April 3, 2007 - v2
Checksum:i5DD7B0EAB181EA08
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 54ALSD → GLRH in AAC52412 (PubMed:8741845).Curated
Sequence conflicti29 – 291E → EE in AAC52412 (PubMed:8741845).Curated
Sequence conflicti46 – 472VQ → LE in AAC52412 (PubMed:8741845).Curated
Sequence conflicti65 – 651E → R in AAC52412 (PubMed:8741845).Curated
Sequence conflicti67 – 671Q → QQ in AAC52412 (PubMed:8741845).Curated
Sequence conflicti86 – 861A → T in BAB92084 (PubMed:11872743).Curated
Sequence conflicti103 – 1031S → M in AAC52412 (PubMed:8741845).Curated
Sequence conflicti153 – 1531P → T in BAE26943 (PubMed:16141072).Curated
Sequence conflicti161 – 1611K → R in AAC52412 (PubMed:8741845).Curated
Sequence conflicti171 – 1766AYLPEE → PTCLRN in AAC52412 (PubMed:8741845).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13841 Genomic DNA. Translation: AAC52412.1.
AB074758 mRNA. Translation: BAB92084.1.
AK146162 mRNA. Translation: BAE26943.1.
AK149356 mRNA. Translation: BAE28832.1.
AK167644 mRNA. Translation: BAE39695.1.
AK169854 mRNA. Translation: BAE41412.1.
BC003421 mRNA. Translation: AAH03421.1.
BC055438 mRNA. Translation: AAH55438.1.
CCDSiCCDS20484.1.
RefSeqiNP_031536.2. NM_007510.2.
UniGeneiMm.29045.

Genome annotation databases

EnsembliENSMUST00000019354; ENSMUSP00000019354; ENSMUSG00000019210.
GeneIDi11973.
KEGGimmu:11973.
UCSCiuc009dnr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13841 Genomic DNA. Translation: AAC52412.1.
AB074758 mRNA. Translation: BAB92084.1.
AK146162 mRNA. Translation: BAE26943.1.
AK149356 mRNA. Translation: BAE28832.1.
AK167644 mRNA. Translation: BAE39695.1.
AK169854 mRNA. Translation: BAE41412.1.
BC003421 mRNA. Translation: AAH03421.1.
BC055438 mRNA. Translation: AAH55438.1.
CCDSiCCDS20484.1.
RefSeqiNP_031536.2. NM_007510.2.
UniGeneiMm.29045.

3D structure databases

ProteinModelPortaliP50518.
SMRiP50518. Positions 2-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP50518. 7 interactions.
MINTiMINT-4139807.
STRINGi10090.ENSMUSP00000019354.

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

iPTMnetiP50518.
PhosphoSiteiP50518.

Proteomic databases

EPDiP50518.
MaxQBiP50518.
PaxDbiP50518.
PRIDEiP50518.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019354; ENSMUSP00000019354; ENSMUSG00000019210.
GeneIDi11973.
KEGGimmu:11973.
UCSCiuc009dnr.1. mouse.

Organism-specific databases

CTDi529.
MGIiMGI:894326. Atp6v1e1.

Phylogenomic databases

eggNOGiKOG1664. Eukaryota.
COG1390. LUCA.
GeneTreeiENSGT00390000002730.
HOGENOMiHOG000202506.
HOVERGENiHBG002309.
InParanoidiP50518.
KOiK02150.
OMAiEYQTVLT.
OrthoDBiEOG70PC01.
PhylomeDBiP50518.
TreeFamiTF313479.

Enzyme and pathway databases

ReactomeiR-MMU-77387. Insulin receptor recycling.
R-MMU-917977. Transferrin endocytosis and recycling.
R-MMU-983712. Ion channel transport.

Miscellaneous databases

ChiTaRSiAtp6v1e1. mouse.
NextBioi280099.
PROiP50518.
SOURCEiSearch...

Gene expression databases

BgeeiP50518.
CleanExiMM_ATP6V1E1.
ExpressionAtlasiP50518. baseline and differential.
GenevisibleiP50518. MM.

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. "Resorption-cycle-dependent polarization of mRNAs for different subunits of V-ATPase in bone-resorbing osteoclasts."
    Laitala T., Howell M.L., Dean G.E., Vaananen H.K.
    Mol. Biol. Cell 7:129-142(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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], TISSUE SPECIFICITY.
  3. "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, DBA/2J and NOD.
    Tissue: Placenta and Retina.
  4. "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: Czech II and FVB/N.
    Tissue: Mammary tumor.
  5. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 14-26; 35-43; 54-60; 71-82; 86-101; 112-131; 140-147; 200-214 AND 215-224, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  6. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "RAB-like 2 has an essential role in male fertility, sperm intra-flagellar transport, and tail assembly."
    Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J., Whisstock J.C., Field M.C., Adams V., Ishikawa T., Aitken R.J., Whittle B., Goodnow C.C., Ormandy C.J., O'Bryan M.K.
    PLoS Genet. 8:E1002969-E1002969(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABL2, TISSUE SPECIFICITY.

Entry informationi

Entry nameiVATE1_MOUSE
AccessioniPrimary (citable) accession number: P50518
Secondary accession number(s): Q3UK59, Q8K5D6, Q99LD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 3, 2007
Last modified: May 11, 2016
This is version 136 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.