ID   VA0E1_MOUSE             Reviewed;          81 AA.
AC   Q9CQD8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=V-type proton ATPase subunit e 1;
DE            Short=V-ATPase subunit e 1;
DE   AltName: Full=Vacuolar proton pump subunit e 1;
GN   Name=Atp6v0e1; Synonyms=Atp6v0e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Medulla oblongata, Ovary, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons (By similarity). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments and in some cell
CC       types, is targeted to the plasma membrane, where it is responsible for
CC       acidifying the extracellular environment (By similarity).
CC       {ECO:0000250|UniProtKB:O15342, ECO:0000250|UniProtKB:Q2KIB5}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC       similarity). {ECO:0000250|UniProtKB:O15342}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the V-ATPase e1/e2 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AK007610; BAB25133.1; -; mRNA.
DR   EMBL; AK013229; BAB28727.1; -; mRNA.
DR   EMBL; AK017760; BAB30911.1; -; mRNA.
DR   EMBL; AK030335; BAC26909.1; -; mRNA.
DR   EMBL; AK134836; BAE22305.1; -; mRNA.
DR   EMBL; AK159669; BAE35273.1; -; mRNA.
DR   EMBL; AK168015; BAE40002.1; -; mRNA.
DR   EMBL; BC024733; AAH24733.1; -; mRNA.
DR   CCDS; CCDS28554.1; -.
DR   PIR; JC7602; JC7602.
DR   RefSeq; NP_079548.1; NM_025272.2.
DR   AlphaFoldDB; Q9CQD8; -.
DR   SMR; Q9CQD8; -.
DR   BioGRID; 198266; 2.
DR   STRING; 10090.ENSMUSP00000127552; -.
DR   TCDB; 3.A.2.2.6; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   PhosphoSitePlus; Q9CQD8; -.
DR   PaxDb; Q9CQD8; -.
DR   PRIDE; Q9CQD8; -.
DR   Antibodypedia; 73907; 11 antibodies from 4 providers.
DR   DNASU; 11974; -.
DR   Ensembl; ENSMUST00000015719; ENSMUSP00000015719; ENSMUSG00000015575.
DR   Ensembl; ENSMUST00000167352; ENSMUSP00000127552; ENSMUSG00000015575.
DR   GeneID; 11974; -.
DR   KEGG; mmu:11974; -.
DR   UCSC; uc008beh.1; mouse.
DR   CTD; 11974; -.
DR   MGI; MGI:1328318; Atp6v0e.
DR   VEuPathDB; HostDB:ENSMUSG00000015575; -.
DR   eggNOG; KOG3500; Eukaryota.
DR   GeneTree; ENSGT00940000156866; -.
DR   HOGENOM; CLU_170555_0_1_1; -.
DR   InParanoid; Q9CQD8; -.
DR   OMA; AREWGNP; -.
DR   OrthoDB; 1613627at2759; -.
DR   PhylomeDB; Q9CQD8; -.
DR   TreeFam; TF300290; -.
DR   Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-MMU-77387; Insulin receptor recycling.
DR   Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-MMU-983712; Ion channel transport.
DR   BioGRID-ORCS; 11974; 16 hits in 74 CRISPR screens.
DR   ChiTaRS; Atp6v0e; mouse.
DR   PRO; PR:Q9CQD8; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9CQD8; protein.
DR   Bgee; ENSMUSG00000015575; Expressed in choroid plexus of fourth ventricle and 268 other tissues.
DR   ExpressionAtlas; Q9CQD8; baseline and differential.
DR   Genevisible; Q9CQD8; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; ISO:MGI.
DR   GO; GO:1902600; P:proton transmembrane transport; ISO:MGI.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR008389; ATPase_V0-cplx_e1/e2_su.
DR   InterPro; IPR017385; ATPase_V0-cplx_e1/e2_su_met.
DR   PANTHER; PTHR12263; PTHR12263; 1.
DR   Pfam; PF05493; ATP_synt_H; 1.
DR   PIRSF; PIRSF038097; V-ATP_synth_e1/e2; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..81
FT                   /note="V-type proton ATPase subunit e 1"
FT                   /id="PRO_0000270196"
FT   TOPO_DOM        1..7
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..81
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   81 AA;  9340 MW;  9A47F165D72B2A2D CRC64;
     MAYHGLTVPL IVMSVFWGFV GLLVPWFIPK GPNRGVIITM LVTCSVCCYL FWLIAILAQL
     NPLFGPQLKN ETIWYLKYHW P