VA0E1_HUMAN
ID VA0E1_HUMAN Reviewed; 81 AA.
AC O15342; B2R557; D3DQM1; Q6IBE8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=V-type proton ATPase subunit e 1;
DE Short=V-ATPase subunit e 1;
DE AltName: Full=V-ATPase 9.2 kDa membrane accessory protein;
DE AltName: Full=V-ATPase M9.2 subunit;
DE AltName: Full=Vacuolar proton pump subunit e 1;
GN Name=ATP6V0E1; Synonyms=ATP6H, ATP6V0E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=9556572; DOI=10.1074/jbc.273.18.10939;
RA Ludwig J., Kerscher S., Brandt U., Pfeiffer K., Getlawi F., Apps D.K.,
RA Schaegger H.;
RT "Identification and characterization of a novel 9.2-kDa membrane sector-
RT associated protein of vacuolar proton-ATPase from chromaffin granules.";
RL J. Biol. Chem. 273:10939-10947(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17350184; DOI=10.1016/j.gene.2007.01.020;
RA Blake-Palmer K.G., Su Y., Smith A.N., Karet F.E.;
RT "Molecular cloning and characterization of a novel form of the human
RT vacuolar H+-ATPase e-subunit: an essential proton pump component.";
RL Gene 393:94-100(2007).
RN [8] {ECO:0007744|PDB:6WLW, ECO:0007744|PDB:6WM2, ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, AND GLYCOSYLATION AT ASN-70.
RX PubMed=33065002; DOI=10.1016/j.molcel.2020.09.029;
RA Wang L., Wu D., Robinson C.V., Wu H., Fu T.M.;
RT "Structures of a Complete Human V-ATPase Reveal Mechanisms of Its
RT Assembly.";
RL Mol. Cell 80:501-511.e3(2020).
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 (PubMed:33065002). 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:Q2KIB5, ECO:0000269|PubMed:33065002}.
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 (PubMed:33065002). The V1 complex consists of three
CC catalytic AB heterodimers that form a heterohexamer, three peripheral
CC stalks each consisting of EG heterodimers, one central rotor including
CC subunits D and F, and the regulatory subunits C and H
CC (PubMed:33065002). The proton translocation complex V0 consists of the
CC proton transport subunit a, a ring of proteolipid subunits c9c'',
CC rotary subunit d, subunits e and f, and the accessory subunits
CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002).
CC {ECO:0000269|PubMed:33065002}.
CC -!- INTERACTION:
CC O15342; P05090: APOD; NbExp=3; IntAct=EBI-12935759, EBI-715495;
CC O15342; O14735: CDIPT; NbExp=3; IntAct=EBI-12935759, EBI-358858;
CC O15342; Q4VAQ0: COL8A2; NbExp=3; IntAct=EBI-12935759, EBI-10241815;
CC O15342; P54849: EMP1; NbExp=3; IntAct=EBI-12935759, EBI-4319440;
CC O15342; O00155: GPR25; NbExp=3; IntAct=EBI-12935759, EBI-10178951;
CC O15342; P43628: KIR2DL3; NbExp=3; IntAct=EBI-12935759, EBI-8632435;
CC O15342; Q969L2: MAL2; NbExp=3; IntAct=EBI-12935759, EBI-944295;
CC O15342; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-12935759, EBI-12070086;
CC O15342; Q96JQ5: MS4A4A; NbExp=3; IntAct=EBI-12935759, EBI-12820341;
CC O15342; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-12935759, EBI-2863634;
CC O15342; P35372-10: OPRM1; NbExp=3; IntAct=EBI-12935759, EBI-12807478;
CC O15342; P26678: PLN; NbExp=3; IntAct=EBI-12935759, EBI-692836;
CC O15342; Q9BQS2-2: SYT15; NbExp=3; IntAct=EBI-12935759, EBI-13373352;
CC O15342; A2RU14: TMEM218; NbExp=3; IntAct=EBI-12935759, EBI-10173151;
CC O15342; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-12935759, EBI-11956809;
CC O15342; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-12935759, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17350184}.
CC -!- SIMILARITY: Belongs to the V-ATPase e1/e2 subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA75571.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y15286; CAA75571.1; ALT_INIT; mRNA.
DR EMBL; CR456856; CAG33137.1; -; mRNA.
DR EMBL; CR542131; CAG46928.1; -; mRNA.
DR EMBL; AK312068; BAG35004.1; -; mRNA.
DR EMBL; CH471062; EAW61417.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61418.1; -; Genomic_DNA.
DR EMBL; BC119714; AAI19715.1; -; mRNA.
DR EMBL; BC119715; AAI19716.1; -; mRNA.
DR CCDS; CCDS4383.1; -.
DR RefSeq; NP_003936.1; NM_003945.3.
DR PDB; 6WLW; EM; 3.00 A; S=1-81.
DR PDB; 6WM2; EM; 3.10 A; S=1-81.
DR PDB; 6WM3; EM; 3.40 A; S=1-81.
DR PDB; 6WM4; EM; 3.60 A; S=1-81.
DR PDBsum; 6WLW; -.
DR PDBsum; 6WM2; -.
DR PDBsum; 6WM3; -.
DR PDBsum; 6WM4; -.
DR AlphaFoldDB; O15342; -.
DR SMR; O15342; -.
DR BioGRID; 114473; 33.
DR IntAct; O15342; 26.
DR STRING; 9606.ENSP00000429690; -.
DR DrugBank; DB01133; Tiludronic acid.
DR GlyConnect; 1899; 1 N-Linked glycan (1 site).
DR GlyGen; O15342; 1 site, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; O15342; -.
DR BioMuta; ATP6V0E1; -.
DR MassIVE; O15342; -.
DR PaxDb; O15342; -.
DR PeptideAtlas; O15342; -.
DR PRIDE; O15342; -.
DR TopDownProteomics; O15342; -.
DR Antibodypedia; 73907; 11 antibodies from 4 providers.
DR DNASU; 8992; -.
DR Ensembl; ENST00000517669.1; ENSP00000427941.1; ENSG00000113732.9.
DR Ensembl; ENST00000519374.6; ENSP00000429690.1; ENSG00000113732.9.
DR GeneID; 8992; -.
DR KEGG; hsa:8992; -.
DR MANE-Select; ENST00000519374.6; ENSP00000429690.1; NM_003945.4; NP_003936.1.
DR UCSC; uc003mcd.2; human.
DR CTD; 8992; -.
DR DisGeNET; 8992; -.
DR GeneCards; ATP6V0E1; -.
DR HGNC; HGNC:863; ATP6V0E1.
DR HPA; ENSG00000113732; Low tissue specificity.
DR MIM; 603931; gene.
DR neXtProt; NX_O15342; -.
DR OpenTargets; ENSG00000113732; -.
DR PharmGKB; PA25151; -.
DR VEuPathDB; HostDB:ENSG00000113732; -.
DR eggNOG; KOG3500; Eukaryota.
DR GeneTree; ENSGT00940000156866; -.
DR HOGENOM; CLU_170555_0_1_1; -.
DR InParanoid; O15342; -.
DR OMA; VCWLFWL; -.
DR OrthoDB; 1613627at2759; -.
DR PhylomeDB; O15342; -.
DR TreeFam; TF300290; -.
DR BioCyc; MetaCyc:HS03712-MON; -.
DR PathwayCommons; O15342; -.
DR Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-HSA-77387; Insulin receptor recycling.
DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR Reactome; R-HSA-983712; Ion channel transport.
DR SignaLink; O15342; -.
DR SIGNOR; O15342; -.
DR BioGRID-ORCS; 8992; 83 hits in 1078 CRISPR screens.
DR ChiTaRS; ATP6V0E1; human.
DR GeneWiki; ATP6V0E1; -.
DR GenomeRNAi; 8992; -.
DR Pharos; O15342; Tbio.
DR PRO; PR:O15342; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O15342; protein.
DR Bgee; ENSG00000113732; Expressed in epithelium of nasopharynx and 205 other tissues.
DR ExpressionAtlas; O15342; baseline and differential.
DR Genevisible; O15342; HS.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0042625; F:ATPase-coupled ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IGI:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IGI:UniProtKB.
DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0007035; P:vacuolar acidification; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..81
FT /note="V-type proton ATPase subunit e 1"
FT /id="PRO_0000071740"
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:0000269|PubMed:33065002,
FT ECO:0000312|PDB:6WLW, ECO:0000312|PDB:6WM2,
FT ECO:0000312|PDB:6WM3, ECO:0000312|PDB:6WM4"
FT HELIX 7..22
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 34..57
FT /evidence="ECO:0007829|PDB:6WLW"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:6WLW"
SQ SEQUENCE 81 AA; 9374 MW; 9A47F16FDD2B2027 CRC64;
MAYHGLTVPL IVMSVFWGFV GFLVPWFIPK GPNRGVIITM LVTCSVCCYL FWLIAILAQL
NPLFGPQLKN ETIWYLKYHW P
