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 28-JAN-2026, entry version 191. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_003945.4. 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 PDB; 7U4T; EM; 3.60 A; S=1-81. DR PDB; 7UNF; EM; 4.08 A; m=1-81. DR PDB; 9CF8; EM; 3.46 A; S=1-81. DR PDB; 9CFC; EM; 3.47 A; S=1-81. DR PDB; 9DET; EM; 3.00 A; e=1-81. DR PDBsum; 6WLW; -. DR PDBsum; 6WM2; -. DR PDBsum; 6WM3; -. DR PDBsum; 6WM4; -. DR PDBsum; 7U4T; -. DR PDBsum; 7UNF; -. DR PDBsum; 9CF8; -. DR PDBsum; 9CFC; -. DR PDBsum; 9DET; -. DR AlphaFoldDB; O15342; -. DR EMDB; EMD-21844; -. DR EMDB; EMD-21847; -. DR EMDB; EMD-21848; -. DR EMDB; EMD-21849; -. DR EMDB; EMD-26334; -. DR EMDB; EMD-26623; -. DR EMDB; EMD-45533; -. DR EMDB; EMD-45536; -. DR SMR; O15342; -. DR BioGRID; 114473; 34. DR ComplexPortal; CPX-2470; Vacuolar proton translocating ATPase complex, ATP6V0A1 variant. DR ComplexPortal; CPX-6904; Vacuolar proton translocating ATPase complex, ATP6V0A2 variant. DR ComplexPortal; CPX-6905; Vacuolar proton translocating ATPase complex, ATP6V0A3 variant. DR ComplexPortal; CPX-6912; Vacuolar proton translocating ATPase complex, ATP6V0A4 variant. DR FunCoup; O15342; 667. DR IntAct; O15342; 28. DR STRING; 9606.ENSP00000429690; -. DR DrugBank; DB01133; Tiludronic acid. DR GlyConnect; 1899; 1 N-Linked glycan (1 site). DR GlyCosmos; O15342; 1 site, 1 glycan. DR GlyGen; O15342; 2 sites, 7 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; O15342; -. DR PhosphoSitePlus; O15342; -. DR BioMuta; ATP6V0E1; -. DR PaxDb; 9606-ENSP00000429690; -. DR PeptideAtlas; O15342; -. DR TopDownProteomics; O15342; -. DR Antibodypedia; 73907; 11 antibodies from 4 providers. DR DNASU; 8992; -. DR Ensembl; ENST00000517669.1; ENSP00000427941.1; ENSG00000113732.10. DR Ensembl; ENST00000519374.6; ENSP00000429690.1; ENSG00000113732.10. 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 AGR; HGNC:863; -. DR ClinPGx; PA25151; -. 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 OpenTargets; ENSG00000113732; -. DR VEuPathDB; HostDB:ENSG00000113732; -. DR eggNOG; KOG3500; Eukaryota. DR GeneTree; ENSGT00940000156866; -. DR HOGENOM; CLU_170555_0_1_1; -. DR InParanoid; O15342; -. DR OMA; SENITMG; -. DR OrthoDB; 1508846at2759; -. DR PAN-GO; O15342; 1 GO annotation based on evolutionary models. DR PhylomeDB; O15342; -. DR BioCyc; MetaCyc:HS03712-MONOMER; -. 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 Reactome; R-HSA-9857377; Regulation of MITF-M-dependent genes involved in lysosome biogenesis and autophagy. DR SignaLink; O15342; -. DR SIGNOR; O15342; -. DR Agora; ENSG00000113732; -. DR BioGRID-ORCS; 8992; 87 hits in 1156 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 207 other cell types or tissues. DR ExpressionAtlas; O15342; baseline and differential. DR GO; GO:0010008; C:endosome membrane; TAS:Reactome. 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:SF5; V-TYPE PROTON ATPASE SUBUNIT E 1; 1. DR PANTHER; PTHR12263; VACUOLAR ATP SYNTHASE SUBUNIT H; 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; Proteomics identification; Reference proteome; Transmembrane; KW Transmembrane helix; 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 //