ID VATE1_HUMAN Reviewed; 226 AA. AC P36543; A8MUE4; A8MUN4; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 28-JAN-2026, entry version 222. DE RecName: Full=V-type proton ATPase subunit E 1; DE Short=V-ATPase subunit E 1; DE AltName: Full=V-ATPase 31 kDa subunit; DE Short=p31; DE AltName: Full=Vacuolar proton pump subunit E 1; GN Name=ATP6V1E1; Synonyms=ATP6E, ATP6E2; 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] (ISOFORM 1). RX PubMed=1533641; DOI=10.1016/s0021-9258(19)50184-3; RA Hemken P., Guo X.-L., Wang Z.-Q., Zhang K., Gluck S.; RT "Immunologic evidence that vacuolar H+ ATPases with heterogeneous forms of RT Mr = 31,000 subunit have different membrane distributions in mammalian RT kidney."; RL J. Biol. Chem. 267:9948-9957(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8004105; DOI=10.1093/hmg/3.2.335; RA Baud V., Mears A., Lamour V., Scamps C., McDermid A., Lipinski M.; RT "The E subunit of vacuolar H(+)-ATPase localizes close to the centromere on RT human chromosome 22."; RL Hum. Mol. Genet. 3:335-339(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Osteoclastoma; RX PubMed=8250920; DOI=10.1006/bbrc.1993.2434; RA van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.; RT "Cloning and tissue distribution of subunits C, D, and E of the human RT vacuolar H(+)-ATPase."; RL Biochem. Biophys. Res. Commun. 197:15-21(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Brain, and Cerebellum; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [8] RP PROTEIN SEQUENCE OF 112-131, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Vishwanath V.; RL Submitted (MAR-2007) to UniProtKB. RN [9] RP INTERACTION WITH ALDOC. RX PubMed=11399750; DOI=10.1074/jbc.m008768200; RA Lu M., Holliday L.S., Zhang L., Dunn W.A. Jr., Gluck S.L.; RT "Interaction between aldolase and vacuolar H+-ATPase: evidence for direct RT coupling of glycolysis to the ATP-hydrolyzing proton pump."; RL J. Biol. Chem. 276:30407-30413(2001). RN [10] RP TISSUE SPECIFICITY. RX PubMed=12036578; DOI=10.1016/s0378-1119(02)00542-5; RA Imai-Senga Y., Sun-Wada G.H., Wada Y., Futai M.; RT "A human gene, ATP6E1, encoding a testis-specific isoform of H(+)-ATPase RT subunit E."; RL Gene 289:7-12(2002). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP INTERACTION WITH RAB11B. RX PubMed=20717956; DOI=10.1002/jcp.22388; RA Oehlke O., Martin H.W., Osterberg N., Roussa E.; RT "Rab11b and its effector Rip11 regulate the acidosis-induced traffic of V- RT ATPase in salivary ducts."; RL J. Cell. Physiol. 226:638-651(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [16] RP INVOLVEMENT IN ARCL2C, TISSUE SPECIFICITY, AND VARIANTS ARCL2C PRO-128 AND RP TRP-212. RX PubMed=28065471; DOI=10.1016/j.ajhg.2016.12.010; RA Van Damme T., Gardeitchik T., Mohamed M., Guerrero-Castillo S., RA Freisinger P., Guillemyn B., Kariminejad A., Dalloyaux D., van Kraaij S., RA Lefeber D.J., Syx D., Steyaert W., De Rycke R., Hoischen A., Kamsteeg E.J., RA Wong S.Y., van Scherpenzeel M., Jamali P., Brandt U., Nijtmans L., RA Korenke G.C., Chung B.H., Mak C.C., Hausser I., Kornak U., RA Fischer-Zirnsak B., Strom T.M., Meitinger T., Alanay Y., Utine G.E., RA Leung P.K., Ghaderi-Sohi S., Coucke P., Symoens S., De Paepe A., Thiel C., RA Haack T.B., Malfait F., Morava E., Callewaert B., Wevers R.A.; RT "Mutations in ATP6V1E1 or ATP6V1A cause autosomal-recessive cutis laxa."; RL Am. J. Hum. Genet. 100:216-227(2017). RN [17] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=29993276; DOI=10.1152/ajprenal.00539.2017; RA Frische S., Chambrey R., Trepiccione F., Zamani R., Marcussen N., RA Alexander R.T., Skjoedt K., Svenningsen P., Dimke H.; RT "H+-ATPase B1 subunit localizes to thick ascending limb and distal RT convoluted tubule of rodent and human kidney."; RL Am. J. Physiol. 315:F429-F444(2018). RN [18] RP REVIEW. RX PubMed=32001091; DOI=10.1016/j.tibs.2019.12.007; RA Vasanthakumar T., Rubinstein J.L.; RT "Structure and Roles of V-type ATPases."; RL Trends Biochem. Sci. 45:295-307(2020). RN [19] {ECO:0007744|PDB:6WLZ, ECO:0007744|PDB:6WM2, ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4} RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS), FUNCTION, AND RP IDENTIFICATION IN THE V-ATPASE COMPLEX. 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). RN [20] RP VARIANT [LARGE SCALE ANALYSIS] GLY-50. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Subunit of the V1 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:32001091, PubMed:33065002). V-ATPase is responsible for CC acidifying and maintaining the pH of intracellular compartments and in CC some cell types, is targeted to the plasma membrane, where it is CC responsible for acidifying the extracellular environment CC (PubMed:32001091). {ECO:0000269|PubMed:33065002, CC ECO:0000303|PubMed:32001091}. 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). Interacts with CC RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (By similarity). CC Interacts with ALDOC (PubMed:11399750). Interacts with RAB11B CC (PubMed:20717956). {ECO:0000250|UniProtKB:P50518, CC ECO:0000269|PubMed:11399750, ECO:0000269|PubMed:20717956, CC ECO:0000269|PubMed:33065002}. CC -!- INTERACTION: CC P36543; O75348: ATP6V1G1; NbExp=3; IntAct=EBI-348639, EBI-711802; CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000269|PubMed:29993276}; Peripheral membrane protein CC {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle CC membrane {ECO:0000250|UniProtKB:Q6PCU2}; Peripheral membrane protein CC {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane CC {ECO:0000250|UniProtKB:Q6PCU2}; Peripheral membrane protein CC {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P36543-1; Sequence=Displayed; CC Name=2; CC IsoId=P36543-2; Sequence=VSP_042925; CC Name=3; CC IsoId=P36543-3; Sequence=VSP_044589; CC -!- TISSUE SPECIFICITY: Kidney; localizes to early distal nephron, CC encompassing thick ascending limbs and distal convoluted tubules (at CC protein level) (PubMed:29993276). Ubiquitous (PubMed:12036578). High CC expression in the skin (PubMed:28065471). {ECO:0000269|PubMed:12036578, CC ECO:0000269|PubMed:28065471, ECO:0000269|PubMed:29993276}. CC -!- DISEASE: Cutis laxa, autosomal recessive, 2C (ARCL2C) [MIM:617402]: A CC form of cutis laxa, a disorder characterized by an excessive congenital CC skin wrinkling, a large fontanelle with delayed closure, a typical CC facial appearance with downslanting palpebral fissures, and a general CC connective tissue weakness. Most ARCL2C patients exhibit severe CC hypotonia as well as cardiovascular involvement. CC {ECO:0000269|PubMed:28065471}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {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; X76228; CAA53814.1; -; mRNA. DR EMBL; X71491; CAA50592.1; -; mRNA. DR EMBL; CR456385; CAG30271.1; -; mRNA. DR EMBL; AK294623; BAG57804.1; -; mRNA. DR EMBL; AK315941; BAH14312.1; -; mRNA. DR EMBL; AC004019; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006285; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007666; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC004443; AAH04443.1; -; mRNA. DR CCDS; CCDS13745.1; -. [P36543-1] DR CCDS; CCDS42977.1; -. [P36543-2] DR CCDS; CCDS42978.1; -. [P36543-3] DR PIR; S60562; S60562. DR RefSeq; NP_001034455.1; NM_001039366.1. [P36543-2] DR RefSeq; NP_001034456.1; NM_001039367.1. [P36543-3] DR RefSeq; NP_001687.1; NM_001696.4. [P36543-1] DR PDB; 6WLZ; EM; 2.90 A; H/I/J=1-226. DR PDB; 6WM2; EM; 3.10 A; H/I/J=1-226. DR PDB; 6WM3; EM; 3.40 A; H/I/J=1-226. DR PDB; 6WM4; EM; 3.60 A; H/I/J=1-226. DR PDB; 7U4T; EM; 3.60 A; H/I/J=1-226. DR PDB; 7UNF; EM; 4.08 A; b/c/d=1-226. DR PDB; 9CF8; EM; 3.46 A; H/I/J=1-226. DR PDB; 9CFC; EM; 3.47 A; H/I/J=1-226. DR PDBsum; 6WLZ; -. DR PDBsum; 6WM2; -. DR PDBsum; 6WM3; -. DR PDBsum; 6WM4; -. DR PDBsum; 7U4T; -. DR PDBsum; 7UNF; -. DR PDBsum; 9CF8; -. DR PDBsum; 9CFC; -. DR AlphaFoldDB; P36543; -. DR EMDB; EMD-21845; -. 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; P36543; -. DR BioGRID; 107012; 138. 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; P36543; 2062. DR IntAct; P36543; 41. DR MINT; P36543; -. DR STRING; 9606.ENSP00000253413; -. DR DrugBank; DB01133; Tiludronic acid. DR TCDB; 3.A.2.2.4; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily. DR CarbonylDB; P36543; -. DR GlyGen; P36543; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P36543; -. DR MetOSite; P36543; -. DR PhosphoSitePlus; P36543; -. DR SwissPalm; P36543; -. DR BioMuta; ATP6V1E1; -. DR DMDM; 549207; -. DR jPOST; P36543; -. DR MassIVE; P36543; -. DR PaxDb; 9606-ENSP00000253413; -. DR PeptideAtlas; P36543; -. DR ProteomicsDB; 2120; -. DR ProteomicsDB; 55209; -. [P36543-1] DR ProteomicsDB; 55210; -. [P36543-2] DR Pumba; P36543; -. DR Antibodypedia; 4024; 192 antibodies from 25 providers. DR DNASU; 529; -. DR Ensembl; ENST00000253413.10; ENSP00000253413.5; ENSG00000131100.14. [P36543-1] DR Ensembl; ENST00000399796.6; ENSP00000382694.2; ENSG00000131100.14. [P36543-3] DR Ensembl; ENST00000399798.6; ENSP00000382696.2; ENSG00000131100.14. [P36543-2] DR GeneID; 529; -. DR KEGG; hsa:529; -. DR MANE-Select; ENST00000253413.10; ENSP00000253413.5; NM_001696.4; NP_001687.1. DR UCSC; uc002zms.3; human. [P36543-1] DR AGR; HGNC:857; -. DR ClinPGx; PA25158; -. DR CTD; 529; -. DR DisGeNET; 529; -. DR GeneCards; ATP6V1E1; -. DR HGNC; HGNC:857; ATP6V1E1. DR HPA; ENSG00000131100; Low tissue specificity. DR MalaCards; ATP6V1E1; -. DR MIM; 108746; gene. DR MIM; 617402; phenotype. DR OpenTargets; ENSG00000131100; -. DR Orphanet; 357074; Autosomal recessive cutis laxa type 2, classic type. DR VEuPathDB; HostDB:ENSG00000131100; -. DR eggNOG; KOG1664; Eukaryota. DR GeneTree; ENSGT00390000002730; -. DR HOGENOM; CLU_073641_2_0_1; -. DR InParanoid; P36543; -. DR OMA; YISRDHQ; -. DR OrthoDB; 10263003at2759; -. DR PAN-GO; P36543; 1 GO annotation based on evolutionary models. DR PhylomeDB; P36543; -. DR BioCyc; MetaCyc:HS05489-MONOMER; -. DR PathwayCommons; P36543; -. 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; P36543; -. DR Agora; ENSG00000131100; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 529; 754 hits in 1159 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; ATP6V1E1; human. DR GeneWiki; ATP6V1E1; -. DR GenomeRNAi; 529; -. DR Pharos; P36543; Tbio. DR PRO; PR:P36543; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; P36543; protein. DR Bgee; ENSG00000131100; Expressed in middle temporal gyrus and 216 other cell types or tissues. DR ExpressionAtlas; P36543; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005768; C:endosome; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0005902; C:microvillus; IEA:Ensembl. DR GO; GO:0016469; C:proton-transporting two-sector ATPase complex; TAS:ProtInc. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IDA:UniProtKB. DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central. DR GO; GO:1902600; P:proton transmembrane transport; TAS:ProtInc. DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL. DR GO; GO:0097401; P:synaptic vesicle lumen acidification; IEA:Ensembl. DR FunFam; 3.30.2320.30:FF:000001; V-type proton atpase subunit e 1; 1. DR Gene3D; 6.10.250.1620; -; 1. DR Gene3D; 3.30.2320.30; ATP synthase, E subunit, C-terminal; 1. DR HAMAP; MF_00311; ATP_synth_E_arch; 1. DR InterPro; IPR038495; ATPase_E_C. DR InterPro; IPR002842; ATPase_V1_Esu. DR PANTHER; PTHR45715; ATPASE H+-TRANSPORTING V1 SUBUNIT E1A-RELATED; 1. DR Pfam; PF01991; vATP-synt_E; 1. DR SUPFAM; SSF160527; V-type ATPase subunit E-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; KW Cytoplasmic vesicle; Direct protein sequencing; Disease variant; KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein; KW Proteomics identification; Reference proteome; Synapse; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:25944712" FT CHAIN 2..226 FT /note="V-type proton ATPase subunit E 1" FT /id="PRO_0000117295" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:25944712" FT MOD_RES 56 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P50518" FT VAR_SEQ 12..33 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042925" FT VAR_SEQ 93..122 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044589" FT VARIANT 50 FT /note="R -> G (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036565" FT VARIANT 128 FT /note="L -> P (in ARCL2C; dbSNP:rs1060505031)" FT /evidence="ECO:0000269|PubMed:28065471" FT /id="VAR_078604" FT VARIANT 212 FT /note="R -> W (in ARCL2C; dbSNP:rs1028534806)" FT /evidence="ECO:0000269|PubMed:28065471" FT /id="VAR_078605" FT CONFLICT 32 FT /note="A -> R (in Ref. 3; CAA50592)" FT /evidence="ECO:0000305" FT CONFLICT 86 FT /note="A -> G (in Ref. 1; no nucleotide entry)" FT /evidence="ECO:0000305" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:6WM2" FT HELIX 35..107 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 109..127 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 130..135 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 141..159 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 164..167 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:6WM2" FT STRAND 179..184 FT /evidence="ECO:0007829|PDB:6WLZ" FT STRAND 188..195 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 196..206 FT /evidence="ECO:0007829|PDB:6WLZ" FT HELIX 208..216 FT /evidence="ECO:0007829|PDB:6WLZ" SQ SEQUENCE 226 AA; 26145 MW; DFD0D44E6D9AEA17 CRC64; MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMEYYEKK EKQIEQQKKI QMSNLMNQAR LKVLRARDDL ITDLLNEAKQ RLSKVVKDTT RYQVLLDGLV LQGLYQLLEP RMIVRCRKQD FPLVKAAVQK AIPMYKIATK NDVDVQIDQE SYLPEDIAGG VEIYNGDRKI KVSNTLESRL DLIAQQMMPE VRGALFGANA NRKFLD //