VATE1_HUMAN
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 03-AUG-2022, entry version 205.
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:33065002, PubMed:32001091). 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 -!- 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}.
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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_001696.3. [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 PDBsum; 6WLZ; -.
DR PDBsum; 6WM2; -.
DR PDBsum; 6WM3; -.
DR PDBsum; 6WM4; -.
DR AlphaFoldDB; P36543; -.
DR SMR; P36543; -.
DR BioGRID; 107012; 91.
DR IntAct; P36543; 21.
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 iPTMnet; P36543; -.
DR MetOSite; P36543; -.
DR PhosphoSitePlus; P36543; -.
DR SwissPalm; P36543; -.
DR BioMuta; ATP6V1E1; -.
DR DMDM; 549207; -.
DR UCD-2DPAGE; P36543; -.
DR EPD; P36543; -.
DR jPOST; P36543; -.
DR MassIVE; P36543; -.
DR MaxQB; P36543; -.
DR PaxDb; P36543; -.
DR PeptideAtlas; P36543; -.
DR PRIDE; P36543; -.
DR ProteomicsDB; 2120; -.
DR ProteomicsDB; 55209; -. [P36543-1]
DR ProteomicsDB; 55210; -. [P36543-2]
DR Antibodypedia; 4024; 191 antibodies from 24 providers.
DR DNASU; 529; -.
DR Ensembl; ENST00000253413.10; ENSP00000253413.5; ENSG00000131100.13. [P36543-1]
DR Ensembl; ENST00000399796.6; ENSP00000382694.2; ENSG00000131100.13. [P36543-3]
DR Ensembl; ENST00000399798.6; ENSP00000382696.2; ENSG00000131100.13. [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 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 neXtProt; NX_P36543; -.
DR OpenTargets; ENSG00000131100; -.
DR Orphanet; 357074; Autosomal recessive cutis laxa type 2, classic type.
DR PharmGKB; PA25158; -.
DR VEuPathDB; HostDB:ENSG00000131100; -.
DR eggNOG; KOG1664; Eukaryota.
DR GeneTree; ENSGT00390000002730; -.
DR HOGENOM; CLU_073641_2_0_1; -.
DR InParanoid; P36543; -.
DR OMA; MYNENGK; -.
DR PhylomeDB; P36543; -.
DR TreeFam; TF313479; -.
DR BioCyc; MetaCyc:HS05489-MON; -.
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 SignaLink; P36543; -.
DR BioGRID-ORCS; 529; 729 hits in 1076 CRISPR screens.
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 214 other tissues.
DR ExpressionAtlas; P36543; baseline and differential.
DR Genevisible; P36543; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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 Gene3D; 3.30.2320.30; -; 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; PTHR45715; 1.
DR Pfam; PF01991; vATP-synt_E; 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 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
