ID   VATE2_HUMAN             Reviewed;         226 AA.
AC   Q96A05;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=V-type proton ATPase subunit E 2;
DE            Short=V-ATPase subunit E 2;
DE   AltName: Full=Vacuolar proton pump subunit E 2;
GN   Name=ATP6V1E2; Synonyms=ATP6E1, ATP6EL2, ATP6V1EL2;
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], AND 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Cervix;
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 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. V-ATPase is responsible for acidifying and maintaining the pH
CC       of intracellular compartments and in some cell types, is targeted to
CC       the plasma membrane, where it is responsible for acidifying the
CC       extracellular environment. {ECO:0000250|UniProtKB:P36543}.
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. The V1 complex consists of three catalytic AB heterodimers
CC       that form a heterohexamer, three peripheral stalks each consisting of
CC       EG heterodimers, one central rotor including subunits D and F, and the
CC       regulatory subunits C and H. The proton translocation complex V0
CC       consists of the proton transport subunit a, a ring of proteolipid
CC       subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC       subunits ATP6AP1/Ac45 and ATP6AP2/PRR. {ECO:0000250|UniProtKB:P36543}.
CC   -!- INTERACTION:
CC       Q96A05; O75348: ATP6V1G1; NbExp=12; IntAct=EBI-8650380, EBI-711802;
CC       Q96A05; O95670: ATP6V1G2; NbExp=6; IntAct=EBI-8650380, EBI-348290;
CC       Q96A05; Q9BUW7: BBLN; NbExp=3; IntAct=EBI-8650380, EBI-752084;
CC       Q96A05; Q14696: MESD; NbExp=3; IntAct=EBI-8650380, EBI-6165891;
CC       Q96A05; A6NK89: RASSF10; NbExp=3; IntAct=EBI-8650380, EBI-6912267;
CC   -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12036578}.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR   EMBL; AB074759; BAC00847.1; -; mRNA.
DR   EMBL; AK058055; BAB71643.1; -; mRNA.
DR   EMBL; AC018682; AAY14833.1; -; Genomic_DNA.
DR   EMBL; BC008981; AAH08981.1; -; mRNA.
DR   EMBL; BC034808; AAH34808.1; -; mRNA.
DR   CCDS; CCDS1826.1; -.
DR   RefSeq; NP_001304992.1; NM_001318063.1.
DR   RefSeq; XP_005264690.1; XM_005264633.2.
DR   RefSeq; XP_005264691.1; XM_005264634.2.
DR   RefSeq; XP_011531450.1; XM_011533148.2.
DR   RefSeq; XP_011531451.1; XM_011533149.2.
DR   RefSeq; XP_011531452.1; XM_011533150.2.
DR   RefSeq; XP_011531453.1; XM_011533151.2.
DR   RefSeq; XP_011531454.1; XM_011533152.2.
DR   RefSeq; XP_011531455.1; XM_011533153.2.
DR   RefSeq; XP_016860714.1; XM_017005225.1.
DR   RefSeq; XP_016860715.1; XM_017005226.1.
DR   AlphaFoldDB; Q96A05; -.
DR   SMR; Q96A05; -.
DR   BioGRID; 124715; 25.
DR   IntAct; Q96A05; 8.
DR   MINT; Q96A05; -.
DR   STRING; 9606.ENSP00000304891; -.
DR   DrugBank; DB01133; Tiludronic acid.
DR   iPTMnet; Q96A05; -.
DR   PhosphoSitePlus; Q96A05; -.
DR   BioMuta; ATP6V1E2; -.
DR   DMDM; 74731076; -.
DR   EPD; Q96A05; -.
DR   jPOST; Q96A05; -.
DR   MassIVE; Q96A05; -.
DR   MaxQB; Q96A05; -.
DR   PaxDb; Q96A05; -.
DR   PeptideAtlas; Q96A05; -.
DR   PRIDE; Q96A05; -.
DR   ProteomicsDB; 75888; -.
DR   Antibodypedia; 51230; 105 antibodies from 21 providers.
DR   DNASU; 90423; -.
DR   Ensembl; ENST00000306448.4; ENSP00000304891.4; ENSG00000250565.7.
DR   Ensembl; ENST00000522587.6; ENSP00000428141.1; ENSG00000250565.7.
DR   GeneID; 90423; -.
DR   KEGG; hsa:90423; -.
DR   MANE-Select; ENST00000522587.6; ENSP00000428141.1; NM_001318063.2; NP_001304992.1.
DR   UCSC; uc002ruy.3; human.
DR   CTD; 90423; -.
DR   DisGeNET; 90423; -.
DR   GeneCards; ATP6V1E2; -.
DR   HGNC; HGNC:18125; ATP6V1E2.
DR   HPA; ENSG00000250565; Tissue enriched (testis).
DR   MIM; 617385; gene.
DR   neXtProt; NX_Q96A05; -.
DR   OpenTargets; ENSG00000250565; -.
DR   PharmGKB; PA25159; -.
DR   VEuPathDB; HostDB:ENSG00000250565; -.
DR   eggNOG; KOG1664; Eukaryota.
DR   GeneTree; ENSGT00390000002730; -.
DR   HOGENOM; CLU_073641_2_0_1; -.
DR   InParanoid; Q96A05; -.
DR   OMA; MSTVRNQ; -.
DR   OrthoDB; 1489718at2759; -.
DR   PhylomeDB; Q96A05; -.
DR   TreeFam; TF313479; -.
DR   BioCyc; MetaCyc:HS10256-MON; -.
DR   PathwayCommons; Q96A05; -.
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; Q96A05; -.
DR   BioGRID-ORCS; 90423; 12 hits in 1076 CRISPR screens.
DR   ChiTaRS; ATP6V1E2; human.
DR   GeneWiki; ATP6V1E2; -.
DR   GenomeRNAi; 90423; -.
DR   Pharos; Q96A05; Tbio.
DR   PRO; PR:Q96A05; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q96A05; protein.
DR   Bgee; ENSG00000250565; Expressed in sperm and 138 other tissues.
DR   ExpressionAtlas; Q96A05; baseline and differential.
DR   Genevisible; Q96A05; HS.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
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   Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT   CHAIN           1..226
FT                   /note="V-type proton ATPase subunit E 2"
FT                   /id="PRO_0000282344"
SQ   SEQUENCE   226 AA;  26074 MW;  40546707D944ED20 CRC64;
     MALSDVDVKK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMEYYEKK
     EKQIEQQKKI LMSTMRNQAR LKVLRARNDL ISDLLSEAKL RLSRIVEDPE VYQGLLDKLV
     LQGLLRLLEP VMIVRCRPQD LLLVEAAVQK AIPEYMTISQ KHVEVQIDKE AYLAVNAAGG
     VEVYSGNQRI KVSNTLESRL DLSAKQKMPE IRMALFGANT NRKFFI