ID   VATE2_MOUSE             Reviewed;         226 AA.
AC   Q9D593; Q6P8U8; Q810S5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 150.
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;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11872743; DOI=10.1074/jbc.m111567200;
RA   Sun-Wada G.H., Imai-Senga Y., Yamamoto A., Murata Y., Hirata T., Wada Y.,
RA   Futai M.;
RT   "A proton pump ATPase with testis-specific E1-subunit isoform required for
RT   acrosome acidification.";
RL   J. Biol. Chem. 277:18098-18105(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11872743}.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR   EMBL; AB074757; BAB92083.1; -; mRNA.
DR   EMBL; AK015654; BAB29919.1; -; mRNA.
DR   EMBL; BC049547; AAH49547.2; -; mRNA.
DR   EMBL; BC061059; AAH61059.1; -; mRNA.
DR   CCDS; CCDS29009.1; -.
DR   RefSeq; NP_083397.3; NM_029121.3.
DR   AlphaFoldDB; Q9D593; -.
DR   SMR; Q9D593; -.
DR   BioGRID; 217076; 2.
DR   IntAct; Q9D593; 1.
DR   MINT; Q9D593; -.
DR   STRING; 10090.ENSMUSP00000157221; -.
DR   TCDB; 3.A.2.2.6; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; Q9D593; -.
DR   PhosphoSitePlus; Q9D593; -.
DR   jPOST; Q9D593; -.
DR   MaxQB; Q9D593; -.
DR   PaxDb; 10090-ENSMUSP00000065285; -.
DR   PeptideAtlas; Q9D593; -.
DR   ProteomicsDB; 297975; -.
DR   Antibodypedia; 51230; 120 antibodies from 21 providers.
DR   DNASU; 74915; -.
DR   Ensembl; ENSMUST00000065758.8; ENSMUSP00000065285.8; ENSMUSG00000053375.9.
DR   Ensembl; ENSMUST00000233995.2; ENSMUSP00000157221.2; ENSMUSG00000053375.9.
DR   Ensembl; ENSMUST00000235110.2; ENSMUSP00000157068.2; ENSMUSG00000053375.9.
DR   GeneID; 74915; -.
DR   KEGG; mmu:74915; -.
DR   UCSC; uc008dul.1; mouse.
DR   AGR; MGI:1922165; -.
DR   CTD; 90423; -.
DR   MGI; MGI:1922165; Atp6v1e2.
DR   VEuPathDB; HostDB:ENSMUSG00000053375; -.
DR   eggNOG; KOG1664; Eukaryota.
DR   GeneTree; ENSGT00390000002730; -.
DR   HOGENOM; CLU_073641_2_0_1; -.
DR   InParanoid; Q9D593; -.
DR   OMA; MSTVRNQ; -.
DR   OrthoDB; 5397689at2759; -.
DR   PhylomeDB; Q9D593; -.
DR   TreeFam; TF313479; -.
DR   Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-MMU-77387; Insulin receptor recycling.
DR   Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-MMU-983712; Ion channel transport.
DR   BioGRID-ORCS; 74915; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Atp6v1e2; mouse.
DR   PRO; PR:Q9D593; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9D593; Protein.
DR   Bgee; ENSMUSG00000053375; Expressed in seminiferous tubule of testis and 22 other cell types or tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
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; IGI:MGI.
DR   GO; GO:1902600; P:proton transmembrane transport; IGI:MGI.
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   PANTHER; PTHR45715:SF7; V-TYPE PROTON ATPASE SUBUNIT E 2; 1.
DR   Pfam; PF01991; vATP-synt_E; 1.
DR   SUPFAM; SSF160527; V-type ATPase subunit E-like; 1.
DR   Genevisible; Q9D593; MM.
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_0000282345"
FT   CONFLICT        55
FT                   /note="D -> G (in Ref. 3; AAH61059)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   226 AA;  26307 MW;  AE5F501F02B8F98F CRC64;
     MALTDIDVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMDYFEKK
     EKQIEQQKKI QLSTMRNQAR ITVLRARDNL ILELLKDAKM RLSRIVSDEE IYQDLLDKLV
     LQALLRLLEP VMIVRCRPQD LHLVESAVLR AIPQYMRLCQ KHLEVQVDQT EHLPSNAAGG
     VEVYSSDQKI KVSNTLESRL NLAAMQKMPE IRGILFGDNT SRKFFT
//