VATE1_MOUSE
ID VATE1_MOUSE Reviewed; 226 AA.
AC P50518; Q3UK59; Q8K5D6; Q99LD0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
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 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 [GENOMIC DNA].
RX PubMed=8741845; DOI=10.1091/mbc.7.1.129;
RA Laitala T., Howell M.L., Dean G.E., Vaananen H.K.;
RT "Resorption-cycle-dependent polarization of mRNAs for different subunits of
RT V-ATPase in bone-resorbing osteoclasts.";
RL Mol. Biol. Cell 7:129-142(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=Placenta, and Retina;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [5]
RP PROTEIN SEQUENCE OF 14-26; 35-43; 54-60; 71-82; 86-101; 112-131; 140-147;
RP 200-214 AND 215-224, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [8]
RP INTERACTION WITH RABL2, AND TISSUE SPECIFICITY.
RX PubMed=23055941; DOI=10.1371/journal.pgen.1002969;
RA Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J., Whisstock J.C.,
RA Field M.C., Adams V., Ishikawa T., Aitken R.J., Whittle B., Goodnow C.C.,
RA Ormandy C.J., O'Bryan M.K.;
RT "RAB-like 2 has an essential role in male fertility, sperm intra-flagellar
RT transport, and tail assembly.";
RL PLoS Genet. 8:E1002969-E1002969(2012).
RN [9]
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).
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 (By similarity). 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: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 (By similarity). The V1 complex consists of three catalytic
CC AB heterodimers that form a heterohexamer, three peripheral stalks each
CC consisting of EG heterodimers, one central rotor including subunits D
CC and F, and the regulatory subunits C and H (By similarity). The proton
CC translocation complex V0 consists of the proton transport subunit a, a
CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-
CC bound RABL2 (PubMed:23055941). Interacts with ALDOC (By similarity).
CC Interacts with RAB11B (By similarity). {ECO:0000250|UniProtKB:P36543,
CC ECO:0000269|PubMed:23055941}.
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 -!- TISSUE SPECIFICITY: Expressed within the midpiece of sperm tail (at
CC protein level) (PubMed:11872743, PubMed:23055941). Kidney; localizes to
CC early distal nephron, encompassing thick ascending limbs and distal
CC convoluted tubules (at protein level) (PubMed:29993276).
CC {ECO:0000269|PubMed:11872743, ECO:0000269|PubMed:23055941,
CC ECO:0000269|PubMed:29993276}.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR EMBL; U13841; AAC52412.1; -; Genomic_DNA.
DR EMBL; AB074758; BAB92084.1; -; mRNA.
DR EMBL; AK146162; BAE26943.1; -; mRNA.
DR EMBL; AK149356; BAE28832.1; -; mRNA.
DR EMBL; AK167644; BAE39695.1; -; mRNA.
DR EMBL; AK169854; BAE41412.1; -; mRNA.
DR EMBL; BC003421; AAH03421.1; -; mRNA.
DR EMBL; BC055438; AAH55438.1; -; mRNA.
DR CCDS; CCDS20484.1; -.
DR RefSeq; NP_031536.2; NM_007510.2.
DR AlphaFoldDB; P50518; -.
DR SMR; P50518; -.
DR BioGRID; 198265; 14.
DR IntAct; P50518; 4.
DR MINT; P50518; -.
DR STRING; 10090.ENSMUSP00000019354; -.
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; P50518; -.
DR PhosphoSitePlus; P50518; -.
DR SwissPalm; P50518; -.
DR EPD; P50518; -.
DR jPOST; P50518; -.
DR MaxQB; P50518; -.
DR PaxDb; P50518; -.
DR PeptideAtlas; P50518; -.
DR PRIDE; P50518; -.
DR ProteomicsDB; 297959; -.
DR Antibodypedia; 4024; 191 antibodies from 24 providers.
DR DNASU; 11973; -.
DR Ensembl; ENSMUST00000019354; ENSMUSP00000019354; ENSMUSG00000019210.
DR GeneID; 11973; -.
DR KEGG; mmu:11973; -.
DR UCSC; uc009dnr.1; mouse.
DR CTD; 529; -.
DR MGI; MGI:894326; Atp6v1e1.
DR VEuPathDB; HostDB:ENSMUSG00000019210; -.
DR eggNOG; KOG1664; Eukaryota.
DR GeneTree; ENSGT00390000002730; -.
DR HOGENOM; CLU_073641_2_0_1; -.
DR InParanoid; P50518; -.
DR OMA; AIDTQYE; -.
DR OrthoDB; 1489718at2759; -.
DR PhylomeDB; P50518; -.
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; 11973; 24 hits in 71 CRISPR screens.
DR ChiTaRS; Atp6v1e1; mouse.
DR PRO; PR:P50518; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P50518; protein.
DR Bgee; ENSMUSG00000019210; Expressed in facial nucleus and 296 other tissues.
DR ExpressionAtlas; P50518; baseline and differential.
DR Genevisible; P50518; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
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; 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 Acetylation; Cell membrane; Cytoplasmic vesicle; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P36543"
FT CHAIN 2..226
FT /note="V-type proton ATPase subunit E 1"
FT /id="PRO_0000117296"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P36543"
FT MOD_RES 56
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT CONFLICT 2..5
FT /note="ALSD -> GLRH (in Ref. 1; AAC52412)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="E -> EE (in Ref. 1; AAC52412)"
FT /evidence="ECO:0000305"
FT CONFLICT 46..47
FT /note="VQ -> LE (in Ref. 1; AAC52412)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="E -> R (in Ref. 1; AAC52412)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="Q -> QQ (in Ref. 1; AAC52412)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="A -> T (in Ref. 2; BAB92084)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="S -> M (in Ref. 1; AAC52412)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="P -> T (in Ref. 3; BAE26943)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="K -> R (in Ref. 1; AAC52412)"
FT /evidence="ECO:0000305"
FT CONFLICT 171..176
FT /note="AYLPEE -> PTCLRN (in Ref. 1; AAC52412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 26157 MW; 5DD7B0EAB181EA08 CRC64;
MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMEYYEKK
EKQIEQQKKI QMSNLMNQAR LKVLRARDDL ITDLLNEAKQ RLSKVVKDTT RYQVLLDGLV
LQGLYQLLEP RMIVRCRKQD FPLVKAAVQK AIPMYKIATK KDVDVQIDQE AYLPEEIAGG
VEIYNGDRKI KVSNTLESRL DLIAQQMMPE VRGALFGANA NRKFLD
