ID   VATE2_BOVIN             Reviewed;         226 AA.
AC   Q32LB7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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:P11019}.
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:P11019}.
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; BC109658; AAI09659.1; -; mRNA.
DR   RefSeq; NP_001073081.1; NM_001079613.2.
DR   RefSeq; XP_010808270.1; XM_010809968.2.
DR   RefSeq; XP_010808271.1; XM_010809969.2.
DR   AlphaFoldDB; Q32LB7; -.
DR   SMR; Q32LB7; -.
DR   STRING; 9913.ENSBTAP00000018250; -.
DR   PaxDb; Q32LB7; -.
DR   PRIDE; Q32LB7; -.
DR   Ensembl; ENSBTAT00000018250; ENSBTAP00000018250; ENSBTAG00000013734.
DR   GeneID; 540113; -.
DR   KEGG; bta:540113; -.
DR   CTD; 90423; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013734; -.
DR   VGNC; VGNC:26323; ATP6V1E2.
DR   eggNOG; KOG1664; Eukaryota.
DR   GeneTree; ENSGT00390000002730; -.
DR   HOGENOM; CLU_073641_2_0_1; -.
DR   InParanoid; Q32LB7; -.
DR   OMA; MSTVRNQ; -.
DR   OrthoDB; 1489718at2759; -.
DR   TreeFam; TF313479; -.
DR   Reactome; R-BTA-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-BTA-9639288; Amino acids regulate mTORC1.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000013734; Expressed in semen and 89 other tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
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   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   2: Evidence at transcript 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_0000282343"
SQ   SEQUENCE   226 AA;  26171 MW;  AAB5F4E050BB192E CRC64;
     MALSDVDVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMEYYEKK
     EKQIEQQKKI QMSTLRNQAR LKVLRARNDL ISELLNDAKL RLSRIVTDPE FYQGLLDKLV
     LQGLLRLLEP VVIVRCRPQD HFLVEAAVQR AIPQYTAVSH RCVEVQVDKE VQLATDTTGG
     VEVYSSDQRI MVSNTLESRL DLLSQQKMPE IRKALFGANA NRKFFV