VA0E1_BOVIN
ID VA0E1_BOVIN Reviewed; 81 AA.
AC P81103; O18981; Q3ZBN2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=V-type proton ATPase subunit e 1;
DE Short=V-ATPase subunit e 1;
DE AltName: Full=V-ATPase 9.2 kDa membrane accessory protein;
DE AltName: Full=V-ATPase M9.2 subunit;
DE AltName: Full=Vacuolar proton pump subunit e 1;
GN Name=ATP6V0E1; Synonyms=ATP6H, ATP6V0E;
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=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-20, AND NUCLEOTIDE SEQUENCE [MRNA] OF 20-81.
RC TISSUE=Adrenal medulla;
RX PubMed=9556572; DOI=10.1074/jbc.273.18.10939;
RA Ludwig J., Kerscher S., Brandt U., Pfeiffer K., Getlawi F., Apps D.K.,
RA Schaegger H.;
RT "Identification and characterization of a novel 9.2-kDa membrane sector-
RT associated protein of vacuolar proton-ATPase from chromaffin granules.";
RL J. Biol. Chem. 273:10939-10947(1998).
CC -!- FUNCTION: Subunit of the V0 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:O15342, ECO:0000250|UniProtKB:Q2KIB5}.
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). {ECO:0000250|UniProtKB:O15342}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in lung, heart, spleen, kidney and
CC adrenal gland. Not found in brain.
CC -!- SIMILARITY: Belongs to the V-ATPase e1/e2 subunit family.
CC {ECO:0000305}.
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DR EMBL; BC103204; AAI03205.1; -; mRNA.
DR EMBL; Y15285; CAA75570.1; -; mRNA.
DR RefSeq; NP_001029222.1; NM_001034050.2.
DR AlphaFoldDB; P81103; -.
DR SMR; P81103; -.
DR CORUM; P81103; -.
DR STRING; 9913.ENSBTAP00000020094; -.
DR PaxDb; P81103; -.
DR PRIDE; P81103; -.
DR Ensembl; ENSBTAT00000020094; ENSBTAP00000020094; ENSBTAG00000015100.
DR GeneID; 338075; -.
DR KEGG; bta:338075; -.
DR CTD; 8992; -.
DR VEuPathDB; HostDB:ENSBTAG00000015100; -.
DR VGNC; VGNC:26314; ATP6V0E1.
DR eggNOG; KOG3500; Eukaryota.
DR GeneTree; ENSGT00940000156866; -.
DR HOGENOM; CLU_170555_0_1_1; -.
DR InParanoid; P81103; -.
DR OMA; AREWGNP; -.
DR OrthoDB; 1613627at2759; -.
DR TreeFam; TF300290; -.
DR Reactome; R-BTA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-BTA-9639288; Amino acids regulate mTORC1.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000015100; Expressed in adenohypophysis and 103 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR008389; ATPase_V0-cplx_e1/e2_su.
DR InterPro; IPR017385; ATPase_V0-cplx_e1/e2_su_met.
DR PANTHER; PTHR12263; PTHR12263; 1.
DR Pfam; PF05493; ATP_synt_H; 1.
DR PIRSF; PIRSF038097; V-ATP_synth_e1/e2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9556572"
FT CHAIN 2..81
FT /note="V-type proton ATPase subunit e 1"
FT /id="PRO_0000071738"
FT TOPO_DOM 2..7
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..81
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 81 AA; 9304 MW; 8E5B29BFDD305844 CRC64;
MAYTGLTVPL IVMSVFWGIV GFLVPWFIPK GPNRGVIITM LVTCSVCCYL FWLIAILAQL
NPLFGPQLKN ETIWYLKYHW P
