ID   VA0E1_CANLF             Reviewed;          81 AA.
AC   Q9BDP4; Q9N0Q1;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 90.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Shah A.B., Gitschier J.;
RT   "Identification of canine mRNA for vacuolar-proton ATPase subunit (ATP6H)
RT   mRNA.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11471056; DOI=10.1007/s00335-001-2059-1;
RA   Nanji M., Coronado V.A., Cox D.W.;
RT   "ATP6H, a subunit of vacuolar ATPase involved in metal transport:
RT   evaluation in canine copper toxicosis.";
RL   Mamm. Genome 12:617-621(2001).
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   -!- SIMILARITY: Belongs to the V-ATPase e1/e2 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF258614; AAF71753.1; -; mRNA.
DR   EMBL; AF343440; AAK28556.1; -; mRNA.
DR   RefSeq; NP_001003128.1; NM_001003128.1.
DR   AlphaFoldDB; Q9BDP4; -.
DR   SMR; Q9BDP4; -.
DR   STRING; 9612.ENSCAFP00000039612; -.
DR   PaxDb; Q9BDP4; -.
DR   GeneID; 403729; -.
DR   KEGG; cfa:403729; -.
DR   CTD; 8992; -.
DR   eggNOG; KOG3500; Eukaryota.
DR   InParanoid; Q9BDP4; -.
DR   OrthoDB; 1613627at2759; -.
DR   Proteomes; UP000002254; Unplaced.
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   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   3: Inferred from homology;
KW   Glycoprotein; Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..81
FT                   /note="V-type proton ATPase subunit e 1"
FT                   /id="PRO_0000071739"
FT   TOPO_DOM        1..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"
FT   CONFLICT        77
FT                   /note="K -> R (in Ref. 1; AAF71753)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   81 AA;  9364 MW;  9A47FE60DD242F27 CRC64;
     MAYHGLTVPL IVMSVFWGFV GFCVPWFIPK GPNRGVIITM LVTCSVCCYL FWLIAILAQL
     NPLFGPQLKN ETIWYLKYHW P