ID   VATG1_CANLF             Reviewed;         118 AA.
AC   Q5WR09;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=V-type proton ATPase subunit G 1;
DE            Short=V-ATPase subunit G 1;
DE   AltName: Full=Vacuolar proton pump subunit G 1;
GN   Name=ATP6V1G1; Synonyms=ATP6G;
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 [GENOMIC DNA].
RA   Wagner J.L., Palti Y., DiDario D.D.;
RT   "Gemomic map of a portion of the canine MHC class I histocompatibility
RT   complex.";
RL   Submitted (SEP-2003) 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 (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). In aerobic
CC       conditions, involved in intracellular iron homeostasis, thus triggering
CC       the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to
CC       HIF1A hydroxylation and subsequent proteasomal degradation (By
CC       similarity). {ECO:0000250|UniProtKB:O75348}.
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:O75348}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:O75348}.
CC   -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {ECO:0000305}.
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DR   EMBL; AY423389; AAR27887.1; -; Genomic_DNA.
DR   RefSeq; NP_001014398.1; NM_001014376.1.
DR   AlphaFoldDB; Q5WR09; -.
DR   SMR; Q5WR09; -.
DR   STRING; 9612.ENSCAFP00000000733; -.
DR   PaxDb; Q5WR09; -.
DR   Ensembl; ENSCAFT00040017226; ENSCAFP00040014934; ENSCAFG00040009280.
DR   Ensembl; ENSCAFT00845018361; ENSCAFP00845014333; ENSCAFG00845010427.
DR   GeneID; 474840; -.
DR   KEGG; cfa:474840; -.
DR   CTD; 534; -.
DR   VEuPathDB; HostDB:ENSCAFG00845010427; -.
DR   eggNOG; KOG1772; Eukaryota.
DR   GeneTree; ENSGT00940000161280; -.
DR   HOGENOM; CLU_125101_1_1_1; -.
DR   InParanoid; Q5WR09; -.
DR   OMA; HPNYRIT; -.
DR   OrthoDB; 1566576at2759; -.
DR   TreeFam; TF313777; -.
DR   Proteomes; UP000002254; Chromosome 12.
DR   Bgee; ENSCAFG00000000513; Expressed in temporal lobe and 50 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   InterPro; IPR005124; V-ATPase_G.
DR   PANTHER; PTHR12713; PTHR12713; 1.
DR   Pfam; PF03179; V-ATPase_G; 1.
DR   TIGRFAMs; TIGR01147; V_ATP_synt_G; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cell membrane; Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O75348"
FT   CHAIN           2..118
FT                   /note="V-type proton ATPase subunit G 1"
FT                   /id="PRO_0000192896"
FT   REGION          55..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O75348"
SQ   SEQUENCE   118 AA;  13592 MW;  586A80CAECD9557D CRC64;
     MASQSQGIQQ LLQAEKRAAE KVADARKRKA RRLKQAKEEA QMEVELYRRE REQEFQSKQQ
     AAMGSQGNLS AEVEQATRRQ VQGMQSSQQR NRERVLAQLL GMVCDVRPQV HPNYRIAV