VATG1_BOVIN
ID VATG1_BOVIN Reviewed; 118 AA.
AC P79251; Q32KN3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=V-type proton ATPase subunit G 1;
DE Short=V-ATPase subunit G 1;
DE AltName: Full=V-ATPase 13 kDa subunit 1;
DE AltName: Full=Vacuolar proton pump subunit G 1;
DE AltName: Full=Vacuolar proton pump subunit M16;
GN Name=ATP6V1G1; Synonyms=ATP6G, ATP6G1;
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 [MRNA], AND PROTEIN SEQUENCE OF 83-99.
RC TISSUE=Adrenal medulla;
RX PubMed=8786335; DOI=10.1242/jeb.199.5.1147;
RA Supekova L., Sbia M., Supek F., Ma Y., Nelson N.;
RT "A novel subunit of vacuolar H(+)-ATPase related to the b subunit of F-
RT ATPases.";
RL J. Exp. Biol. 199:1147-1156(1996).
RN [2]
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.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=9099722; DOI=10.1074/jbc.272.16.10721;
RA Crider B.P., Andersen P., White A.E., Zhou Z., Li X., Mattsson J.P.,
RA Lundberg L., Keeling D.J., Xie X.S., Stone D.K., Peng S.B.;
RT "Subunit G of the vacuolar proton pump. Molecular characterization and
RT functional expression.";
RL J. Biol. Chem. 272:10721-10728(1997).
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 ECO:0000250|UniProtKB:Q0VCV6}.
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:Q0VCV6}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:O75348}.
CC -!- TISSUE SPECIFICITY: Brain, heart, kidney and spleen.
CC {ECO:0000269|PubMed:9099722}.
CC -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {ECO:0000305}.
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DR EMBL; S82464; AAB37487.1; -; mRNA.
DR EMBL; BC110010; AAI10011.1; -; mRNA.
DR RefSeq; NP_776670.1; NM_174245.2.
DR AlphaFoldDB; P79251; -.
DR SMR; P79251; -.
DR CORUM; P79251; -.
DR STRING; 9913.ENSBTAP00000000240; -.
DR PaxDb; P79251; -.
DR PeptideAtlas; P79251; -.
DR PRIDE; P79251; -.
DR Ensembl; ENSBTAT00000000240; ENSBTAP00000000240; ENSBTAG00000000203.
DR GeneID; 281641; -.
DR KEGG; bta:281641; -.
DR CTD; 9550; -.
DR VEuPathDB; HostDB:ENSBTAG00000000203; -.
DR VGNC; VGNC:26324; ATP6V1G1.
DR eggNOG; KOG1772; Eukaryota.
DR GeneTree; ENSGT00940000154399; -.
DR HOGENOM; CLU_125101_1_1_1; -.
DR InParanoid; P79251; -.
DR OMA; HSKGNEQ; -.
DR OrthoDB; 1566576at2759; -.
DR TreeFam; TF313777; -.
DR Reactome; R-BTA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-BTA-9639288; Amino acids regulate mTORC1.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000000203; Expressed in adenohypophysis and 104 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Cell membrane; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW 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_0000192895"
FT REGION 19..42
FT /note="Disordered"
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; 13682 MW; F889D85391ECB3A0 CRC64;
MASQSQGIQQ LLQAEKRAAE KVSEARKRKN RRLKQAKEEA QAEVEQYRLQ REKEFKAKEA
AALGSHGSCS TEVEKDTQEK MTILQTYFQQ NRDEVLDNLL AFVCDIRPEI HENYRING
