ID   VATG_MANSE              Reviewed;         117 AA.
AC   Q25532;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=V-type proton ATPase subunit G;
DE            Short=V-ATPase subunit G;
DE   AltName: Full=V-ATPase 13 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit G;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   TISSUE=Larval midgut;
RX   PubMed=8626552; DOI=10.1074/jbc.271.14.8502;
RA   Lepier A., Graef R., Azuma M., Merzendorfer H., Harvey W.R., Wieczorek H.;
RT   "The peripheral complex of the tobacco hornworm V-ATPase contains a novel
RT   13-kDa subunit G.";
RL   J. Biol. Chem. 271:8502-8508(1996).
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).
CC       {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 VhaAC45 and ATP6AP2 (By similarity).
CC       {ECO:0000250|UniProtKB:O75348}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:8626552}; Peripheral membrane protein
CC       {ECO:0000305}. Note=Apical plasma membrane of the goblet cells and
CC       Malpighian tubule brush border membrane. {ECO:0000269|PubMed:8626552}.
CC   -!- SIMILARITY: Belongs to the V-ATPase G 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; X92805; CAA63422.1; -; mRNA.
DR   AlphaFoldDB; Q25532; -.
DR   SMR; Q25532; -.
DR   DIP; DIP-61392N; -.
DR   IntAct; Q25532; 1.
DR   PRIDE; Q25532; -.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IEA:InterPro.
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   Cell membrane; Hydrogen ion transport; Ion transport; Membrane; Transport.
FT   CHAIN           1..117
FT                   /note="V-type proton ATPase subunit G"
FT                   /id="PRO_0000192907"
FT   REGION          23..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   117 AA;  13693 MW;  A57A0DC532EB9D74 CRC64;
     MASQTHGIQQ LLAAEKRAAE KVSEARKRKA KRLKQAKEEA QDEVEKYRQE RERQFKEFEA
     KHMGTREGVA AKIDAETRIK IDEMNKMVQT QKEAVIKDVL NLVYDIKPEL HINYRVV