ID   VATG3_XENLA             Reviewed;         118 AA.
AC   Q5XGW0;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=V-type proton ATPase subunit G 3;
DE            Short=V-ATPase subunit G 3;
GN   Name=atp6v1g3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) 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. V-ATPase is responsible for acidifying and maintaining the pH
CC       of intracellular compartments and in some cell types, is targeted to
CC       the plasma membrane, where it is responsible for acidifying the
CC       extracellular environment. {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. 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 two accessory
CC       subunits. {ECO:0000250|UniProtKB:O75348}.
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; BC084318; AAH84318.1; -; mRNA.
DR   RefSeq; NP_001088408.1; NM_001094939.1.
DR   AlphaFoldDB; Q5XGW0; -.
DR   SMR; Q5XGW0; -.
DR   DNASU; 495264; -.
DR   GeneID; 495264; -.
DR   KEGG; xla:495264; -.
DR   CTD; 495264; -.
DR   Xenbase; XB-GENE-6254107; atp6v1g3.L.
DR   OMA; DQYRMQK; -.
DR   OrthoDB; 1566576at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 495264; Expressed in kidney and 9 other tissues.
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   Coiled coil; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..118
FT                   /note="V-type proton ATPase subunit G 3"
FT                   /id="PRO_0000364225"
FT   REGION          19..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          3..54
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   118 AA;  13871 MW;  05C6E4FCED0A5141 CRC64;
     MASQSQGIQQ LLQAEKRAKD KLEEAKKRKN KRLRQAKEEA TADIDQYRLK READFRRIQT
     SVMGSQGNLA VKIEEQTVEK IQFYSSSYNK YKEGVLKELL DLAYNIKPEL HTNYKYKI