ID   VATG2_MACMU             Reviewed;         118 AA.
AC   Q5TM18;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=V-type proton ATPase subunit G 2;
DE            Short=V-ATPase subunit G 2;
DE   AltName: Full=Vacuolar proton pump subunit G 2;
GN   Name=ATP6V1G2;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15269276; DOI=10.1093/molbev/msh216;
RA   Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT   "Rhesus macaque class I duplicon structures, organization, and evolution
RT   within the alpha block of the major histocompatibility complex.";
RL   Mol. Biol. Evol. 21:2079-2091(2004).
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 the accessory
CC       subunits ATP6AP1/Ac45 and ATP6AP2/PRR. {ECO:0000250|UniProtKB:O75348}.
CC   -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000250|UniProtKB:O95670}.
CC       Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC       {ECO:0000250|UniProtKB:Q0VCV6}; Peripheral membrane protein
CC       {ECO:0000305}. Note=Highly enriched in late-stage melanosomes.
CC       {ECO:0000250|UniProtKB:O95670}.
CC   -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {ECO:0000305}.
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DR   EMBL; AB128049; BAD69727.1; -; Genomic_DNA.
DR   RefSeq; NP_001040610.1; NM_001047145.1.
DR   AlphaFoldDB; Q5TM18; -.
DR   SMR; Q5TM18; -.
DR   Ensembl; ENSMMUT00000092688; ENSMMUP00000071954; ENSMMUG00000052422.
DR   GeneID; 715331; -.
DR   KEGG; mcc:715331; -.
DR   CTD; 534; -.
DR   VEuPathDB; HostDB:ENSMMUG00000052422; -.
DR   GeneTree; ENSGT00940000161280; -.
DR   HOGENOM; CLU_125101_1_1_1; -.
DR   OrthoDB; 1566576at2759; -.
DR   Proteomes; UP000006718; Chromosome 4.
DR   Bgee; ENSMMUG00000052422; Expressed in superior frontal gyrus and 13 other tissues.
DR   ExpressionAtlas; Q5TM18; baseline.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:Ensembl.
DR   GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR   GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IBA:GO_Central.
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   Cytoplasmic vesicle; Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Transport.
FT   CHAIN           1..118
FT                   /note="V-type proton ATPase subunit G 2"
FT                   /id="PRO_0000192901"
FT   REGION          23..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   118 AA;  13595 MW;  5D51C9D0DFF0557D CRC64;
     MASQSQGIQQ LLQAEKRAAE KVADARKRKA RRLKQAKEEA QMEVEQYRRE REQEFQSKQQ
     AAMGSQGNLS AEVEQATRRQ VQGMQSSQQR NRERVLAQLL GMVCDVRPQV HPNYRISA