ID   VATG2_PANTR             Reviewed;         118 AA.
AC   Q1XHY9; Q1XHZ2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA   Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA   Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA   Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA   Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA   Inoko H., Bahram S.;
RT   "Rapid evolution of major histocompatibility complex class I genes in
RT   primates generates new disease alleles in humans via hitchhiking
RT   diversity.";
RL   Genetics 173:1555-1570(2006).
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; AB210169; BAE92778.1; -; Genomic_DNA.
DR   EMBL; AB210170; BAE92781.1; -; Genomic_DNA.
DR   RefSeq; NP_001107639.1; NM_001114167.1.
DR   AlphaFoldDB; Q1XHY9; -.
DR   SMR; Q1XHY9; -.
DR   GeneID; 744244; -.
DR   KEGG; ptr:744244; -.
DR   CTD; 534; -.
DR   InParanoid; Q1XHY9; -.
DR   OrthoDB; 1566576at2759; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
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   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_0000235188"
FT   REGION          25..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   118 AA;  13585 MW;  A1B53CE0C8D76569 CRC64;
     MASQSQGIQQ LLQAEKRAAE KVADARKRKA RRLKQAKEEA QMEVEQYRRE REHEFQSKQQ
     AAMGSQGNLS AEVEQATRHQ VQGMQSSQQR NRERVLAQLL GMVCDVRPQV HPNYRISA