VATG2_BOVIN
ID VATG2_BOVIN Reviewed; 118 AA.
AC Q0VCV6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=V-type proton ATPase subunit G 2 {ECO:0000305};
DE Short=V-ATPase subunit G 2 {ECO:0000305};
DE AltName: Full=Vacuolar proton pump subunit G 2 {ECO:0000305};
GN Name=ATP6V1G2 {ECO:0000312|VGNC:VGNC:57164};
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 {ECO:0000312|EMBL:AAI19977.1};
RN [1] {ECO:0000312|EMBL:AAI19977.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI19977.1};
RC TISSUE=Brain cortex {ECO:0000312|EMBL:AAI19977.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32764564; DOI=10.1038/s41467-020-17762-9;
RA Wang R., Long T., Hassan A., Wang J., Sun Y., Xie X.S., Li X.;
RT "Cryo-EM structures of intact V-ATPase from bovine brain.";
RL Nat. Commun. 11:3921-3921(2020).
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 (PubMed:32764564). 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 (PubMed:32764564).
CC {ECO:0000269|PubMed:32764564}.
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 (PubMed:32764564). The V1 complex consists of three
CC catalytic AB heterodimers that form a heterohexamer, three peripheral
CC stalks each consisting of EG heterodimers, one central rotor including
CC subunits D and F, and the regulatory subunits C and H
CC (PubMed:32764564). The proton translocation complex V0 consists of the
CC proton transport subunit a, a ring of proteolipid subunits c9c'',
CC rotary subunit d, subunits e and f, and the accessory subunits
CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:32764564).
CC {ECO:0000269|PubMed:32764564}.
CC -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000250|UniProtKB:O95670}.
CC Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000269|PubMed:32764564}; Peripheral membrane protein
CC {ECO:0000305}. Note=Highly enriched in late-stage melanosomes.
CC {ECO:0000250|UniProtKB:O95670}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32764564}.
CC -!- SIMILARITY: Belongs to the V-ATPase G subunit family.
CC {ECO:0000255|RuleBase:RU364019}.
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DR EMBL; BC119976; AAI19977.1; -; mRNA.
DR RefSeq; NP_001069132.1; NM_001075664.1.
DR PDB; 6XBW; EM; 3.37 A; M/N/O=1-118.
DR PDB; 6XBY; EM; 3.79 A; M/N/O=1-118.
DR PDB; 7KHR; EM; 3.62 A; M/N/O=1-118.
DR PDBsum; 6XBW; -.
DR PDBsum; 6XBY; -.
DR PDBsum; 7KHR; -.
DR SMR; Q0VCV6; -.
DR STRING; 9913.ENSBTAP00000019267; -.
DR PaxDb; Q0VCV6; -.
DR Ensembl; ENSBTAT00000019267; ENSBTAP00000019267; ENSBTAG00000014491.
DR GeneID; 514368; -.
DR KEGG; bta:514368; -.
DR CTD; 534; -.
DR VEuPathDB; HostDB:ENSBTAG00000014491; -.
DR VGNC; VGNC:57164; ATP6V1G2.
DR eggNOG; KOG1772; Eukaryota.
DR GeneTree; ENSGT00940000161280; -.
DR HOGENOM; CLU_125101_1_1_1; -.
DR InParanoid; Q0VCV6; -.
DR OMA; HPNYRIT; -.
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 23.
DR Bgee; ENSBTAG00000014491; Expressed in retina and 81 other tissues.
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: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; IDA: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:0045851; P:pH reduction; IC:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IC: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 3D-structure; Coiled coil; Cytoplasmic vesicle; Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Transport.
FT CHAIN 1..118
FT /note="V-type proton ATPase subunit G 2"
FT /id="PRO_0000454079"
FT REGION 25..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 8..57
FT /evidence="ECO:0000255"
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"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 44..73
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:6XBW"
SQ SEQUENCE 118 AA; 13565 MW; 5D48ED95DEB4107D CRC64;
MASQSQGIQQ LLQAEKRAAE KVADARKRKA RRLKQAKEEA QMEVDQYRRE REQEFQSKQQ
AAMGSQGNLS AEVEQATRRQ VQGMQSSQQR NRERVLAQLL GMVCDVRPQV HPNYRIAA
