VATG1_ARATH
ID VATG1_ARATH Reviewed; 110 AA.
AC O82628;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=V-type proton ATPase subunit G1;
DE Short=V-ATPase subunit G1;
DE AltName: Full=Vacuolar H(+)-ATPase subunit G isoform 1;
DE AltName: Full=Vacuolar proton pump subunit G1;
GN Name=VHA-G1; Synonyms=AVMA10, VAG1, VATG1, VMA10;
GN OrderedLocusNames=At3g01390; ORFNames=T13O15.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RA Rouquie D., Tournaire-Roux C., Szponarski W., Rossignol M., Doumas P.;
RT "Cloning and expression of G subunits of vacuolar-type ATPase from
RT plants.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hagai K., Nelson H., Nelson N.;
RT "cDNA encoding subunit G of Arabidopsis thaliana V-ATPase.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11950611; DOI=10.1016/s1360-1385(02)02240-9;
RA Sze H., Schumacher K., Mueller M.L., Padmanaban S., Taiz L.;
RT "A simple nomenclature for a complex proton pump: VHA genes encode the
RT vacuolar H(+)-ATPase.";
RL Trends Plant Sci. 7:157-161(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
CC -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar
CC ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of
CC intracellular compartments in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c'', d and e).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
CC Vacuole membrane {ECO:0000269|PubMed:17151019}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {ECO:0000305}.
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DR EMBL; AJ005901; CAA06758.1; -; mRNA.
DR EMBL; AF181688; AAD54418.1; -; mRNA.
DR EMBL; AC010870; AAF24609.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73659.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73660.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65962.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65963.1; -; Genomic_DNA.
DR EMBL; AY072365; AAL62357.1; -; mRNA.
DR EMBL; AY114730; AAM48049.1; -; mRNA.
DR PIR; T51825; T51825.
DR RefSeq; NP_001327894.1; NM_001337334.1.
DR RefSeq; NP_001327895.1; NM_001337333.1.
DR RefSeq; NP_186788.1; NM_111005.6.
DR RefSeq; NP_850489.1; NM_180158.3.
DR AlphaFoldDB; O82628; -.
DR SMR; O82628; -.
DR BioGRID; 6463; 4.
DR IntAct; O82628; 1.
DR STRING; 3702.AT3G01390.2; -.
DR TCDB; 3.A.2.2.5; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; O82628; -.
DR MetOSite; O82628; -.
DR PaxDb; O82628; -.
DR PRIDE; O82628; -.
DR ProteomicsDB; 243223; -.
DR EnsemblPlants; AT3G01390.1; AT3G01390.1; AT3G01390.
DR EnsemblPlants; AT3G01390.2; AT3G01390.2; AT3G01390.
DR EnsemblPlants; AT3G01390.3; AT3G01390.3; AT3G01390.
DR EnsemblPlants; AT3G01390.4; AT3G01390.4; AT3G01390.
DR GeneID; 821130; -.
DR Gramene; AT3G01390.1; AT3G01390.1; AT3G01390.
DR Gramene; AT3G01390.2; AT3G01390.2; AT3G01390.
DR Gramene; AT3G01390.3; AT3G01390.3; AT3G01390.
DR Gramene; AT3G01390.4; AT3G01390.4; AT3G01390.
DR KEGG; ath:AT3G01390; -.
DR Araport; AT3G01390; -.
DR TAIR; locus:2096682; AT3G01390.
DR eggNOG; KOG1772; Eukaryota.
DR HOGENOM; CLU_125101_3_1_1; -.
DR InParanoid; O82628; -.
DR OMA; HSKGNEQ; -.
DR OrthoDB; 1599029at2759; -.
DR PhylomeDB; O82628; -.
DR PRO; PR:O82628; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O82628; baseline and differential.
DR Genevisible; O82628; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0016469; C:proton-transporting two-sector ATPase complex; ISS:TAIR.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISS:TAIR.
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 1: Evidence at protein level;
KW Acetylation; Cell membrane; Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transport; Vacuole.
FT CHAIN 1..110
FT /note="V-type proton ATPase subunit G1"
FT /id="PRO_0000192908"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O82629"
SQ SEQUENCE 110 AA; 12397 MW; C486D697AD434142 CRC64;
MESNRGQGSI QQLLAAEVEA QHIVNAARTA KMARLKQAKE EAEKEIAEYK AQTEQDFQRK
LEETSGDSGA NVKRLEQETD TKIEQLKNEA SRISKDVVEM LLKHVTTVKN
