VATH_ARATH
ID VATH_ARATH Reviewed; 441 AA.
AC Q9LX65;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=V-type proton ATPase subunit H;
DE Short=V-ATPase subunit H;
DE AltName: Full=Vacuolar H(+)-ATPase subunit H;
DE AltName: Full=Vacuolar proton pump subunit H;
GN Name=VHA-H; OrderedLocusNames=At3g42050; ORFNames=F4M19_10;
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 [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 [2]
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 [3]
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 [4]
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 [5]
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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase.
CC Subunit H activates the ATPase activity of the enzyme and couples
CC ATPase activity to proton flow. Vacuolar ATPase is responsible for
CC acidifying a variety of intracellular compartments in eukaryotic cells,
CC thus providing most of the energy required for transport processes in
CC the vacuolar system (By similarity). {ECO:0000250}.
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: Vacuole membrane {ECO:0000269|PubMed:17151019};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the V-ATPase H subunit family. {ECO:0000305}.
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DR EMBL; AL356013; CAB91576.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77718.1; -; Genomic_DNA.
DR EMBL; AY091685; AAM10284.1; -; mRNA.
DR PIR; T48960; T48960.
DR RefSeq; NP_189791.1; NM_114072.4.
DR AlphaFoldDB; Q9LX65; -.
DR SMR; Q9LX65; -.
DR BioGRID; 8496; 5.
DR IntAct; Q9LX65; 1.
DR STRING; 3702.AT3G42050.1; -.
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; Q9LX65; -.
DR SwissPalm; Q9LX65; -.
DR PaxDb; Q9LX65; -.
DR PRIDE; Q9LX65; -.
DR ProteomicsDB; 228528; -.
DR DNASU; 823170; -.
DR EnsemblPlants; AT3G42050.1; AT3G42050.1; AT3G42050.
DR GeneID; 823170; -.
DR Gramene; AT3G42050.1; AT3G42050.1; AT3G42050.
DR KEGG; ath:AT3G42050; -.
DR Araport; AT3G42050; -.
DR TAIR; locus:2083881; AT3G42050.
DR eggNOG; KOG2759; Eukaryota.
DR HOGENOM; CLU_025709_3_0_1; -.
DR InParanoid; Q9LX65; -.
DR OMA; KDQNVRY; -.
DR OrthoDB; 751335at2759; -.
DR PhylomeDB; Q9LX65; -.
DR PRO; PR:Q9LX65; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LX65; baseline and differential.
DR Genevisible; Q9LX65; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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:0005774; C:vacuolar membrane; HDA:TAIR.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 1.25.40.150; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004908; ATPase_V1-cplx_hsu.
DR InterPro; IPR011987; ATPase_V1-cplx_hsu_C.
DR InterPro; IPR038497; ATPase_V1-cplx_hsu_C_sf.
DR PANTHER; PTHR10698; PTHR10698; 1.
DR Pfam; PF11698; V-ATPase_H_C; 1.
DR Pfam; PF03224; V-ATPase_H_N; 1.
DR PIRSF; PIRSF032184; ATPase_V1_H; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transport; Vacuole.
FT CHAIN 1..441
FT /note="V-type proton ATPase subunit H"
FT /id="PRO_0000124200"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 441 AA; 50284 MW; E0D57EB194158528 CRC64;
MDQAELSIEQ VLKRDIPWET YMNTKLVSAK GLQLLRRYDK KPESARAQLL DEDGPAYVHL
FVSILRDIFK EETVEYVLAL IYEMLSANPT RARLFHDESL ANEDTYEPFL RLLWKGNWFI
QEKSCKILAW IISARPKAGN AVIGNGIDDV LKGLVEWLCA QLKQPSHPTR GVPIAISCLS
SLLKEPVVRS SFVQADGVKL LVPLISPAST QQSIQLLYET CLCIWLLSYY EPAIEYLATS
RTMQRLTEVV KHSTKEKVVR VVILTFRNLL PKGTFGAQMV DLGLPHIIHS LKTQAWSDED
LLDALNQLEE GLKDKIKKLS SFDKYKQEVL LGHLDWNPMH KETNFWRENV TCFEENDFQI
LRVLLTILDT SSDPRSLAVA CFDISQFIQY HAAGRVIVAD LKAKERVMKL INHENAEVTK
NAILCIQRLL LGAKYASFLQ A
