VATB2_ARATH
ID VATB2_ARATH Reviewed; 487 AA.
AC Q9SZN1; B9DGU0; B9DHP3; Q56W88; Q94AY7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=V-type proton ATPase subunit B2;
DE Short=V-ATPase subunit B2;
DE AltName: Full=Vacuolar H(+)-ATPase subunit B isoform 2;
DE AltName: Full=Vacuolar proton pump subunit B2;
GN Name=VHA-B2; OrderedLocusNames=At4g38510; ORFNames=F20M13.70;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-487.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Non-catalytic subunit of the peripheral V1 complex of
CC vacuolar 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: Vacuole membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SZN1-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK73967.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD95251.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL035540; CAB37507.1; -; Genomic_DNA.
DR EMBL; AL161593; CAB80515.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86936.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86937.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86938.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86939.1; -; Genomic_DNA.
DR EMBL; AY039518; AAK62575.1; -; mRNA.
DR EMBL; AY045609; AAK73967.1; ALT_FRAME; mRNA.
DR EMBL; AY059167; AAL15392.1; -; mRNA.
DR EMBL; AY090334; AAL90995.1; -; mRNA.
DR EMBL; AK317281; BAH19957.1; -; mRNA.
DR EMBL; AK317596; BAH20260.1; -; mRNA.
DR EMBL; AK222158; BAD95251.1; ALT_INIT; mRNA.
DR PIR; T05679; T05679.
DR RefSeq; NP_001031807.1; NM_001036730.2. [Q9SZN1-1]
DR RefSeq; NP_001031808.1; NM_001036731.2. [Q9SZN1-1]
DR RefSeq; NP_195563.1; NM_120012.4. [Q9SZN1-1]
DR RefSeq; NP_974707.1; NM_202978.2. [Q9SZN1-1]
DR AlphaFoldDB; Q9SZN1; -.
DR SMR; Q9SZN1; -.
DR BioGRID; 15288; 9.
DR IntAct; Q9SZN1; 1.
DR STRING; 3702.AT4G38510.5; -.
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; Q9SZN1; -.
DR PaxDb; Q9SZN1; -.
DR PRIDE; Q9SZN1; -.
DR ProteomicsDB; 242317; -. [Q9SZN1-1]
DR EnsemblPlants; AT4G38510.1; AT4G38510.1; AT4G38510. [Q9SZN1-1]
DR EnsemblPlants; AT4G38510.2; AT4G38510.2; AT4G38510. [Q9SZN1-1]
DR EnsemblPlants; AT4G38510.3; AT4G38510.3; AT4G38510. [Q9SZN1-1]
DR EnsemblPlants; AT4G38510.4; AT4G38510.4; AT4G38510. [Q9SZN1-1]
DR GeneID; 830008; -.
DR Gramene; AT4G38510.1; AT4G38510.1; AT4G38510. [Q9SZN1-1]
DR Gramene; AT4G38510.2; AT4G38510.2; AT4G38510. [Q9SZN1-1]
DR Gramene; AT4G38510.3; AT4G38510.3; AT4G38510. [Q9SZN1-1]
DR Gramene; AT4G38510.4; AT4G38510.4; AT4G38510. [Q9SZN1-1]
DR KEGG; ath:AT4G38510; -.
DR Araport; AT4G38510; -.
DR eggNOG; KOG1351; Eukaryota.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; Q9SZN1; -.
DR OMA; ILPEAYC; -.
DR PhylomeDB; Q9SZN1; -.
DR BioCyc; ARA:AT4G38510-MON; -.
DR PRO; PR:Q9SZN1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZN1; baseline and differential.
DR Genevisible; Q9SZN1; AT.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR PANTHER; PTHR43389; PTHR43389; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..487
FT /note="V-type proton ATPase subunit B2"
FT /id="PRO_0000373816"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 37
FT /note="K -> R (in Ref. 4; BAH19957)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="I -> F (in Ref. 4; BAH19957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 54305 MW; 170224B66A22F1F1 CRC64;
MGAAENNLEM EGTLEIGMEY RTVSGVAGPL VILEKVKGPK YQEIVNIRLG DGTTRRGQVL
EVDGEKAVVQ VFEGTSGIDN KYTTVQFTGE VLKTPVSLDM LGRIFNGSGK PIDNGPPILP
EAYLDISGSS INPSERTYPE EMIQTGISTI DVMNSIARGQ KIPLFSAAGL PHNEIAAQIC
RQAGLVKRLE KSDNLLEHQE DDNFAIVFAA MGVNMETAQF FKRDFEENGS MERVTLFLNL
ANDPTIERII TPRIALTTAE YLAYECGKHV LVILTDMSSY ADALREVSAA REEVPGRRGY
PGYMYTDLAT IYERAGRIEG RKGSITQIPI LTMPNDDITH PTPDLTGYIT EGQIYIDRQL
HNRQIYPPIN VLPSLSRLMK SAIGEGMTRR DHSDVSNQLY ANYAIGKDVQ AMKAVVGEEA
LSSEDLLYLE FLDKFERKFV AQGAYDTRNI FQSLDLAWTL LRIFPRELLH RIPAKTLDQF
YSRDTTN
