VATB1_ARATH
ID VATB1_ARATH Reviewed; 486 AA.
AC P11574; Q42205; Q8L584; Q9LQR5;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=V-type proton ATPase subunit B1;
DE Short=V-ATPase subunit B1;
DE AltName: Full=V-ATPase 57 kDa subunit;
DE AltName: Full=Vacuolar H(+)-ATPase subunit B isoform 1;
DE AltName: Full=Vacuolar proton pump subunit B1;
GN Name=VHA-B1; Synonyms=AT57; OrderedLocusNames=At1g76030; ORFNames=T4O12.24;
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].
RX PubMed=2903860; DOI=10.1016/s0021-9258(19)81313-3;
RA Manolson M.F., Ouellette B.F.F., Filion M., Poole R.J.;
RT "cDNA sequence and homologies of the '57-kDa' nucleotide-binding subunit of
RT the vacuolar ATPase from Arabidopsis.";
RL J. Biol. Chem. 263:17987-17994(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 235-334.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
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).
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 -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC36485.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J04185; AAC36485.1; ALT_INIT; mRNA.
DR EMBL; AC007396; AAF26763.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35786.1; -; Genomic_DNA.
DR EMBL; AY094424; AAM19797.1; -; mRNA.
DR EMBL; AY125532; AAM78042.1; -; mRNA.
DR EMBL; Z29126; CAA82390.1; -; mRNA.
DR PIR; A31886; A31886.
DR PIR; G96788; G96788.
DR RefSeq; NP_177729.1; NM_106251.5.
DR AlphaFoldDB; P11574; -.
DR SMR; P11574; -.
DR BioGRID; 29153; 13.
DR IntAct; P11574; 2.
DR STRING; 3702.AT1G76030.1; -.
DR MoonProt; P11574; -.
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; P11574; -.
DR PaxDb; P11574; -.
DR PRIDE; P11574; -.
DR ProteomicsDB; 243222; -.
DR EnsemblPlants; AT1G76030.1; AT1G76030.1; AT1G76030.
DR GeneID; 843934; -.
DR Gramene; AT1G76030.1; AT1G76030.1; AT1G76030.
DR KEGG; ath:AT1G76030; -.
DR Araport; AT1G76030; -.
DR TAIR; locus:2204430; AT1G76030.
DR eggNOG; KOG1351; Eukaryota.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; P11574; -.
DR OMA; TNDITHP; -.
DR OrthoDB; 541116at2759; -.
DR PhylomeDB; P11574; -.
DR BioCyc; ARA:AT1G76030-MON; -.
DR PRO; PR:P11574; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P11574; baseline and differential.
DR Genevisible; P11574; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0051015; F:actin filament binding; IDA:TAIR.
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:0051017; P:actin filament bundle assembly; IDA:TAIR.
DR GO; GO:0051693; P:actin filament capping; IDA:TAIR.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IMP:TAIR.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IDA:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CAFA.
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 2: Evidence at transcript level;
KW Acetylation; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN1"
FT CHAIN 2..486
FT /note="V-type proton ATPase subunit B1"
FT /id="PRO_0000144639"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN1"
FT CONFLICT 297
FT /note="R -> V (in Ref. 5; CAA82390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 54108 MW; 0EC3B68E92CC9F0A CRC64;
MGTNDLDIEE GTLEIGMEYR TVSGVAGPLV ILDKVKGPKY QEIVNIRLGD GSTRRGQVLE
VDGEKAVVQV FEGTSGIDNK FTTVQFTGEV LKTPVSLDML GRIFNGSGKP IDNGPPILPE
AYLDISGSSI NPSERTYPEE MIQTGISTID VMNSIARGQK IPLFSAAGLP HNEIAAQICR
QAGLVKRLEK TVDLLEDHGE DNFAIVFAAM GVNMETAQFF KRDFEENGSM ERVTLFLNLA
NDPTIERIIT PRIALTTAEY LAYECGKHVL VILTDMSSYA DALREVSAAR EEVPGRRGYP
GYMYTDLATI YERAGRIEGR KGSITQIPIL TMPNDDITHP TPDLTGYITE GQIYIDRQLH
NRQIYPPINV LPSLSRLMKS AIGEGMTRKD HSDVSNQLYA NYAIGKDVQA MKAVVGEEAL
SSEDLLYLEF LDKFERKFVM QGAYDTRNIF QSLDLAWTLL RIFPRELLHR IPAKTLDQFY
SRDSTS
