VATE3_ARATH
ID VATE3_ARATH Reviewed; 237 AA.
AC P0CAN7; Q9SH70;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=V-type proton ATPase subunit E3;
DE Short=V-ATPase subunit E3;
DE AltName: Full=Vacuolar H(+)-ATPase subunit E isoform 3;
DE AltName: Full=Vacuolar proton pump subunit E3;
GN Name=VHA-E3; OrderedLocusNames=At1g64200; ORFNames=F22C12.4;
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=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 [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=17565583; DOI=10.1111/j.1365-313x.2007.03136.x;
RA Silverstein K.A.T., Moskal W.A. Jr., Wu H.C., Underwood B.A., Graham M.A.,
RA Town C.D., VandenBosch K.A.;
RT "Small cysteine-rich peptides resembling antimicrobial peptides have been
RT under-predicted in plants.";
RL Plant J. 51:262-280(2007).
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 DEVELOPMENTAL STAGE.
RX PubMed=15610355; DOI=10.1111/j.1365-313x.2004.02283.x;
RA Strompen G., Dettmer J., Stierhof Y.-D., Schumacher K., Juergens G.,
RA Mayer U.;
RT "Arabidopsis vacuolar H(+)-ATPase subunit E isoform 1 is required for Golgi
RT organization and vacuole function in embryogenesis.";
RL Plant J. 41:125-132(2005).
CC -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase
CC essential for assembly or catalytic function. V-ATPase is responsible
CC for acidifying a variety of intracellular compartments in eukaryotic
CC cells (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:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
CC {ECO:0000269|PubMed:15610355}.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24559.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g64195 and At1g64200.; Evidence={ECO:0000305};
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DR EMBL; AC007764; AAF24559.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34209.1; -; Genomic_DNA.
DR EMBL; EF182846; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; C96666; C96666.
DR RefSeq; NP_176602.1; NM_105094.3.
DR AlphaFoldDB; P0CAN7; -.
DR SMR; P0CAN7; -.
DR BioGRID; 27946; 10.
DR STRING; 3702.AT1G64200.1; -.
DR TCDB; 3.A.2.2.5; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PaxDb; P0CAN7; -.
DR PRIDE; P0CAN7; -.
DR ProteomicsDB; 228578; -.
DR EnsemblPlants; AT1G64200.1; AT1G64200.1; AT1G64200.
DR GeneID; 842725; -.
DR Gramene; AT1G64200.1; AT1G64200.1; AT1G64200.
DR KEGG; ath:AT1G64200; -.
DR Araport; AT1G64200; -.
DR TAIR; locus:2024527; AT1G64200.
DR eggNOG; KOG1664; Eukaryota.
DR HOGENOM; CLU_073641_1_0_1; -.
DR InParanoid; P0CAN7; -.
DR OMA; AIDTQYE; -.
DR OrthoDB; 1489718at2759; -.
DR PhylomeDB; P0CAN7; -.
DR PRO; PR:P0CAN7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P0CAN7; baseline and differential.
DR Genevisible; P0CAN7; AT.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR Gene3D; 3.30.2320.30; -; 1.
DR HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR InterPro; IPR038495; ATPase_E_C.
DR InterPro; IPR002842; ATPase_V1_Esu.
DR PANTHER; PTHR45715; PTHR45715; 1.
DR Pfam; PF01991; vATP-synt_E; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transport; Vacuole.
FT CHAIN 1..237
FT /note="V-type proton ATPase subunit E3"
FT /id="PRO_0000373819"
FT COILED 9..67
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q39258"
SQ SEQUENCE 237 AA; 27085 MW; CCC1E4DB4E9A0C75 CRC64;
MNDADASIQI QQMVRFIRQE AEEKANEISI SSEEEFNIEK LQLVEAEKKK IRQEYEKKEK
QVDVRKKIDY SMQLNASRIK VLQAQDDIVN AMKEEAAKQL LKVSQHGFFN HHHHQYKHLL
KDLIVQCLLR LKEPAVLLRC REEDLDIVES MLDDASEEYC KKAKVHAPEI IVDKDIFLPP
APSDDDPHAL SCAGGVVLAS RDGKIVCENT LDARLEVAFR NKLPEIRKSL FGKVGAA