VDAC1_ARATH
ID VDAC1_ARATH Reviewed; 276 AA.
AC Q9SRH5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Mitochondrial outer membrane protein porin 1;
DE AltName: Full=Voltage-dependent anion-selective channel protein 1;
DE Short=AtVDAC1;
DE Short=VDAC-1;
GN Name=VDAC1; OrderedLocusNames=At3g01280; ORFNames=T22N4.9;
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 PROTEIN SEQUENCE OF 2-9, AND SUBCELLULAR LOCATION.
RC TISSUE=Leaf, and Stem;
RX PubMed=11743114; DOI=10.1104/pp.010474;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=19326079; DOI=10.1007/s10059-009-0041-z;
RA Lee S.M., Hoang M.H., Han H.J., Kim H.S., Lee K., Kim K.E., Kim D.H.,
RA Lee S.Y., Chung W.S.;
RT "Pathogen inducible voltage-dependent anion channel (AtVDAC) isoforms are
RT localized to mitochondria membrane in Arabidopsis.";
RL Mol. Cells 27:321-327(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, GENE FAMILY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-223.
RX PubMed=21705391; DOI=10.1093/jxb/err113;
RA Tateda C., Watanabe K., Kusano T., Takahashi Y.;
RT "Molecular and genetic characterization of the gene family encoding the
RT voltage-dependent anion channel in Arabidopsis.";
RL J. Exp. Bot. 62:4773-4785(2011).
CC -!- FUNCTION: Forms a channel through the mitochondrial outer membrane that
CC allows diffusion of small hydrophilic molecules. The channel adopts an
CC open conformation at low or zero membrane potential and a closed
CC conformation at potentials above 30-40 mV. The open state has a weak
CC anion selectivity whereas the closed state is cation-selective (By
CC similarity). Involved in plant development at reproductive stage, is
CC important for pollen development and may regulate hydrogen peroxide
CC generation during disease resistance. {ECO:0000250,
CC ECO:0000269|PubMed:21705391}.
CC -!- INTERACTION:
CC Q9SRH5; Q42525: HXK1; NbExp=2; IntAct=EBI-1644501, EBI-1644489;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:19326079, ECO:0000269|PubMed:21705391}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot meristems, root meristematic
CC zone, lateral roots, leaves, stigma and anthers.
CC {ECO:0000269|PubMed:21705391}.
CC -!- INDUCTION: By the bacterial pathogen P.syringae pv. tomato.
CC {ECO:0000269|PubMed:19326079, ECO:0000269|PubMed:21705391}.
CC -!- DOMAIN: Consists mainly of membrane-spanning sided beta-sheets.
CC -!- DISRUPTION PHENOTYPE: In vdac1-6 homozygous plants, normal growth, but
CC small siliques and decreased pollen germination rate and tube length.
CC {ECO:0000269|PubMed:21705391}.
CC -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin (TC 1.B.8.1)
CC family. {ECO:0000305}.
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DR EMBL; AC010676; AAF03498.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73632.1; -; Genomic_DNA.
DR EMBL; AY037217; AAK59817.1; -; mRNA.
DR EMBL; AY113169; AAM47472.1; -; mRNA.
DR RefSeq; NP_186777.1; NM_110994.4.
DR AlphaFoldDB; Q9SRH5; -.
DR SMR; Q9SRH5; -.
DR BioGRID; 6248; 6.
DR IntAct; Q9SRH5; 4.
DR MINT; Q9SRH5; -.
DR STRING; 3702.AT3G01280.1; -.
DR TCDB; 1.B.8.1.15; the mitochondrial and plastid porin (mpp) family.
DR iPTMnet; Q9SRH5; -.
DR PaxDb; Q9SRH5; -.
DR PRIDE; Q9SRH5; -.
DR ProteomicsDB; 243225; -.
DR DNASU; 820914; -.
DR EnsemblPlants; AT3G01280.1; AT3G01280.1; AT3G01280.
DR GeneID; 820914; -.
DR Gramene; AT3G01280.1; AT3G01280.1; AT3G01280.
DR KEGG; ath:AT3G01280; -.
DR Araport; AT3G01280; -.
DR TAIR; locus:2100252; AT3G01280.
DR eggNOG; KOG3126; Eukaryota.
DR HOGENOM; CLU_069937_0_0_1; -.
DR InParanoid; Q9SRH5; -.
DR OMA; CRIPDQS; -.
DR OrthoDB; 938262at2759; -.
DR PhylomeDB; Q9SRH5; -.
DR PRO; PR:Q9SRH5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRH5; baseline and differential.
DR Genevisible; Q9SRH5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0008308; F:voltage-gated anion channel activity; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR CDD; cd07306; Porin3_VDAC; 1.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR001925; Porin_Euk.
DR InterPro; IPR027246; Porin_Euk/Tom40.
DR PANTHER; PTHR11743; PTHR11743; 1.
DR Pfam; PF01459; Porin_3; 1.
DR PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Plant defense; Porin; Reference proteome;
KW Transmembrane; Transmembrane beta strand; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11743114"
FT CHAIN 2..276
FT /note="Mitochondrial outer membrane protein porin 1"
FT /id="PRO_0000050526"
FT MUTAGEN 223
FT /note="P->H: Alteration of subcellular localization."
FT /evidence="ECO:0000269|PubMed:21705391"
SQ SEQUENCE 276 AA; 29425 MW; 7F33F53E56E9765C CRC64;
MVKGPGLYTE IGKKARDLLY KDHNSDQKFS ITTFSPAGVA ITSTGTKKGD LLLGDVAFQS
RRKNITTDLK VCTDSTFLIT ATVDEAAPGL RSIFSFKVPD QNSGKVELQY LHEYAGISTS
MGLTQNPTVN FSGVIGSNVL AVGTDVSFDT KSGNFTKINA GLSFTKEDLI ASLTVNDKGD
LLNASYYHIV NPLFNTAVGA EVSHKLSSKD STITVGTQHS LDPLTSVKAR VNSAGIASAL
IQHEWKPKSF FTISGEVDTK SIDKSAKVGL ALALKP
