VDAC3_ARATH
ID VDAC3_ARATH Reviewed; 274 AA.
AC Q9SMX3; Q8L815; Q8LET4;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Mitochondrial outer membrane protein porin 3;
DE AltName: Full=Protein HYPERSENSITIVE RESPONSE 2;
DE Short=Athsr2;
DE AltName: Full=Voltage-dependent anion-selective channel protein 3;
DE Short=AtVDAC3;
DE Short=VDAC-3;
GN Name=VDAC3; Synonyms=HSR2; OrderedLocusNames=At5g15090; ORFNames=F2G14.210;
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 {ECO:0000312|EMBL:CAC01828.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10518009; DOI=10.1016/s0014-5793(99)01233-8;
RA Lacomme C.J., Roby D.;
RT "Identification of new early markers of the hypersensitive response in
RT Arabidopsis thaliana.";
RL FEBS Lett. 459:149-153(1999).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3] {ECO:0000305}
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-16, 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [8]
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 [9]
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 [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GENE FAMILY, AND DISRUPTION
RP PHENOTYPE.
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).
RN [11]
RP INTERACTION WITH KIN14F/KP1.
RX PubMed=21406623; DOI=10.1105/tpc.110.082420;
RA Yang X.Y., Chen Z.W., Xu T., Qu Z., Pan X.D., Qin X.H., Ren D.T., Liu G.Q.;
RT "Arabidopsis kinesin KP1 specifically interacts with VDAC3, a mitochondrial
RT protein, and regulates respiration during seed germination at low
RT temperature.";
RL Plant Cell 23:1093-1106(2011).
RN [12]
RP INTERACTION WITH FBA6 AND GAPC1.
RX PubMed=23316205; DOI=10.3389/fpls.2012.00284;
RA Wojtera-Kwiczor J., Gross F., Leffers H.M., Kang M., Schneider M.,
RA Scheibe R.;
RT "Transfer of a redox-signal through the cytosol by redox-dependent
RT microcompartmentation of glycolytic enzymes at mitochondria and actin
RT cytoskeleton.";
RL Front. Plant Sci. 3:284-284(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
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). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KIN14F/KP1 (PubMed:21406623). Interacts with
CC FBA6 AND GAPC1 (PubMed:23316205). {ECO:0000269|PubMed:21406623,
CC ECO:0000269|PubMed:23316205}.
CC -!- INTERACTION:
CC Q9SMX3; Q9SEU8: TRXM2; NbExp=4; IntAct=EBI-4457873, EBI-4475330;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:11743114,
CC ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:19326079,
CC ECO:0000269|PubMed:21705391}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf tips, anthers and stigma.
CC {ECO:0000269|PubMed:21705391}.
CC -!- INDUCTION: Induced during the hypersensitive response to X.campestris
CC pv campestris and by the bacterial pathogen P.syringae pv. tomato.
CC {ECO:0000269|PubMed:10518009, ECO:0000269|PubMed:19326079}.
CC -!- DOMAIN: Consists mainly of membrane-spanning sided beta-sheets.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {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; AJ131391; CAA10363.1; -; mRNA.
DR EMBL; AL391146; CAC01828.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92115.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92116.1; -; Genomic_DNA.
DR EMBL; AY063891; AAL36247.1; -; mRNA.
DR EMBL; AY122918; AAM67451.1; -; mRNA.
DR EMBL; AY085248; AAM62480.1; -; mRNA.
DR PIR; T51454; T51454.
DR RefSeq; NP_001190314.1; NM_001203385.1.
DR RefSeq; NP_197013.1; NM_121513.5.
DR AlphaFoldDB; Q9SMX3; -.
DR SMR; Q9SMX3; -.
DR BioGRID; 16638; 15.
DR IntAct; Q9SMX3; 2.
DR MINT; Q9SMX3; -.
DR STRING; 3702.AT5G15090.2; -.
DR TCDB; 1.B.8.1.19; the mitochondrial and plastid porin (mpp) family.
DR iPTMnet; Q9SMX3; -.
DR PaxDb; Q9SMX3; -.
DR PRIDE; Q9SMX3; -.
DR ProteomicsDB; 228582; -.
DR EnsemblPlants; AT5G15090.1; AT5G15090.1; AT5G15090.
DR EnsemblPlants; AT5G15090.2; AT5G15090.2; AT5G15090.
DR GeneID; 831361; -.
DR Gramene; AT5G15090.1; AT5G15090.1; AT5G15090.
DR Gramene; AT5G15090.2; AT5G15090.2; AT5G15090.
DR KEGG; ath:AT5G15090; -.
DR Araport; AT5G15090; -.
DR TAIR; locus:2147820; AT5G15090.
DR eggNOG; KOG3126; Eukaryota.
DR HOGENOM; CLU_069937_0_0_1; -.
DR InParanoid; Q9SMX3; -.
DR OMA; QAKLPDH; -.
DR OrthoDB; 938262at2759; -.
DR PhylomeDB; Q9SMX3; -.
DR PRO; PR:Q9SMX3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SMX3; baseline and differential.
DR Genevisible; Q9SMX3; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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; IDA:TAIR.
DR GO; GO:0009060; P:aerobic respiration; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IMP: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 Cell membrane; Direct protein sequencing; Hypersensitive response;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Plant defense; Porin; Reference proteome; Transmembrane;
KW Transmembrane beta strand; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11743114"
FT CHAIN 2..274
FT /note="Mitochondrial outer membrane protein porin 3"
FT /id="PRO_0000050527"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CONFLICT 63
FT /note="N -> K (in Ref. 5; AAM62480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 29211 MW; 938E671BEB454275 CRC64;
MVKGPGLYTE IGKKARDLLY RDYQGDQKFS VTTYSSTGVA ITTTGTNKGS LFLGDVATQV
KNNNFTADVK VSTDSSLLTT LTFDEPAPGL KVIVQAKLPD HKSGKAEVQY FHDYAGISTS
VGFTATPIVN FSGVVGTNGL SLGTDVAYNT ESGNFKHFNA GFNFTKDDLT ASLILNDKGE
KLNASYYQIV SPSTVVGAEI SHNFTTKENA ITVGTQHALD PLTTVKARVN NAGVANALIQ
HEWRPKSFFT VSGEVDSKAI DKSAKVGIAL ALKP
