VDAC4_ARATH
ID VDAC4_ARATH Reviewed; 274 AA.
AC Q9FKM2;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Mitochondrial outer membrane protein porin 4;
DE AltName: Full=Voltage-dependent anion-selective channel protein 4;
DE Short=AtVDAC4;
DE Short=VDAC-4;
GN Name=VDAC4; OrderedLocusNames=At5g57490; ORFNames=MUA2.6;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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].
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
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 [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, GENE FAMILY, AND
RP DISRUPTION 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 [8]
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: 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 growth and development at the vegetative
CC and reproductive stages. Is important for leaf and pollen development
CC and mitochondrial membrane potential steady state. May be involved in
CC disease resistance. {ECO:0000250, ECO:0000269|PubMed:21705391}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:19326079,
CC ECO:0000269|PubMed:21705391}. Note=Also localized in other unidentified
CC cellular compartments.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21705391}.
CC -!- INDUCTION: By the bacterial pathogen P.syringae pv. tomato.
CC {ECO:0000269|PubMed:19326079}.
CC -!- DOMAIN: Consists mainly of membrane-spanning sided beta-sheets.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants with lesion mimic phenotype and
CC increased expression of the pathogenesis-related genes PR1, PR2 and
CC PR5. Delayed flowering, impaired development of anthers and short
CC siliques with sterile seeds. {ECO:0000269|PubMed:21705391}.
CC -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin (TC 1.B.8.1)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB011482; BAB08784.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96907.1; -; Genomic_DNA.
DR EMBL; AY034928; AAK59435.1; -; mRNA.
DR EMBL; AY059112; AAL15218.1; -; mRNA.
DR EMBL; AY086306; AAM64378.1; -; mRNA.
DR RefSeq; NP_200557.1; NM_125130.3.
DR AlphaFoldDB; Q9FKM2; -.
DR SMR; Q9FKM2; -.
DR STRING; 3702.AT5G57490.1; -.
DR iPTMnet; Q9FKM2; -.
DR SwissPalm; Q9FKM2; -.
DR PaxDb; Q9FKM2; -.
DR PRIDE; Q9FKM2; -.
DR ProteomicsDB; 228583; -.
DR DNASU; 835853; -.
DR EnsemblPlants; AT5G57490.1; AT5G57490.1; AT5G57490.
DR GeneID; 835853; -.
DR Gramene; AT5G57490.1; AT5G57490.1; AT5G57490.
DR KEGG; ath:AT5G57490; -.
DR Araport; AT5G57490; -.
DR TAIR; locus:2174517; AT5G57490.
DR eggNOG; KOG3126; Eukaryota.
DR HOGENOM; CLU_069937_0_0_1; -.
DR InParanoid; Q9FKM2; -.
DR OMA; PWSWRLN; -.
DR OrthoDB; 938262at2759; -.
DR PhylomeDB; Q9FKM2; -.
DR PRO; PR:Q9FKM2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKM2; baseline and differential.
DR Genevisible; Q9FKM2; AT.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA: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:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0008308; F:voltage-gated anion channel activity; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; 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.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Growth regulation; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein; Porin;
KW Reference proteome; Transmembrane; Transmembrane beta strand; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..274
FT /note="Mitochondrial outer membrane protein porin 4"
FT /id="PRO_0000414082"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SMX3"
SQ SEQUENCE 274 AA; 29505 MW; 20404992240902CF CRC64;
MGSSPAPFAD IGKKAKDLLN KDYIFDHKFT LTMLSATGTE FVATGLKKDD FFFGDISTLY
KGQNTIVDLK IDSHSSVSTK VTLKNLLPSA KAVISFKIPD HKSGKLDVQY VHPHATLNSS
IGLNPTPLLD LSATIGSQNV CLGGEVSFDT ASSSLTKYNA GIGFNNQGVS AALILEDKGE
SLRATYVHTV NPTTSFGAEL IRRFSNYNNS FTVGSSHSVD QFTVVKTRFS NSGKAGMVVQ
REWRPKSHIT FSAEYDSKAV TSSPKLGLAL ALKP
