VDAC1_MOUSE
ID VDAC1_MOUSE Reviewed; 296 AA.
AC Q60932; B1ASZ9; Q5SVC6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Voltage-dependent anion-selective channel protein 1;
DE Short=VDAC-1;
DE Short=mVDAC1;
DE AltName: Full=Outer mitochondrial membrane protein porin 1;
DE AltName: Full=Plasmalemmal porin;
DE AltName: Full=Voltage-dependent anion-selective channel protein 5;
DE Short=VDAC-5;
DE Short=mVDAC5;
GN Name=Vdac1; Synonyms=Vdac5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MT-VDAC1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8660977; DOI=10.1006/geno.1996.0193;
RA Sampson M.J., Lovell R.S., Craigen W.J.;
RT "Isolation, characterization, and mapping of two mouse mitochondrial
RT voltage-dependent anion channel isoforms.";
RL Genomics 33:283-288(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS MT-VDAC1 AND PL-VDAC1),
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10716730; DOI=10.1073/pnas.97.7.3201;
RA Buettner R., Papoutsoglou G., Scemes E., Spray D.C., Dermietzel R.;
RT "Evidence for secretory pathway localization of a voltage-dependent anion
RT channel isoform.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3201-3206(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MT-VDAC1).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Amnion, Embryonic kidney, Embryonic stomach, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MT-VDAC1).
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 34-41; 46-66; 77-106; 110-123; 134-174; 177-210;
RP 214-231; 238-279 AND 288-296, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP FUNCTION.
RX PubMed=15477379; DOI=10.1085/jgp.200409154;
RA Okada S.F., O'Neal W.K., Huang P., Nicholas R.A., Ostrowski L.E.,
RA Craigen W.J., Lazarowski E.R., Boucher R.C.;
RT "Voltage-dependent anion channel-1 (VDAC-1) contributes to ATP release and
RT cell volume regulation in murine cells.";
RL J. Gen. Physiol. 124:513-526(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32 AND SER-253, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-122 AND LYS-265, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [13]
RP INTERACTION WITH AMYLOID-BETA AND APP, AND SUBCELLULAR LOCATION.
RX PubMed=25168729; DOI=10.1016/j.neuroscience.2014.07.079;
RA Fernandez-Echevarria C., Diaz M., Ferrer I., Canerina-Amaro A., Marin R.;
RT "Abeta promotes VDAC1 channel dephosphorylation in neuronal lipid rafts.
RT Relevance to the mechanisms of neurotoxicity in Alzheimer's disease.";
RL Neuroscience 278:354-366(2014).
RN [14]
RP FUNCTION, UBIQUITINATION AT LYS-25; LYS-33; LYS-66; LYS-122; LYS-123 AND
RP LYS-287, AND MUTAGENESIS OF LYS-25; LYS-33; LYS-66; 122-LYS-LYS-123 AND
RP LYS-287.
RX PubMed=32047033; DOI=10.1073/pnas.1909814117;
RA Ham S.J., Lee D., Yoo H., Jun K., Shin H., Chung J.;
RT "Decision between mitophagy and apoptosis by Parkin via VDAC1
RT ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:4281-4291(2020).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 14-296, FUNCTION, AND TOPOLOGY.
RX PubMed=18988731; DOI=10.1073/pnas.0809634105;
RA Ujwal R., Cascio D., Colletier J.-P., Faham S., Zhang J., Toro L., Ping P.,
RA Abramson J.;
RT "The crystal structure of mouse VDAC1 at 2.3 A resolution reveals
RT mechanistic insights into metabolite gating.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17742-17747(2008).
CC -!- FUNCTION: Forms a channel through the mitochondrial outer membrane and
CC also the plasma membrane. The channel at the outer mitochondrial
CC membrane allows diffusion of small hydrophilic molecules; in the plasma
CC membrane it is involved in cell volume regulation and apoptosis. It
CC adopts an open conformation at low or zero membrane potential and a
CC closed conformation at potentials above 30-40 mV. The open state has a
CC weak anion selectivity whereas the closed state is cation-selective.
CC Binds various signaling molecules, including the sphingolipid ceramide,
CC the phospholipid phosphatidylcholine, and the sterol cholesterol (By
CC similarity). In depolarized mitochondria, acts downstream of PRKN and
CC PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by
CC PRKN promotes mitophagy, while monoubiquitination by PRKN decreases
CC mitochondrial calcium influx which ultimately inhibits apoptosis
CC (PubMed:32047033). May participate in the formation of the permeability
CC transition pore complex (PTPC) responsible for the release of
CC mitochondrial products that triggers apoptosis (PubMed:10716730,
CC PubMed:15477379, PubMed:18988731). May mediate ATP export from cells
CC (By similarity). {ECO:0000250|UniProtKB:P21796,
CC ECO:0000269|PubMed:10716730, ECO:0000269|PubMed:15477379,
CC ECO:0000269|PubMed:18988731, ECO:0000269|PubMed:32047033}.
CC -!- ACTIVITY REGULATION: Inhibited by nitric oxide.
CC {ECO:0000250|UniProtKB:P21796}.
CC -!- SUBUNIT: Homodimer and homotrimer; in response to cyclic AMP or calcium
CC (By similarity). Interacts with hexokinases including HK1. The HK1-
CC VDAC1 complex interacts with ATF2. Interacts with BCL2L1. Interacts
CC with BAK1. Interacts with RTL10/BOP (via BH3 domain) (By similarity).
CC Interacts with amyloid-beta and APP; induces VDAC1 dephosphorylation
CC (PubMed:25168729). Component of the mitochondrial permeability
CC transition pore complex (mPTPC), at least composed of SPG7, VDAC1 and
CC PPIF. Interacts with SPG7, NIPSNAP2 and SLC25A30 (By similarity).
CC Interacts with TMEM41B (By similarity). Interacts with BCAP31 (By
CC similarity). {ECO:0000250|UniProtKB:P21796,
CC ECO:0000269|PubMed:25168729}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mt-VDAC1]: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:10716730}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18988731}.
CC -!- SUBCELLULAR LOCATION: [Isoform Pl-VDAC1]: Cell membrane
CC {ECO:0000269|PubMed:10716730}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18988731}. Membrane raft
CC {ECO:0000269|PubMed:25168729}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18988731}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Pl-VDAC1;
CC IsoId=Q60932-1; Sequence=Displayed;
CC Name=Mt-VDAC1;
CC IsoId=Q60932-2; Sequence=VSP_005075;
CC -!- TISSUE SPECIFICITY: High levels of expression detected in heart,
CC kidney, brain, and skeletal muscle. Not expressed in testis.
CC {ECO:0000269|PubMed:8660977}.
CC -!- DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19
CC beta-strands. The helical N-terminus folds back into the pore opening
CC and plays a role in voltage-gated channel activity.
CC {ECO:0000250|UniProtKB:P21796}.
CC -!- PTM: Phosphorylation at Ser-206 by NEK1 promotes the open
CC conformational state preventing excessive mitochondrial membrane
CC permeability and subsequent apoptotic cell death after injury.
CC Phosphorylation by the AKT-GSK3B axis stabilizes the protein probably
CC by preventing ubiquitin-mediated proteasomal degradation.
CC {ECO:0000250|UniProtKB:P21796}.
CC -!- PTM: Ubiquitinated (PubMed:32047033). Undergoes monoubiquitination and
CC polyubiquitination by PRKN; monoubiquitination at Lys-287 inhibits
CC apoptosis, whereas polyubiquitination leads to its degradation and
CC promotes mitophagy (PubMed:32047033). Deubiquitinated by USP30 (By
CC similarity). {ECO:0000250|UniProtKB:P21796,
CC ECO:0000269|PubMed:32047033}.
CC -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC {ECO:0000305}.
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DR EMBL; U30840; AAB47777.1; -; mRNA.
DR EMBL; AK168672; BAE40522.1; -; mRNA.
DR EMBL; AK169671; BAE41292.1; -; mRNA.
DR EMBL; AK169354; BAE41103.1; -; mRNA.
DR EMBL; AK169282; BAE41040.1; -; mRNA.
DR EMBL; AK169160; BAE40939.1; -; mRNA.
DR EMBL; AL645589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC092257; AAH92257.1; -; mRNA.
DR CCDS; CCDS24671.1; -. [Q60932-2]
DR RefSeq; NP_035824.1; NM_011694.5. [Q60932-2]
DR PDB; 3EMN; X-ray; 2.30 A; X=14-296.
DR PDB; 4C69; X-ray; 2.28 A; X=14-296.
DR PDB; 7KUH; EM; 3.12 A; X=14-296.
DR PDBsum; 3EMN; -.
DR PDBsum; 4C69; -.
DR PDBsum; 7KUH; -.
DR AlphaFoldDB; Q60932; -.
DR BMRB; Q60932; -.
DR SMR; Q60932; -.
DR BioGRID; 204507; 35.
DR IntAct; Q60932; 45.
DR MINT; Q60932; -.
DR STRING; 10090.ENSMUSP00000099819; -.
DR iPTMnet; Q60932; -.
DR PhosphoSitePlus; Q60932; -.
DR SwissPalm; Q60932; -.
DR REPRODUCTION-2DPAGE; Q60932; -.
DR SWISS-2DPAGE; Q60932; -.
DR EPD; Q60932; -.
DR jPOST; Q60932; -.
DR MaxQB; Q60932; -.
DR PaxDb; Q60932; -.
DR PeptideAtlas; Q60932; -.
DR PRIDE; Q60932; -.
DR ProteomicsDB; 300195; -. [Q60932-1]
DR ProteomicsDB; 300196; -. [Q60932-2]
DR ABCD; Q60932; 1 sequenced antibody.
DR Antibodypedia; 3137; 745 antibodies from 47 providers.
DR DNASU; 22333; -.
DR Ensembl; ENSMUST00000020673; ENSMUSP00000020673; ENSMUSG00000020402. [Q60932-1]
DR Ensembl; ENSMUST00000102758; ENSMUSP00000099819; ENSMUSG00000020402. [Q60932-2]
DR GeneID; 22333; -.
DR KEGG; mmu:22333; -.
DR UCSC; uc007ivm.1; mouse. [Q60932-1]
DR CTD; 7416; -.
DR MGI; MGI:106919; Vdac1.
DR VEuPathDB; HostDB:ENSMUSG00000020402; -.
DR eggNOG; KOG3126; Eukaryota.
DR GeneTree; ENSGT00950000182869; -.
DR HOGENOM; CLU_044399_2_0_1; -.
DR InParanoid; Q60932; -.
DR OMA; IKTAYKC; -.
DR OrthoDB; 938262at2759; -.
DR PhylomeDB; Q60932; -.
DR TreeFam; TF315091; -.
DR Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-70268; Pyruvate metabolism.
DR BioGRID-ORCS; 22333; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Vdac1; mouse.
DR EvolutionaryTrace; Q60932; -.
DR PRO; PR:Q60932; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q60932; protein.
DR Bgee; ENSMUSG00000020402; Expressed in floor plate of midbrain and 250 other tissues.
DR ExpressionAtlas; Q60932; baseline and differential.
DR Genevisible; Q60932; MM.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005757; C:mitochondrial permeability transition pore complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0005253; F:anion channel activity; ISO:MGI.
DR GO; GO:0097001; F:ceramide binding; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0008308; F:voltage-gated anion channel activity; IDA:UniProtKB.
DR GO; GO:0006820; P:anion transport; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0110099; P:negative regulation of calcium import into the mitochondrion; ISO:MGI.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:MGI.
DR GO; GO:1905091; P:positive regulation of parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; ISO:MGI.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
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 InterPro; IPR030270; VDAC1.
DR PANTHER; PTHR11743; PTHR11743; 1.
DR PANTHER; PTHR11743:SF13; PTHR11743:SF13; 1.
DR Pfam; PF01459; Porin_3; 1.
DR PRINTS; PR00185; EUKARYTPORIN.
DR PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell membrane;
KW Direct protein sequencing; Ion transport; Isopeptide bond; Lipid-binding;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; NAD;
KW Nucleotide-binding; Phosphoprotein; Porin; Reference proteome;
KW Transmembrane; Transmembrane beta strand; Transport; Ubl conjugation.
FT CHAIN 1..296
FT /note="Voltage-dependent anion-selective channel protein 1"
FT /id="PRO_0000050500"
FT TRANSMEM 39..46
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 52..61
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 67..77
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 82..89
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 93..101
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 108..117
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 123..132
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 136..145
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 149..158
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 162..171
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 178..188
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 191..198
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 202..211
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 215..223
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 230..239
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 244..251
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 255..264
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 268..276
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT TRANSMEM 286..296
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18988731"
FT BINDING 255..257
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT BINDING 273..277
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT SITE 86
FT /note="Involved in ceramide and phosphatidylcholine
FT binding. Critical for channel structural stability and
FT gating"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2L0"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 33
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 80
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 122
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 206
FT /note="Phosphoserine; by NEK1"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 279
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:32047033"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:32047033"
FT CROSSLNK 66
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:32047033"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:32047033"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:32047033"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:32047033"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform Mt-VDAC1)"
FT /evidence="ECO:0000303|PubMed:10716730,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:8660977"
FT /id="VSP_005075"
FT MUTAGEN 25
FT /note="K->R: Decreased localization of SQSTM1/p62 to
FT damaged mitochondria; when associated with R-33; R-66 and
FT 122-R-R-123."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 33
FT /note="K->R: Decreased localization of SQSTM1/p62 to
FT damaged mitochondria; when associated with R-25; R-66 and
FT 122-R-R-123."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 66
FT /note="K->R: Decreased localization of SQSTM1/p62 to
FT damaged mitochondria; when associated with R-25; R-33 and
FT 122-R-R-123."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 122..123
FT /note="KK->RR: Decreased localization of SQSTM1/p62 to
FT damaged mitochondria; when associated with R-25; R-33 and
FT R-66."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 287
FT /note="K->R: No effect on localization of SQSTM1/p62 to
FT damaged mitochondria."
FT /evidence="ECO:0000269|PubMed:32047033"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:4C69"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 49..61
FT /evidence="ECO:0007829|PDB:4C69"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:4C69"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:7KUH"
FT STRAND 94..105
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:4C69"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:4C69"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 176..187
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 189..198
FT /evidence="ECO:0007829|PDB:4C69"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 202..212
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 230..241
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 254..265
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 268..277
FT /evidence="ECO:0007829|PDB:4C69"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4C69"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:4C69"
FT INIT_MET Q60932-2:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT MOD_RES Q60932-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 32351 MW; C0710C1717063B32 CRC64;
MCSFFLVLLL WQNMAVPPTY ADLGKSARDV FTKGYGFGLI KLDLKTKSEN GLEFTSSGSA
NTETTKVNGS LETKYRWTEY GLTFTEKWNT DNTLGTEITV EDQLARGLKL TFDSSFSPNT
GKKNAKIKTG YKREHINLGC DVDFDIAGPS IRGALVLGYE GWLAGYQMNF ETSKSRVTQS
NFAVGYKTDE FQLHTNVNDG TEFGGSIYQK VNKKLETAVN LAWTAGNSNT RFGIAAKYQV
DPDACFSAKV NNSSLIGLGY TQTLKPGIKL TLSALLDGKN VNAGGHKLGL GLEFQA
