VDAC_DROME
ID VDAC_DROME Reviewed; 282 AA.
AC Q94920; Q29QZ3; Q94997; Q9VKP1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Voltage-dependent anion-selective channel;
DE AltName: Full=DmVDAC;
DE AltName: Full=Porin;
GN Name=porin; Synonyms=POR-1, VDAC; ORFNames=CG6647;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=9271262; DOI=10.1016/s0005-2736(97)00059-x;
RA Ryerse J.S., Blachly-Dyson E., Forte M.A., Nagel B.;
RT "Cloning and molecular characterization of a voltage-dependent anion-
RT selective channel (VDAC) from Drosophila melanogaster.";
RL Biochim. Biophys. Acta 1327:204-212(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-10.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=8797793; DOI=10.1016/0014-5793(96)00268-2;
RA Messina A., Neri M., Perosa F., Caggese C., Marino M., Caizzi R.,
RA De Pinto V.;
RT "Cloning and chromosomal localization of a cDNA encoding a mitochondrial
RT porin from Drosophila melanogaster.";
RL FEBS Lett. 384:9-13(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Larva;
RX PubMed=9688565; DOI=10.1016/s0014-5793(98)00693-0;
RA Oliva M., Messina A., Ragone G., Caggese C., De Pinto V.;
RT "Sequence and expression pattern of the Drosophila melanogaster
RT mitochondrial porin gene: evidence of a conserved protein domain between
RT fly and mouse.";
RL FEBS Lett. 430:327-332(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Ovary;
RX PubMed=10071211; DOI=10.1007/s004380050942;
RA Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R.,
RA Barsanti P.;
RT "Identification of nuclear genes encoding mitochondrial proteins: isolation
RT of a collection of D. melanogaster cDNAs homologous to sequences in the
RT Human Gene Index database.";
RL Mol. Gen. Genet. 261:64-70(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, UBIQUITINATION AT LYS-11; LYS-19; LYS-52; LYS-109 AND LYS-273,
RP AND MUTAGENESIS OF LYS-11; LYS-19; LYS-52; LYS-109 AND LYS-273.
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).
CC -!- FUNCTION: Forms a channel through the mitochondrial outer membrane and
CC also the plasma membrane (By similarity). The channel at the outer
CC mitochondrial membrane allows diffusion of small hydrophilic molecules;
CC in the plasma membrane it is involved in cell volume regulation and
CC apoptosis (By similarity). It adopts an open conformation at low or
CC zero membrane potential and a closed conformation at potentials above
CC 30-40 mV (By similarity). The open state has a weak anion selectivity
CC whereas the closed state is cation-selective (By similarity). In
CC depolarized mitochondria, acts downstream of park to promote mitophagy
CC or prevent apoptosis; polyubiquitination by park promotes mitophagy,
CC while monoubiquitination by park decreases mitochondrial calcium influx
CC which ultimately inhibits apoptosis (PubMed:32047033).
CC {ECO:0000250|UniProtKB:P21796, ECO:0000269|PubMed:32047033}.
CC -!- SUBUNIT: Interacts with hexokinases. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, highest levels
CC are in embryos and pupae. {ECO:0000269|PubMed:9688565}.
CC -!- DOMAIN: Consists mainly of membrane-spanning sided beta-sheets.
CC -!- PTM: Ubiquitinated (PubMed:32047033). Undergoes monoubiquitination and
CC polyubiquitination by park; monoubiquitination at Lys-273 inhibits
CC apoptosis, whereas polyubiquitination at Lys-11, Lys-19, Lys-52 and
CC Lys-109 may promote mitophagy (PubMed:32047033).
CC {ECO:0000269|PubMed:32047033}.
CC -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC {ECO:0000305}.
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DR EMBL; U70314; AAC02635.1; -; mRNA.
DR EMBL; X92408; CAA63143.1; -; mRNA.
DR EMBL; X95692; CAA64988.1; -; mRNA.
DR EMBL; AJ000880; CAA04370.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53022.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10766.1; -; Genomic_DNA.
DR EMBL; AE014134; ABC65894.1; -; Genomic_DNA.
DR EMBL; AY070509; AAL47980.1; -; mRNA.
DR EMBL; BT024247; ABC86309.1; -; mRNA.
DR RefSeq; NP_001033899.1; NM_001038810.2.
DR RefSeq; NP_001245961.1; NM_001259032.1.
DR RefSeq; NP_001260365.1; NM_001273436.1.
DR RefSeq; NP_476813.1; NM_057465.4.
DR RefSeq; NP_599110.1; NM_134283.2.
DR AlphaFoldDB; Q94920; -.
DR SMR; Q94920; -.
DR BioGRID; 60572; 77.
DR DIP; DIP-17501N; -.
DR IntAct; Q94920; 5.
DR MINT; Q94920; -.
DR STRING; 7227.FBpp0079772; -.
DR TCDB; 1.B.8.1.6; the mitochondrial and plastid porin (mpp) family.
DR PaxDb; Q94920; -.
DR PRIDE; Q94920; -.
DR DNASU; 34500; -.
DR EnsemblMetazoa; FBtr0080182; FBpp0079771; FBgn0004363.
DR EnsemblMetazoa; FBtr0080183; FBpp0079772; FBgn0004363.
DR EnsemblMetazoa; FBtr0100584; FBpp0100039; FBgn0004363.
DR EnsemblMetazoa; FBtr0305260; FBpp0293784; FBgn0004363.
DR EnsemblMetazoa; FBtr0332029; FBpp0304343; FBgn0004363.
DR GeneID; 34500; -.
DR KEGG; dme:Dmel_CG6647; -.
DR CTD; 34500; -.
DR FlyBase; FBgn0004363; porin.
DR VEuPathDB; VectorBase:FBgn0004363; -.
DR eggNOG; KOG3126; Eukaryota.
DR GeneTree; ENSGT00950000182869; -.
DR HOGENOM; CLU_044399_2_0_1; -.
DR InParanoid; Q94920; -.
DR OMA; ITLTEKW; -.
DR OrthoDB; 938262at2759; -.
DR PhylomeDB; Q94920; -.
DR Reactome; R-DME-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-70268; Pyruvate metabolism.
DR SignaLink; Q94920; -.
DR BioGRID-ORCS; 34500; 1 hit in 3 CRISPR screens.
DR ChiTaRS; porin; fly.
DR GenomeRNAi; 34500; -.
DR PRO; PR:Q94920; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004363; Expressed in second segment of antenna (Drosophila) and 67 other tissues.
DR ExpressionAtlas; Q94920; baseline and differential.
DR Genevisible; Q94920; DM.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0016006; C:Nebenkern; IDA:FlyBase.
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; IDA:FlyBase.
DR GO; GO:0006811; P:ion transport; IDA:FlyBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0110099; P:negative regulation of calcium import into the mitochondrion; IMP:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0030382; P:sperm mitochondrion organization; IMP:FlyBase.
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; IPR030277; VDAC2.
DR PANTHER; PTHR11743; PTHR11743; 1.
DR PANTHER; PTHR11743:SF12; PTHR11743:SF12; 1.
DR Pfam; PF01459; Porin_3; 1.
DR PRINTS; PR00185; EUKARYTPORIN.
DR PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Ion transport; Isopeptide bond; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Porin; Reference proteome;
KW Transmembrane; Transmembrane beta strand; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8797793"
FT CHAIN 2..282
FT /note="Voltage-dependent anion-selective channel"
FT /id="PRO_0000050520"
FT SITE 72
FT /note="Involved in hexokinase binding"
FT /evidence="ECO:0000250"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:32047033"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:32047033"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:32047033"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:32047033"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 11
FT /note="K->R: Poly-KR; increase in apoptosis when
FT overexpressed in muscle cells, resulting in wing posture
FT abnormalities; when associated with R-19, R-52 and R-109."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 19
FT /note="K->R: Poly-KR; increase in apoptosis when
FT overexpressed in muscle cells, resulting in wing posture
FT abnormalities; when associated with R-11, R-52 and R-109."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 52
FT /note="K->R: Poly-KR; increase in apoptosis when
FT overexpressed in muscle cells, resulting in wing posture
FT abnormalities; when associated with R-11, R-19 and R-109."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 109
FT /note="K->R: Poly-KR; increase in apoptosis when
FT overexpressed in muscle cells, resulting in wing posture
FT abnormalities; when associated with R-11, R-19 and R-52."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 273
FT /note="K->R: Significant increase in apoptosis when
FT overexpressed in muscle cells, resulting in severe wing
FT posture abnormalities and impaired climbing ability."
FT /evidence="ECO:0000269|PubMed:32047033"
FT CONFLICT 231
FT /note="S -> R (in Ref. 2; CAA63143 and 3; CAA64988)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="D -> T (in Ref. 2; CAA63143 and 3; CAA64988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 30550 MW; 173E165C3A2D297D CRC64;
MAPPSYSDLG KQARDIFSKG YNFGLWKLDL KTKTSSGIEF NTAGHSNQES GKVFGSLETK
YKVKDYGLTL TEKWNTDNTL FTEVAVQDQL LEGLKLSLEG NFAPQSGNKN GKFKVAYGHE
NVKADSDVNI DLKGPLINAS AVLGYQGWLA GYQTAFDTQQ SKLTTNNFAL GYTTKDFVLH
TAVNDGQEFS GSIFQRTSDK LDVGVQLSWA SGTSNTKFAI GAKYQLDDDA SVRAKVNNAS
QVGLGYQQKL RDGVTLTLST LVDGKNFNAG GHKIGVGLEL EA
