VDAC1_HUMAN
ID VDAC1_HUMAN Reviewed; 283 AA.
AC P21796; B3KVK4; D3DQ93; Q5FVE7; Q9UIQ5; Q9UPL0;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 234.
DE RecName: Full=Voltage-dependent anion-selective channel protein 1;
DE Short=VDAC-1;
DE Short=hVDAC1;
DE AltName: Full=Outer mitochondrial membrane protein porin 1;
DE AltName: Full=Plasmalemmal porin;
DE AltName: Full=Porin 31HL;
DE AltName: Full=Porin 31HM;
GN Name=VDAC1; Synonyms=VDAC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=8420959; DOI=10.1016/s0021-9258(18)53930-2;
RA Blachly-Dyson E., Zambronicz E.B., Yu W.H., Adams V., McCabe E.R.,
RA Adelman J.P., Colombini M., Forte M.A.;
RT "Cloning and functional expression in yeast of two human isoforms of the
RT outer mitochondrial membrane channel, the voltage-dependent anion
RT channel.";
RL J. Biol. Chem. 268:1835-1841(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RA Blachly-Dyson E., Forte M.A.;
RT "Cloning of human VDAC cDNA.";
RL Biophys. J. 59:216A-216A(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10501981; DOI=10.1007/s003359901158;
RA Decker W.K., Bowles K.R., Schatte E.C., Towbin J.A., Craigen W.J.;
RT "Revised fine mapping of the human voltage-dependent anion channel loci by
RT radiation hybrid analysis.";
RL Mamm. Genome 10:1041-1042(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10772903; DOI=10.1006/bbrc.2000.2487;
RA Messina A., Guarino F., Oliva M., van den Heuvel L.P., Smeitink J.,
RA De Pinto V.;
RT "Characterization of the human porin isoform 1 (HVDAC1) gene by
RT amplification on the whole human genome: a tool for porin deficiency
RT analysis.";
RL Biochem. Biophys. Res. Commun. 270:787-792(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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 [9]
RP PROTEIN SEQUENCE OF 2-283.
RC TISSUE=Lymphocyte;
RX PubMed=2559745;
RA Kayser H., Kratzin H.D., Thinnes F.P., Goetz H., Schmidt W.E., Eckart K.,
RA Hilschmann N.;
RT "Identification of human porins. II. Characterization and primary structure
RT of a 31-lDa porin from human B lymphocytes (Porin 31HL).";
RL Biol. Chem. Hoppe-Seyler 370:1265-1278(1989).
RN [10]
RP PROTEIN SEQUENCE OF 2-283.
RC TISSUE=Skeletal muscle;
RX PubMed=1657034; DOI=10.1515/bchm3.1991.372.2.455;
RA Juergens L., Ilsemann P., Kratzin H.D., Hesse D., Eckart K., Thinnes F.P.,
RA Hilschmann N.;
RT "Studies on human porin. IV. The primary structures of 'Porin 31HM'
RT purified from human skeletal muscle membranes and of 'Porin 31HL' derived
RT from human B lymphocyte membranes are identical.";
RL Biol. Chem. Hoppe-Seyler 372:455-463(1991).
RN [11]
RP PROTEIN SEQUENCE OF 2-283.
RC TISSUE=B-cell;
RA Hein A., Kiafard Z., Hesse D., Hesse J.-O., Zimmermann B., Kratzin H.D.,
RA Schulz H., Reiss J., Thinnes F.P., Goetz H., Hilschmann N.;
RL Submitted (DEC-1997) to UniProtKB.
RN [12]
RP PROTEIN SEQUENCE OF 2-12; 21-61; 64-74; 94-110; 121-139; 162-174; 225-236
RP AND 257-274, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [13]
RP PROTEIN SEQUENCE OF 75-93; 175-197 AND 201-218, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [14]
RP MUTAGENESIS.
RX PubMed=7685903; DOI=10.1073/pnas.90.12.5446;
RA Thomas L., Blachly-Dyson E., Colombini M., Forte M.A.;
RT "Mapping of residues forming the voltage sensor of the voltage-dependent
RT anion-selective channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5446-5449(1993).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=7539795; DOI=10.1074/jbc.270.23.13998;
RA Yu W.H., Wolfgang W., Forte M.A.;
RT "Subcellular localization of human voltage-dependent anion channel
RT isoforms.";
RL J. Biol. Chem. 270:13998-14006(1995).
RN [16]
RP CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=10661876; DOI=10.1515/bc.1999.189;
RA Stadtmueller U., Eben-Brunnen J., Schmid A., Hesse D., Klebert S.,
RA Kratzin H.D., Hesse J., Zimmermann B., Reymann S., Thinnes F.P., Benz R.,
RA Goetz H., Hilschmann N.;
RT "Mitochondria-derived and extra-mitochondrial human type-1 porin are
RT identical as revealed by amino acid sequencing and electrophysiological
RT characterisation.";
RL Biol. Chem. 380:1461-1466(1999).
RN [17]
RP FUNCTION.
RX PubMed=11845315; DOI=10.1007/s004240100656;
RA Thinnes F.P., Walter G., Hellmann K.P., Hellmann T., Merker R., Kiafard Z.,
RA Eben-Brunnen J., Schwarzer C., Goetz H., Hilschmann N.;
RT "Gadolinium as an opener of the outwardly rectifying Cl(-) channel (ORCC).
RT Is there relevance for cystic fibrosis therapy?";
RL Pflugers Arch. 443:S111-S116(2001).
RN [18]
RP FUNCTION IN APOPTOSIS.
RX PubMed=15033708; DOI=10.1196/annals.1299.022;
RA Verrier F., Mignotte B., Jan G., Brenner C.;
RT "Study of PTPC composition during apoptosis for identification of viral
RT protein target.";
RL Ann. N. Y. Acad. Sci. 1010:126-142(2003).
RN [19]
RP INTERACTION WITH INFLUENZA A VIRUS PB1-F2.
RX PubMed=16201016; DOI=10.1371/journal.ppat.0010004;
RA Zamarin D., Garcia-Sastre A., Xiao X., Wang R., Palese P.;
RT "Influenza virus PB1-F2 protein induces cell death through mitochondrial
RT ANT3 and VDAC1.";
RL PLoS Pathog. 1:40-54(2005).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-20 AND LYS-266, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [26]
RP FUNCTION, PHOSPHORYLATION AT SER-193, AND MUTAGENESIS OF SER-193.
RX PubMed=20230784; DOI=10.1016/j.bbrc.2010.03.077;
RA Chen Y., Gaczynska M., Osmulski P., Polci R., Riley D.J.;
RT "Phosphorylation by Nek1 regulates opening and closing of voltage dependent
RT anion channel 1.";
RL Biochem. Biophys. Res. Commun. 394:798-803(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [30]
RP INTERACTION WITH ATF2 AND HK1.
RX PubMed=22304920; DOI=10.1016/j.cell.2012.01.016;
RA Lau E., Kluger H., Varsano T., Lee K., Scheffler I., Rimm D.L., Ideker T.,
RA Ronai Z.A.;
RT "PKCepsilon promotes oncogenic functions of ATF2 in the nucleus while
RT blocking its apoptotic function at mitochondria.";
RL Cell 148:543-555(2012).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [33]
RP INTERACTION WITH RTL10/BOP.
RX PubMed=23055042; DOI=10.1007/s13238-012-2069-7;
RA Zhang X., Weng C., Li Y., Wang X., Jiang C., Li X., Xu Y., Chen Q., Pan L.,
RA Tang H.;
RT "Human Bop is a novel BH3-only member of the Bcl-2 protein family.";
RL Protein Cell 3:790-801(2012).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107 AND SER-240, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [36]
RP IDENTIFICATION IN THE MITOCHONDRIAL PERMEABILITY TRANSITION PORE COMPLEX,
RP AND INTERACTION WITH SPG7; NIPSNAP2 AND SLC25A30.
RX PubMed=26387735; DOI=10.1016/j.molcel.2015.08.009;
RA Shanmughapriya S., Rajan S., Hoffman N.E., Higgins A.M., Tomar D.,
RA Nemani N., Hines K.J., Smith D.J., Eguchi A., Vallem S., Shaikh F.,
RA Cheung M., Leonard N.J., Stolakis R.S., Wolfers M.P., Ibetti J.,
RA Chuprun J.K., Jog N.R., Houser S.R., Koch W.J., Elrod J.W., Madesh M.;
RT "SPG7 is an essential and conserved component of the mitochondrial
RT permeability transition pore.";
RL Mol. Cell 60:47-62(2015).
RN [37]
RP UBIQUITINATION AT LYS-53; LYS-61; LYS-109; LYS-110; LYS-161; LYS-266 AND
RP LYS-274.
RX PubMed=25621951; DOI=10.1038/ncb3097;
RA Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
RA Kirkpatrick D.S., Bingol B., Corn J.E.;
RT "USP30 and parkin homeostatically regulate atypical ubiquitin chains on
RT mitochondria.";
RL Nat. Cell Biol. 17:160-169(2015).
RN [38]
RP ACTIVITY REGULATION.
RX PubMed=21156174; DOI=10.1016/j.febslet.2010.12.008;
RA Cheng Q., Sedlic F., Pravdic D., Bosnjak Z.J., Kwok W.M.;
RT "Biphasic effect of nitric oxide on the cardiac voltage-dependent anion
RT channel.";
RL FEBS Lett. 585:328-334(2011).
RN [39]
RP FUNCTION, INTERACTION WITH BAK1 AND BCL2L1, AND SUBCELLULAR LOCATION.
RX PubMed=25296756; DOI=10.1074/jbc.m114.567792;
RA Li L., Yao Y.C., Gu X.Q., Che D., Ma C.Q., Dai Z.Y., Li C., Zhou T.,
RA Cai W.B., Yang Z.H., Yang X., Gao G.Q.;
RT "Plasminogen kringle 5 induces endothelial cell apoptosis by triggering a
RT voltage-dependent anion channel 1 (VDAC1) positive feedback loop.";
RL J. Biol. Chem. 289:32628-32638(2014).
RN [40]
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 [41]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [42]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=27641616; DOI=10.1038/srep33516;
RA Marginedas-Freixa I., Hattab C., Bouyer G., Halle F., Chene A.,
RA Lefevre S.D., Cambot M., Cueff A., Schmitt M., Gamain B., Lacapere J.J.,
RA Egee S., Bihel F., Le Van Kim C., Ostuni M.A.;
RT "TSPO ligands stimulate ZnPPIX transport and ROS accumulation leading to
RT the inhibition of P. falciparum growth in human blood.";
RL Sci. Rep. 6:33516-33516(2016).
RN [43]
RP INTERACTION WITH TMEM41B.
RX PubMed=30352685; DOI=10.1016/j.bbrc.2018.10.073;
RA Van Alstyne M., Lotti F., Dal Mas A., Area-Gomez E., Pellizzoni L.;
RT "Stasimon/Tmem41b localizes to mitochondria-associated ER membranes and is
RT essential for mouse embryonic development.";
RL Biochem. Biophys. Res. Commun. 506:463-470(2018).
RN [44]
RP FUNCTION, AND SUBUNIT.
RX PubMed=30061676; DOI=10.1038/s41598-018-29885-7;
RA Marginedas-Freixa I., Alvarez C.L., Moras M., Leal Denis M.F., Hattab C.,
RA Halle F., Bihel F., Mouro-Chanteloup I., Lefevre S.D., Le Van Kim C.,
RA Schwarzbaum P.J., Ostuni M.A.;
RT "Human erythrocytes release ATP by a novel pathway involving VDAC
RT oligomerization independent of pannexin-1.";
RL Sci. Rep. 8:11384-11384(2018).
RN [45]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP MUTAGENESIS OF GLU-73.
RX PubMed=31015432; DOI=10.1038/s41467-019-09654-4;
RA Dadsena S., Bockelmann S., Mina J.G.M., Hassan D.G., Korneev S.,
RA Razzera G., Jahn H., Niekamp P., Mueller D., Schneider M., Tafesse F.G.,
RA Marrink S.J., Melo M.N., Holthuis J.C.M.;
RT "Ceramides bind VDAC2 to trigger mitochondrial apoptosis.";
RL Nat. Commun. 10:1832-1832(2019).
RN [46]
RP INTERACTION WITH BCAP31, AND SUBCELLULAR LOCATION.
RX PubMed=31206022; DOI=10.1126/sciadv.aaw1386;
RA Namba T.;
RT "BAP31 regulates mitochondrial function via interaction with Tom40 within
RT ER-mitochondria contact sites.";
RL Sci. Adv. 5:eaaw1386-eaaw1386(2019).
RN [47]
RP FUNCTION, UBIQUITINATION AT LYS-12; LYS-20; LYS-53; LYS-109; LYS-110 AND
RP LYS-274, AND MUTAGENESIS OF LYS-12; LYS-20; LYS-53; 109-LYS-LYS-110 AND
RP LYS-274.
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 [48]
RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF 2-283, AND STRUCTURE BY NMR.
RX PubMed=18832158; DOI=10.1073/pnas.0808115105;
RA Bayrhuber M., Meins T., Habeck M., Becker S., Giller K., Villinger S.,
RA Vonrhein C., Griesinger C., Zweckstetter M., Zeth K.;
RT "Structure of the human voltage-dependent anion channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15370-15375(2008).
RN [49]
RP STRUCTURE BY NMR, FUNCTION, INTERACTION WITH BCL2L1, AND NADH-BINDING.
RX PubMed=18755977; DOI=10.1126/science.1161302;
RA Hiller S., Garces R.G., Malia T.J., Orekhov V.Y., Colombini M., Wagner G.;
RT "Solution structure of the integral human membrane protein VDAC-1 in
RT detergent micelles.";
RL Science 321:1206-1210(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 (PubMed:11845315, PubMed:18755977, PubMed:20230784, PubMed:8420959).
CC Binds various signaling molecules, including the sphingolipid ceramide,
CC the phospholipid phosphatidylcholine, and the sterol cholesterol
CC (PubMed:31015432). In depolarized mitochondria, acts downstream of PRKN
CC and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination
CC by 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:15033708,
CC PubMed:25296756). May mediate ATP export from cells (PubMed:30061676).
CC {ECO:0000269|PubMed:11845315, ECO:0000269|PubMed:15033708,
CC ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:20230784,
CC ECO:0000269|PubMed:25296756, ECO:0000269|PubMed:30061676,
CC ECO:0000269|PubMed:31015432, ECO:0000269|PubMed:32047033,
CC ECO:0000269|PubMed:8420959}.
CC -!- ACTIVITY REGULATION: Inhibited by nitric oxide.
CC {ECO:0000269|PubMed:21156174}.
CC -!- SUBUNIT: Homodimer and homotrimer; in response to cyclic AMP or calcium
CC (PubMed:30061676). Interacts with hexokinases including HK1
CC (PubMed:8420959, PubMed:22304920). The HK1-VDAC1 complex interacts with
CC ATF2 (PubMed:22304920). Interacts with BCL2L1 (PubMed:18755977,
CC PubMed:25296756). Interacts with BAK1 (PubMed:25296756). Interacts with
CC RTL10/BOP (via BH3 domain) (PubMed:23055042). Interacts with amyloid-
CC beta and APP; induces VDAC1 dephosphorylation (PubMed:25168729).
CC Component of the mitochondrial permeability transition pore complex
CC (mPTPC), at least composed of SPG7, VDAC1 and PPIF (PubMed:26387735).
CC Interacts with SPG7, NIPSNAP2 and SLC25A30 (PubMed:26387735). Interacts
CC with TMEM41B (PubMed:30352685). Interacts with BCAP31
CC (PubMed:31206022). {ECO:0000269|PubMed:18755977,
CC ECO:0000269|PubMed:22304920, ECO:0000269|PubMed:23055042,
CC ECO:0000269|PubMed:25168729, ECO:0000269|PubMed:25296756,
CC ECO:0000269|PubMed:26387735, ECO:0000269|PubMed:30061676,
CC ECO:0000269|PubMed:30352685, ECO:0000269|PubMed:31206022,
CC ECO:0000269|PubMed:8420959}.
CC -!- SUBUNIT: (Microbial infection) Interacts with influenza A virus PB1-F2
CC protein. {ECO:0000269|PubMed:16201016}.
CC -!- INTERACTION:
CC P21796; P06493: CDK1; NbExp=3; IntAct=EBI-354158, EBI-444308;
CC P21796; P19367: HK1; NbExp=2; IntAct=EBI-354158, EBI-713162;
CC P21796; Q5S007: LRRK2; NbExp=3; IntAct=EBI-354158, EBI-5323863;
CC P21796; P30041: PRDX6; NbExp=3; IntAct=EBI-354158, EBI-2255129;
CC P21796; Q7L3V2: RTL10; NbExp=2; IntAct=EBI-354158, EBI-10697720;
CC P21796; P12236: SLC25A6; NbExp=4; IntAct=EBI-354158, EBI-356254;
CC P21796; P21796: VDAC1; NbExp=4; IntAct=EBI-354158, EBI-354158;
CC P21796; P45880: VDAC2; NbExp=5; IntAct=EBI-354158, EBI-354022;
CC P21796; Q9Y277: VDAC3; NbExp=2; IntAct=EBI-354158, EBI-354196;
CC P21796; P62258: YWHAE; NbExp=5; IntAct=EBI-354158, EBI-356498;
CC P21796; P0C0U1: PB1; Xeno; NbExp=4; IntAct=EBI-354158, EBI-12579807;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:31015432, ECO:0000269|PubMed:31206022,
CC ECO:0000269|PubMed:7539795}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158,
CC ECO:0000269|PubMed:27641616}. Cell membrane
CC {ECO:0000269|PubMed:25168729, ECO:0000269|PubMed:25296756}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:18755977,
CC ECO:0000269|PubMed:18832158}. Membrane raft
CC {ECO:0000269|PubMed:25168729}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158}.
CC -!- TISSUE SPECIFICITY: Expressed in erythrocytes (at protein level)
CC (PubMed:27641616). Expressed in heart, liver and skeletal muscle
CC (PubMed:8420959). {ECO:0000269|PubMed:27641616,
CC ECO:0000269|PubMed:8420959}.
CC -!- DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19
CC beta-strands (PubMed:18832158, PubMed:18755977). The helical N-terminus
CC folds back into the pore opening and plays a role in voltage-gated
CC channel activity (PubMed:18832158, PubMed:18755977).
CC {ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158}.
CC -!- PTM: Phosphorylation at Ser-193 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:0000269|PubMed:20230784}.
CC -!- PTM: Ubiquitinated (PubMed:25621951, PubMed:32047033). Undergoes
CC monoubiquitination and polyubiquitination by PRKN; monoubiquitination
CC at Lys-274 inhibits apoptosis, whereas polyubiquitination leads to its
CC degradation and promotes mitophagy (PubMed:25621951, PubMed:32047033).
CC Deubiquitinated by USP30 (PubMed:25621951).
CC {ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:32047033}.
CC -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/VDAC1ID50902ch5q31.html";
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DR EMBL; L06132; AAA61272.1; -; mRNA.
DR EMBL; AJ250032; CAB58127.1; -; Genomic_DNA.
DR EMBL; AJ250033; CAB58127.1; JOINED; Genomic_DNA.
DR EMBL; AJ250034; CAB58127.1; JOINED; Genomic_DNA.
DR EMBL; AJ250035; CAB58127.1; JOINED; Genomic_DNA.
DR EMBL; AJ250036; CAB58127.1; JOINED; Genomic_DNA.
DR EMBL; AJ250037; CAB58127.1; JOINED; Genomic_DNA.
DR EMBL; AJ250038; CAB58127.1; JOINED; Genomic_DNA.
DR EMBL; AJ250039; CAB58127.1; JOINED; Genomic_DNA.
DR EMBL; AF151097; AAD54939.1; -; Genomic_DNA.
DR EMBL; AF151093; AAD54939.1; JOINED; Genomic_DNA.
DR EMBL; AF151094; AAD54939.1; JOINED; Genomic_DNA.
DR EMBL; AF151095; AAD54939.1; JOINED; Genomic_DNA.
DR EMBL; AF151096; AAD54939.1; JOINED; Genomic_DNA.
DR EMBL; AC005200; AAC24723.1; -; Genomic_DNA.
DR EMBL; AK122953; BAG53816.1; -; mRNA.
DR EMBL; AC008608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62281.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62282.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62283.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62285.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62286.1; -; Genomic_DNA.
DR EMBL; BC008482; AAH08482.1; -; mRNA.
DR EMBL; BC071168; AAH71168.1; -; mRNA.
DR EMBL; BC090042; AAH90042.1; -; mRNA.
DR CCDS; CCDS4168.1; -.
DR PIR; A44422; MMHUP3.
DR RefSeq; NP_003365.1; NM_003374.2.
DR RefSeq; XP_005272132.1; XM_005272075.3.
DR RefSeq; XP_016865310.1; XM_017009821.1.
DR RefSeq; XP_016865311.1; XM_017009822.1.
DR RefSeq; XP_016865312.1; XM_017009823.1.
DR PDB; 2JK4; X-ray; 4.10 A; A=2-283.
DR PDB; 2K4T; NMR; -; A=1-283.
DR PDB; 5JDP; NMR; -; A=2-283.
DR PDB; 5XDN; X-ray; 3.15 A; A/B=1-283.
DR PDB; 5XDO; X-ray; 3.10 A; A/B=1-283.
DR PDB; 6G6U; X-ray; 2.74 A; A/B=1-283.
DR PDB; 6G73; X-ray; 3.27 A; A/B/C/D=1-283.
DR PDB; 6TIQ; NMR; -; A=1-283.
DR PDB; 6TIR; NMR; -; A=1-283.
DR PDB; 7QI2; NMR; -; A=1-283.
DR PDBsum; 2JK4; -.
DR PDBsum; 2K4T; -.
DR PDBsum; 5JDP; -.
DR PDBsum; 5XDN; -.
DR PDBsum; 5XDO; -.
DR PDBsum; 6G6U; -.
DR PDBsum; 6G73; -.
DR PDBsum; 6TIQ; -.
DR PDBsum; 6TIR; -.
DR PDBsum; 7QI2; -.
DR AlphaFoldDB; P21796; -.
DR BMRB; P21796; -.
DR SMR; P21796; -.
DR BioGRID; 113259; 463.
DR CORUM; P21796; -.
DR DIP; DIP-32862N; -.
DR IntAct; P21796; 254.
DR MINT; P21796; -.
DR STRING; 9606.ENSP00000265333; -.
DR ChEMBL; CHEMBL4295729; -.
DR DrugBank; DB01375; Aluminium monostearate.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB14011; Nabiximols.
DR CarbonylDB; P21796; -.
DR GlyGen; P21796; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P21796; -.
DR PhosphoSitePlus; P21796; -.
DR SwissPalm; P21796; -.
DR BioMuta; VDAC1; -.
DR DMDM; 130683; -.
DR DOSAC-COBS-2DPAGE; P21796; -.
DR OGP; P21796; -.
DR REPRODUCTION-2DPAGE; IPI00216308; -.
DR REPRODUCTION-2DPAGE; P21796; -.
DR UCD-2DPAGE; P21796; -.
DR EPD; P21796; -.
DR jPOST; P21796; -.
DR MassIVE; P21796; -.
DR MaxQB; P21796; -.
DR PaxDb; P21796; -.
DR PeptideAtlas; P21796; -.
DR PRIDE; P21796; -.
DR ProteomicsDB; 53904; -.
DR TopDownProteomics; P21796; -.
DR ABCD; P21796; 1 sequenced antibody.
DR Antibodypedia; 3137; 745 antibodies from 47 providers.
DR DNASU; 7416; -.
DR Ensembl; ENST00000265333.8; ENSP00000265333.3; ENSG00000213585.11.
DR Ensembl; ENST00000395044.7; ENSP00000378484.3; ENSG00000213585.11.
DR Ensembl; ENST00000395047.6; ENSP00000378487.2; ENSG00000213585.11.
DR GeneID; 7416; -.
DR KEGG; hsa:7416; -.
DR MANE-Select; ENST00000265333.8; ENSP00000265333.3; NM_003374.3; NP_003365.1.
DR UCSC; uc003kyp.3; human.
DR CTD; 7416; -.
DR DisGeNET; 7416; -.
DR GeneCards; VDAC1; -.
DR HGNC; HGNC:12669; VDAC1.
DR HPA; ENSG00000213585; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 604492; gene+phenotype.
DR neXtProt; NX_P21796; -.
DR OpenTargets; ENSG00000213585; -.
DR PharmGKB; PA37292; -.
DR VEuPathDB; HostDB:ENSG00000213585; -.
DR eggNOG; KOG3126; Eukaryota.
DR GeneTree; ENSGT00950000182869; -.
DR HOGENOM; CLU_044399_2_0_1; -.
DR InParanoid; P21796; -.
DR OMA; IKTAYKC; -.
DR OrthoDB; 938262at2759; -.
DR PhylomeDB; P21796; -.
DR TreeFam; TF315091; -.
DR PathwayCommons; P21796; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-70268; Pyruvate metabolism.
DR Reactome; R-HSA-8949215; Mitochondrial calcium ion transport.
DR SignaLink; P21796; -.
DR SIGNOR; P21796; -.
DR BioGRID-ORCS; 7416; 251 hits in 1073 CRISPR screens.
DR ChiTaRS; VDAC1; human.
DR EvolutionaryTrace; P21796; -.
DR GeneWiki; VDAC1; -.
DR GenomeRNAi; 7416; -.
DR Pharos; P21796; Tbio.
DR PRO; PR:P21796; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P21796; protein.
DR Bgee; ENSG00000213585; Expressed in biceps brachii and 201 other tissues.
DR ExpressionAtlas; P21796; baseline and differential.
DR Genevisible; P21796; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005757; C:mitochondrial permeability transition pore complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046930; C:pore complex; TAS:HGNC-UCL.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0097001; F:ceramide binding; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:UniProtKB.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0008308; F:voltage-gated anion channel activity; IDA:UniProtKB.
DR GO; GO:0006820; P:anion transport; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
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:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; IEA:Ensembl.
DR GO; GO:1905091; P:positive regulation of parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; IMP:UniProtKB.
DR GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; NAS: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; Apoptosis; Cell membrane;
KW Direct protein sequencing; Host-virus interaction; Ion transport;
KW Isopeptide bond; Lipid-binding; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Porin; Reference proteome;
KW Transmembrane; Transmembrane beta strand; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1657034,
FT ECO:0000269|PubMed:2559745, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..283
FT /note="Voltage-dependent anion-selective channel protein 1"
FT /id="PRO_0000050499"
FT TRANSMEM 26..35
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 39..47
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 54..64
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 69..76
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 80..89
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 95..104
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 111..120
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 123..130
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 137..145
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 150..158
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 163..175
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 178..185
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 189..198
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 202..211
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 218..227
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 231..238
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 242..251
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 254..263
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT TRANSMEM 273..282
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18755977,
FT ECO:0000269|PubMed:18832158"
FT BINDING 242..244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:18755977"
FT BINDING 260..264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:18755977"
FT SITE 73
FT /note="Involved in ceramide and phosphatidylcholine
FT binding. Critical for channel structural stability and
FT gating"
FT /evidence="ECO:0000269|PubMed:31015432,
FT ECO:0000305|PubMed:18832158"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2559745, ECO:0000269|Ref.12,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2L0"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT MOD_RES 20
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 20
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 109
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT MOD_RES 193
FT /note="Phosphoserine; by NEK1"
FT /evidence="ECO:0000269|PubMed:20230784"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT MOD_RES 266
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:32047033"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:32047033"
FT CROSSLNK 53
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951,
FT ECO:0000269|PubMed:32047033"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:25621951,
FT ECO:0000269|PubMed:32047033"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951,
FT ECO:0000269|PubMed:32047033"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951,
FT ECO:0000269|PubMed:32047033"
FT MUTAGEN 12
FT /note="K->R: PRKN-dependent polybiquitination is decreased,
FT whereas PRKN-dependent monoubiquitination, mitochondrial
FT calcium uptake and apoptosis are unaffected; when
FT associated with R-20; R-53 and 109-R-R-110."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 20
FT /note="K->R: PRKN-dependent polybiquitination is decreased,
FT whereas PRKN-dependent monoubiquitination, mitochondrial
FT calcium uptake and apoptosis are unaffected; when
FT associated with R-12; R-53 and 109-R-R-110."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 53
FT /note="K->R: PRKN-dependent polybiquitination is decreased,
FT whereas PRKN-dependent monoubiquitination, mitochondrial
FT calcium uptake and apoptosis are unaffected; when
FT associated with R-12; R-20 and 109-R-R-110."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 73
FT /note="E->Q: Abolishes ceramide and phosphatidylcholine
FT binding."
FT /evidence="ECO:0000269|PubMed:31015432"
FT MUTAGEN 109..110
FT /note="KK->RR: PRKN-dependent polybiquitination is
FT decreased, whereas PRKN-dependent monoubiquitination,
FT mitochondrial calcium uptake and apoptosis are unaffected;
FT when associated with R-12; R-20 and R-53."
FT /evidence="ECO:0000269|PubMed:32047033"
FT MUTAGEN 193
FT /note="S->A: Conformation remains open and constitutively
FT allows cytochrome c efflux."
FT /evidence="ECO:0000269|PubMed:20230784"
FT MUTAGEN 193
FT /note="S->E: Conformation remains closed and prevents
FT cytochrome c leakage."
FT /evidence="ECO:0000269|PubMed:20230784"
FT MUTAGEN 274
FT /note="K->R: Loss of PRKN-dependent monoubiquitination
FT increases mitochondria calcium uptake, and ultimately
FT increased apoptosis. Consequently, mitochondria are swelled
FT with defective cristae structures. PRKN-dependent
FT polyubiquitination is unaffected."
FT /evidence="ECO:0000269|PubMed:32047033"
FT CONFLICT 225
FT /note="Y -> L (in Ref. 4; CAB58127)"
FT /evidence="ECO:0000305"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:6G6U"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:6G6U"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:5XDN"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5XDO"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:6G6U"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 54..64
FT /evidence="ECO:0007829|PDB:6G6U"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:5XDN"
FT STRAND 81..92
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:6G6U"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 109..120
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5JDP"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:6G6U"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 163..174
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:6G6U"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 189..199
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 202..211
FT /evidence="ECO:0007829|PDB:6G6U"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:5XDO"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:6G6U"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5XDN"
FT STRAND 243..252
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:6G6U"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:6TIR"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:6G6U"
FT STRAND 273..282
FT /evidence="ECO:0007829|PDB:6G6U"
SQ SEQUENCE 283 AA; 30773 MW; 89BA3378B04020D5 CRC64;
MAVPPTYADL GKSARDVFTK GYGFGLIKLD LKTKSENGLE FTSSGSANTE TTKVTGSLET
KYRWTEYGLT FTEKWNTDNT LGTEITVEDQ LARGLKLTFD SSFSPNTGKK NAKIKTGYKR
EHINLGCDMD FDIAGPSIRG ALVLGYEGWL AGYQMNFETA KSRVTQSNFA VGYKTDEFQL
HTNVNDGTEF GGSIYQKVNK KLETAVNLAW TAGNSNTRFG IAAKYQIDPD ACFSAKVNNS
SLIGLGYTQT LKPGIKLTLS ALLDGKNVNA GGHKLGLGLE FQA
