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 27-MAR-2024, entry version 243. 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 sterols cholesterol and CC oxysterol (PubMed:31015432). In depolarized mitochondria, acts CC downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; CC polyubiquitination by PRKN promotes mitophagy, while monoubiquitination CC by PRKN decreases mitochondrial calcium influx which ultimately CC inhibits apoptosis (PubMed:32047033). May participate in the formation CC of the permeability transition pore complex (PTPC) responsible for the CC release of mitochondrial products that triggers apoptosis CC (PubMed:15033708, PubMed:25296756). May mediate ATP export from cells CC (PubMed:30061676). {ECO:0000269|PubMed:11845315, CC ECO:0000269|PubMed:15033708, ECO:0000269|PubMed:18755977, CC ECO:0000269|PubMed:20230784, ECO:0000269|PubMed:25296756, CC ECO:0000269|PubMed:30061676, ECO:0000269|PubMed:31015432, CC ECO:0000269|PubMed:32047033, 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="https://atlasgeneticsoncology.org/gene/50902/VDAC1"; 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; 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; 518. DR CORUM; P21796; -. DR DIP; DIP-32862N; -. DR IntAct; P21796; 261. DR MINT; P21796; -. DR STRING; 9606.ENSP00000378487; -. 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 GlyCosmos; P21796; 1 site, 1 glycan. 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 EPD; P21796; -. DR jPOST; P21796; -. DR MassIVE; P21796; -. DR MaxQB; P21796; -. DR PaxDb; 9606-ENSP00000265333; -. DR PeptideAtlas; P21796; -. DR PRIDE; P21796; -. DR ProteomicsDB; 53904; -. DR Pumba; P21796; -. DR TopDownProteomics; P21796; -. DR ABCD; P21796; 1 sequenced antibody. DR Antibodypedia; 3137; 824 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 AGR; HGNC:12669; -. 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; WSNANNL; -. DR OrthoDB; 2897965at2759; -. 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; 256 hits in 1156 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 203 other cell types or tissues. DR ExpressionAtlas; P21796; baseline and differential. 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:0008142; F:oxysterol binding; ISS:UniProtKB. 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 monoatomic anion channel activity; 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:0006820; P:monoatomic anion transport; IDA:UniProtKB. 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; Porin; 1. DR InterPro; IPR023614; Porin_dom_sf. DR InterPro; IPR001925; Porin_Euk. DR InterPro; IPR027246; Porin_Euk/Tom40. DR PANTHER; PTHR11743; VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL; 1. DR PANTHER; PTHR11743:SF13; VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL PROTEIN 1; 1. DR Pfam; PF01459; Porin_3; 1. DR PRINTS; PR00185; EUKARYTPORIN. DR PROSITE; PS00558; EUKARYOTIC_PORIN; 1. DR UCD-2DPAGE; P21796; -. DR Genevisible; P21796; HS. 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 //