ID   VDAC1_YEAST             Reviewed;         283 AA.
AC   P04840; D6W1C3;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 207.
DE   RecName: Full=Mitochondrial outer membrane protein porin 1;
DE   AltName: Full=Voltage-dependent anion-selective channel protein 1;
DE            Short=VDAC-1;
GN   Name=POR1; Synonyms=OMP2, VDAC1; OrderedLocusNames=YNL055C;
GN   ORFNames=N2441, YNL2441C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2408884; DOI=10.1002/j.1460-2075.1985.tb03695.x;
RA   Mihara K., Sato R.;
RT   "Molecular cloning and sequencing of cDNA for yeast porin, an outer
RT   mitochondrial membrane protein: a search for targeting signal in the
RT   primary structure.";
RL   EMBO J. 4:769-774(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2442148; DOI=10.1007/bf00768537;
RA   Forte M.A., Guy H.R., Mannella C.A.;
RT   "Molecular genetics of the VDAC ion channel: structural model and sequence
RT   analysis.";
RL   J. Bioenerg. Biomembr. 19:341-350(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / FY1676;
RX   PubMed=8533472; DOI=10.1002/yea.320111008;
RA   Bergez P., Doignon F., Crouzet M.;
RT   "The sequence of a 44 420 bp fragment located on the left arm of chromosome
RT   XIV from Saccharomyces cerevisiae.";
RL   Yeast 11:967-974(1995).
RN   [4]
RP   ERRATUM OF PUBMED:8533472.
RX   PubMed=8904343;
RX   DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d;
RA   Bergez P., Doignon F., Crouzet M.;
RL   Yeast 12:297-297(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-40; 45-108; 125-132; 165-174; 206-234 AND 237-274,
RP   CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA   Bienvenut W.V., Peters C.;
RL   Submitted (MAY-2005) to UniProtKB.
RN   [8]
RP   MUTAGENESIS OF LYS-61.
RX   PubMed=2478533; DOI=10.1007/bf00762519;
RA   Blachly-Dyson E., Peng S.Z., Colombini M., Forte M.A.;
RT   "Probing the structure of the mitochondrial channel, VDAC, by site-directed
RT   mutagenesis: a progress report.";
RL   J. Bioenerg. Biomembr. 21:471-483(1989).
RN   [9]
RP   MUTAGENESIS OF LYS-19 AND ASP-51.
RA   Thomas L., Blachly-Dyson E., Colombini M., Forte M.A.;
RT   "Probing for the voltage sensor of the VDAC ion channel by site-directed
RT   mutagenesis.";
RL   Biophys. J. 59:215A-215A(1991).
RN   [10]
RP   FUNCTION.
RX   PubMed=9435273; DOI=10.1007/s002329900324;
RA   Lee A.C., Xu X., Blachly-Dyson E., Forte M.A., Colombini M.;
RT   "The role of yeast VDAC genes on the permeability of the mitochondrial
RT   outer membrane.";
RL   J. Membr. Biol. 161:173-181(1998).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA   Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA   van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT   "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT   phosphorylation in assembly of the ATP synthase.";
RL   Mol. Cell. Proteomics 6:1896-1906(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-117, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [14]
RP   INTERACTION WITH AIM5; FCJ1 AND MOS1.
RX   PubMed=21987634; DOI=10.1083/jcb.201107053;
RA   Hoppins S., Collins S.R., Cassidy-Stone A., Hummel E., Devay R.M.,
RA   Lackner L.L., Westermann B., Schuldiner M., Weissman J.S., Nunnari J.;
RT   "A mitochondrial-focused genetic interaction map reveals a scaffold-like
RT   complex required for inner membrane organization in mitochondria.";
RL   J. Cell Biol. 195:323-340(2011).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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).
CC   -!- FUNCTION: Forms a channel through the cell membrane that allows
CC       diffusion of small hydrophilic molecules. The channel adopts an open
CC       conformation at low or zero membrane potential and a closed
CC       conformation at potentials above 30-40 mV. The open state has a weak
CC       anion selectivity whereas the closed state is cation-selective. Is the
CC       major permeability factor of the mitochondrial outer membrane.
CC       {ECO:0000269|PubMed:9435273}.
CC   -!- SUBUNIT: Interacts with AIM5, FCJ1 and MOS1.
CC       {ECO:0000269|PubMed:21987634}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane.
CC   -!- DOMAIN: Consists mainly of membrane-spanning sided beta-sheets. 19
CC       strands distributed along the entire VDAC protein, have the potential
CC       to adopt transmembrane beta pleated sheet structures, which rolled
CC       together may form a 'beta-barrel' type structure, possessing pore
CC       dimensions.
CC   -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC       {ECO:0000305}.
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DR   EMBL; X02324; CAA26184.1; -; mRNA.
DR   EMBL; M34907; AAA35208.1; -; mRNA.
DR   EMBL; U12141; AAA99656.1; -; Genomic_DNA.
DR   EMBL; Z71331; CAA95926.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10489.1; -; Genomic_DNA.
DR   PIR; S58721; MMBYP.
DR   RefSeq; NP_014343.1; NM_001182894.1.
DR   AlphaFoldDB; P04840; -.
DR   SMR; P04840; -.
DR   BioGRID; 35766; 501.
DR   DIP; DIP-6453N; -.
DR   IntAct; P04840; 91.
DR   MINT; P04840; -.
DR   STRING; 4932.YNL055C; -.
DR   TCDB; 1.B.8.1.1; the mitochondrial and plastid porin (mpp) family.
DR   iPTMnet; P04840; -.
DR   MaxQB; P04840; -.
DR   PaxDb; 4932-YNL055C; -.
DR   PeptideAtlas; P04840; -.
DR   DNASU; 855669; -.
DR   EnsemblFungi; YNL055C_mRNA; YNL055C; YNL055C.
DR   GeneID; 855669; -.
DR   KEGG; sce:YNL055C; -.
DR   AGR; SGD:S000005000; -.
DR   SGD; S000005000; POR1.
DR   VEuPathDB; FungiDB:YNL055C; -.
DR   eggNOG; KOG3126; Eukaryota.
DR   GeneTree; ENSGT00950000182869; -.
DR   HOGENOM; CLU_044399_0_1_1; -.
DR   InParanoid; P04840; -.
DR   OMA; WSNANNL; -.
DR   OrthoDB; 2782367at2759; -.
DR   BioCyc; YEAST:G3O-33087-MONOMER; -.
DR   Reactome; R-SCE-70268; Pyruvate metabolism.
DR   BioGRID-ORCS; 855669; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P04840; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P04840; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IPI:SGD.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR   GO; GO:0048039; F:ubiquinone binding; IDA:SGD.
DR   GO; GO:0008308; F:voltage-gated monoatomic anion channel activity; IDA:SGD.
DR   GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR   GO; GO:0045454; P:cell redox homeostasis; IMP:SGD.
DR   GO; GO:0051027; P:DNA transport; IMP:SGD.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR   GO; GO:0006811; P:monoatomic ion transport; IDA:SGD.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:SGD.
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:SF70; GH26960P-RELATED; 1.
DR   PANTHER; PTHR11743; VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL; 1.
DR   Pfam; PF01459; Porin_3; 1.
DR   PRINTS; PR00185; EUKARYTPORIN.
DR   PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
DR   UCD-2DPAGE; P04840; -.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein; Porin; Reference proteome;
KW   Transmembrane; Transmembrane beta strand; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.7"
FT   CHAIN           2..283
FT                   /note="Mitochondrial outer membrane protein porin 1"
FT                   /id="PRO_0000050524"
FT   MOD_RES         109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17761666,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         117
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         19
FT                   /note="K->E: 2.5-fold reduction in steepness of voltage
FT                   dependence."
FT                   /evidence="ECO:0000269|Ref.9"
FT   MUTAGEN         51
FT                   /note="D->K: 2-fold increase in steepness of voltage
FT                   dependence."
FT                   /evidence="ECO:0000269|Ref.9"
FT   MUTAGEN         61
FT                   /note="K->E: Alters the selectivity of VDAC."
FT                   /evidence="ECO:0000269|PubMed:2478533"
FT   CONFLICT        118
FT                   /note="Q -> E (in Ref. 1; CAA26184 and 2; AAA35208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        203..207
FT                   /note="GAKAT -> AKATM (in Ref. 2; AAA35208)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   283 AA;  30428 MW;  C99D03711AF9B54D CRC64;
     MSPPVYSDIS RNINDLLNKD FYHATPAAFD VQTTTANGIK FSLKAKQPVK DGPLSTNVEA
     KLNDKQTGLG LTQGWSNTNN LQTKLEFANL TPGLKNELIT SLTPGVAKSA VLNTTFTQPF
     FTARGAFDLC LKSPTFVGDL TMAHEGIVGG AEFGYDISAG SISRYAMALS YFAKDYSLGA
     TLNNEQITTV DFFQNVNAFL QVGAKATMNC KLPNSNVNIE FATRYLPDAS SQVKAKVSDS
     GIVTLAYKQL LRPGVTLGVG SSFDALKLSE PVHKLGWSLS FDA
//