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VDAC1_PIG
ID   VDAC1_PIG               Reviewed;         283 AA.
AC   Q9MZ16;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Voltage-dependent anion-selective channel protein 1;
DE            Short=VDAC-1;
GN   Name=VDAC1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens;
RA   Rae J.L.;
RT   "Ion channels in the lens.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms a channel through the mitochondrial outer membrane and
CC       also the plasma membrane. The channel at the outer mitochondrial
CC       membrane allows diffusion of small hydrophilic molecules; in the plasma
CC       membrane it is involved in cell volume regulation and apoptosis. It
CC       adopts an open conformation at low or zero membrane potential and a
CC       closed conformation at potentials above 30-40 mV. The open state has a
CC       weak anion selectivity whereas the closed state is cation-selective.
CC       Binds various signaling molecules, including the sphingolipid ceramide,
CC       the phospholipid phosphatidylcholine, and the sterol cholesterol. In
CC       depolarized mitochondria, acts downstream of PRKN and PINK1 to promote
CC       mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes
CC       mitophagy, while monoubiquitination by PRKN decreases mitochondrial
CC       calcium influx which ultimately inhibits apoptosis. May participate in
CC       the formation of the permeability transition pore complex (PTPC)
CC       responsible for the release of mitochondrial products that triggers
CC       apoptosis. May mediate ATP export from cells.
CC       {ECO:0000250|UniProtKB:P21796}.
CC   -!- ACTIVITY REGULATION: Inhibited by nitric oxide.
CC       {ECO:0000250|UniProtKB:P21796}.
CC   -!- SUBUNIT: Homodimer and homotrimer; in response to cyclic AMP or
CC       calcium. Interacts with hexokinases including HK1. The HK1-VDAC1
CC       complex interacts with ATF2. Interacts with BCL2L1. Interacts with
CC       BAK1. Interacts with RTL10/BOP (via BH3 domain). Interacts with
CC       amyloid-beta and APP; induces VDAC1 dephosphorylation. Component of the
CC       mitochondrial permeability transition pore complex (mPTPC), at least
CC       composed of SPG7, VDAC1 and PPIF. Interacts with SPG7, NIPSNAP2 and
CC       SLC25A30. Interacts with TMEM41B. Interacts with BCAP31.
CC       {ECO:0000250|UniProtKB:P21796}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P21796}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P21796}. Cell membrane
CC       {ECO:0000250|UniProtKB:P21796}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P21796}. Membrane raft
CC       {ECO:0000250|UniProtKB:P21796}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P21796}.
CC   -!- DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19
CC       beta-strands. The helical N-terminus folds back into the pore opening
CC       and plays a role in voltage-gated channel activity.
CC       {ECO:0000250|UniProtKB:P21796}.
CC   -!- PTM: Phosphorylation at Ser-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:0000250|UniProtKB:P21796}.
CC   -!- PTM: Ubiquitinated. Undergoes monoubiquitination and polyubiquitination
CC       by PRKN; monoubiquitination at Lys-274 inhibits apoptosis, whereas
CC       polyubiquitination leads to its degradation and promotes mitophagy.
CC       Deubiquitinated by USP30. {ECO:0000250|UniProtKB:P21796}.
CC   -!- MISCELLANEOUS: Dicyclohexylcarbodiimide (DCCD) binding on Glu-73
CC       inhibits hexokinase binding in vitro. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC       {ECO:0000305}.
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DR   EMBL; AF268461; AAF78963.1; -; mRNA.
DR   RefSeq; NP_999125.1; NM_213960.1.
DR   RefSeq; XP_005653005.1; XM_005652948.2.
DR   RefSeq; XP_005653006.1; XM_005652949.2.
DR   RefSeq; XP_005653007.1; XM_005652950.2.
DR   AlphaFoldDB; Q9MZ16; -.
DR   BMRB; Q9MZ16; -.
DR   SMR; Q9MZ16; -.
DR   STRING; 9823.ENSSSCP00000015206; -.
DR   iPTMnet; Q9MZ16; -.
DR   PaxDb; Q9MZ16; -.
DR   PeptideAtlas; Q9MZ16; -.
DR   PRIDE; Q9MZ16; -.
DR   Ensembl; ENSSSCT00000058217; ENSSSCP00000036072; ENSSSCG00000014296.
DR   Ensembl; ENSSSCT00005014713; ENSSSCP00005008789; ENSSSCG00005009366.
DR   Ensembl; ENSSSCT00005014759; ENSSSCP00005008822; ENSSSCG00005009366.
DR   Ensembl; ENSSSCT00015029477; ENSSSCP00015011599; ENSSSCG00015021891.
DR   Ensembl; ENSSSCT00025069273; ENSSSCP00025029833; ENSSSCG00025050567.
DR   Ensembl; ENSSSCT00030006992; ENSSSCP00030003141; ENSSSCG00030005103.
DR   Ensembl; ENSSSCT00035067895; ENSSSCP00035027513; ENSSSCG00035050939.
DR   Ensembl; ENSSSCT00045053437; ENSSSCP00045037160; ENSSSCG00045031086.
DR   Ensembl; ENSSSCT00050090144; ENSSSCP00050038715; ENSSSCG00050066150.
DR   Ensembl; ENSSSCT00055019919; ENSSSCP00055015722; ENSSSCG00055010071.
DR   Ensembl; ENSSSCT00060065887; ENSSSCP00060028202; ENSSSCG00060048503.
DR   Ensembl; ENSSSCT00065037080; ENSSSCP00065015590; ENSSSCG00065027495.
DR   Ensembl; ENSSSCT00070040455; ENSSSCP00070033932; ENSSSCG00070020375.
DR   GeneID; 397010; -.
DR   KEGG; ssc:397010; -.
DR   CTD; 7416; -.
DR   VGNC; VGNC:100881; VDAC1.
DR   eggNOG; KOG3126; Eukaryota.
DR   GeneTree; ENSGT00950000182869; -.
DR   HOGENOM; CLU_044399_2_0_1; -.
DR   InParanoid; Q9MZ16; -.
DR   OMA; IKTAYKC; -.
DR   OrthoDB; 938262at2759; -.
DR   TreeFam; TF315091; -.
DR   Reactome; R-SSC-5205685; PINK1-PRKN Mediated Mitophagy.
DR   Reactome; R-SSC-5689880; Ub-specific processing proteases.
DR   Reactome; R-SSC-70268; Pyruvate metabolism.
DR   Proteomes; UP000008227; Chromosome 2.
DR   Proteomes; UP000314985; Chromosome 2.
DR   Bgee; ENSSSCG00000014296; Expressed in psoas major muscle and 45 other tissues.
DR   ExpressionAtlas; Q9MZ16; baseline and differential.
DR   Genevisible; Q9MZ16; SS.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005757; C:mitochondrial permeability transition pore complex; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008308; F:voltage-gated anion channel activity; ISS:UniProtKB.
DR   GO; GO:0006820; P:anion transport; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Apoptosis; Cell membrane; Ion transport; Isopeptide bond;
KW   Lipid-binding; Membrane; Mitochondrion; Mitochondrion outer membrane; NAD;
KW   Nucleotide-binding; Phosphoprotein; Porin; Reference proteome;
KW   Transmembrane; Transmembrane beta strand; Transport; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   CHAIN           2..283
FT                   /note="Voltage-dependent anion-selective channel protein 1"
FT                   /id="PRO_0000050501"
FT   TRANSMEM        26..35
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        39..47
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        54..64
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        69..76
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        80..89
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        95..104
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        111..120
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        123..130
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        137..145
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        150..158
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        163..175
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        178..185
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        189..198
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        202..211
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        218..227
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        231..238
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        242..251
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        254..263
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        273..282
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   BINDING         242..244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   BINDING         260..264
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   SITE            73
FT                   /note="Involved in ceramide and phosphatidylcholine
FT                   binding. Critical for channel structural stability and
FT                   gating"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
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:0000250|UniProtKB:P21796"
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:0000250|UniProtKB:P21796"
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:0000250|UniProtKB:P21796"
FT   MOD_RES         240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
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:0000250|UniProtKB:P21796"
FT   CROSSLNK        12
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   CROSSLNK        20
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P45880"
FT   CROSSLNK        53
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   CROSSLNK        61
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   CROSSLNK        109
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   CROSSLNK        110
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   CROSSLNK        161
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   CROSSLNK        266
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   CROSSLNK        274
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
SQ   SEQUENCE   283 AA;  30727 MW;  B4ADE7366B31986D CRC64;
     MAVPPTYADL GKSARDVFTK GYGFGLIKLD LKTKSENGLE FTSSGSANTE TTKVTGSLET
     KYRWTEYGLT FTEKWNTDNT LGTEITVEDQ LARGLKLTFD SSFSPNTGKK NAKIKTGYKR
     EHVNLGCDVD FDIAGPSIRG ALVLGYEGWL AGYQMNFETA KSRVTQSNFA VGYKTDEFQL
     HTNVNDGTEF GGSIYQKVNK KLETAVNLAW TAGNSNTRFG IAAKYQIDPD ACFSAKVNNS
     SLIGLGYTQT LKPGIKLTLS ALLDGKNVNA GGHKLGLGLE FQA
 
 
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