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voltage-dependent anion-selective channel protein 1; VDAC-1; hVDAC1; outer mitochondrial membrane protein porin 1; plasmalemmal porin; porin 31HL; porin 31HM (VDAC1 VDAC)

Function: - forms a channel through the mitochondrial outer membrane & also the plasma membrane - the channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules - in the plasma membrane it is involved in cell volume regulation & apoptosis. - it adopts an open conformation at low or zero membrane potential & a closed conformation at potentials > 30-40 mV - the open state has a weak anion selectivity - the closed state is cation-selective - in association with ANT (inner mitochondrial membrane), may form the permeability transition pore complex (PTPC) - VDAC-1 may serve as the mitochondrial binding site for: a) hexokinase b) glycerol kinase c) bcl-2 d) peripheral benzodiazepine receptor - closure of the VDAC-1 channel is the earliest observed mitochondrial change during apoptosis, blocking passage of ADP/ATP - it is thought that bcl-2 may stabilize the open conformation of VDAC-1 - interacts with hexokinases (putative) - interacts with BCL2L1 - interacts with influenza A virus PB1-F2 protein Structure: - consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands - the helical N-terminus folds back into the pore opening & plays a role in voltage-gated channel activity - belongs to the eukaryotic mitochondrial porin family Compartment: - mitochondrial outer membrane - cell membrane Expression: heart, liver & skeletal muscle

Related

ADP/ATP translocase, adenine nucleotide translocase (ANT) or ADP/ATP carrier protein mitochondrial permeability transition pore complex (PTPC)

General

Cl- channel mitochondrial membrane protein pro apoptotic protein voltage-dependent anion channel, voltage-gated anion channel or porin

Properties

SIZE: entity length = 283 aa MW = 31 kD COMPARTMENT: mitochondrial outer membrane (GO:0005741) MOTIF: acetylation site SITE: N-TERMINUS EFFECTOR-BOUND: acetyl Ser phosphorylation site {S13} transmembrane domain {26-35} transmembrane domain {39-47} transmembrane domain {54-64} Tyr phosphorylation site {Y67} transmembrane domain {69-76} MOTIF: glutamate residue {73} transmembrane domain {80-89} transmembrane domain {95-104} MOTIF: Ser phosphorylation site {S101} Ser phosphorylation site {S104} transmembrane domain {111-120} transmembrane domain {123-130} transmembrane domain {137-145} MOTIF: Ser phosphorylation site {S137} transmembrane domain {150-158} transmembrane domain {163-175} transmembrane domain {178-185} transmembrane domain {189-198} MOTIF: Tyr phosphorylation site {Y195} transmembrane domain {202-211} transmembrane domain {218-227} transmembrane domain {231-238} transmembrane domain {242-251} MOTIF: cofactor-binding site [242-244] COFACTOR-BOUND: NAD transmembrane domain {254-263} cofactor-binding site [260-264] COFACTOR-BOUND: NAD transmembrane domain {273-282} ION-PERMEABILITY: Cl- MISC-INFO: EFFECTIVE_DIAMETER 1.7 NM CONDUCTANCE 450 PS

References

  1. UniProt :accession P21796
  2. Benz R. Biophysical properties of porin pores from mitochondrial outer membrane of eukaryotic cells. Experientia. 1990 Feb 15;46(2):131-7. Review. PMID: 1689250
  3. Dermietzel R, Hwang TK, Buettner R, Hofer A, Dotzler E, Kremer M, Deutzmann R, Thinnes FP, Fishman GI, Spray DC, et al. Cloning and in situ localization of a brain-derived porin that constitutes a large-conductance anion channel in astrocytic plasma membranes. Proc Natl Acad Sci U S A. 1994 Jan 18;91(2):499-503. PMID: 7507248
  4. Adams JM, Cory S. Life-or-death decisions by the Bcl-2 protein family. Trends Biochem Sci. 2001 Jan;26(1):61-6. Review. PMID: 11165519

Databases & Figures

OMIM 604492 UniProt P21796 Pfam PF01459 Entrez Gene 7416 Kegg hsa:7416 p53/apoptosis