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Protein

Voltage-dependent anion-selective channel protein 1

Gene

VDAC1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Forms a channel through the mitochondrial outer membrane and 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 and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.By similarity

Enzyme regulationi

Inhibited by nitric oxide.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei73 – 731Involved in hexokinase bindingBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi242 – 2443NADBy similarity
Nucleotide bindingi260 – 2645NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Porin

Keywords - Biological processi

Apoptosis, Ion transport, Transport

Keywords - Ligandi

NAD, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent anion-selective channel protein 1
Short name:
VDAC-1
Alternative name(s):
Outer mitochondrial membrane protein porin 1
Gene namesi
Name:VDAC1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 3

Subcellular locationi

  • Mitochondrion outer membrane By similarity; Multi-pass membrane protein By similarity
  • Cell membrane By similarity; Multi-pass membrane protein By similarity
  • Membrane raft By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei26 – 3510Beta strandedBy similarity
Transmembranei39 – 479Beta strandedBy similarity
Transmembranei54 – 6411Beta strandedBy similarityAdd
BLAST
Transmembranei69 – 768Beta strandedBy similarity
Transmembranei80 – 8910Beta strandedBy similarity
Transmembranei95 – 10410Beta strandedBy similarity
Transmembranei111 – 12010Beta strandedBy similarity
Transmembranei123 – 1308Beta strandedBy similarity
Transmembranei137 – 1459Beta strandedBy similarity
Transmembranei150 – 1589Beta strandedBy similarity
Transmembranei163 – 17513Beta strandedBy similarityAdd
BLAST
Transmembranei178 – 1858Beta strandedBy similarity
Transmembranei189 – 19810Beta strandedBy similarity
Transmembranei202 – 21110Beta strandedBy similarity
Transmembranei218 – 22710Beta strandedBy similarity
Transmembranei231 – 2388Beta strandedBy similarity
Transmembranei242 – 25110Beta strandedBy similarity
Transmembranei254 – 26310Beta strandedBy similarity
Transmembranei273 – 28210Beta strandedBy similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 283282Voltage-dependent anion-selective channel protein 1PRO_0000050502Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei19 – 191PhosphothreonineBy similarity
Modified residuei20 – 201N6-acetyllysine; alternateBy similarity
Modified residuei20 – 201N6-succinyllysine; alternateBy similarity
Cross-linki53 – 53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei67 – 671PhosphotyrosineBy similarity
Modified residuei107 – 1071PhosphothreonineBy similarity
Modified residuei109 – 1091N6-acetyllysine; alternateBy similarity
Cross-linki109 – 109Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki110 – 110Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki161 – 161Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei193 – 1931Phosphoserine; by NEK1By similarity
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei252 – 2521N6-acetyllysineBy similarity
Modified residuei266 – 2661N6-acetyllysine; alternateBy similarity
Cross-linki266 – 266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity

Post-translational modificationi

Phosphorylation at Ser-193 by NEK1 promotes the open conformational state preventing excessive mitochondrial membrane permeability and subsequent apoptotic cell death after injury. Phosphorylation by the AKT-GSK3B axis stabilizes the protein probably by preventing ubiquitin-mediated proteasomal degradation.By similarity
Ubiquitinated by PARK2 during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ9TT15.

Interactioni

Subunit structurei

Interacts with hexokinases including HK1. The HK1-VDAC1 complex interacts with ATF2. Interacts with BCL2L1. Interacts with BAK1. Interacts with BOP/C22orf29 (via BH3 domain). Interacts with beta amyloid and APP; induces VDAC1 dephosphorylation.By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008083.

Family & Domainsi

Domaini

Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands. The helical N-terminus folds back into the pore opening and plays a role in voltage-gated channel activity (By similarity).By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiKOG3126. Eukaryota.
ENOG410ZBK1. LUCA.
GeneTreeiENSGT00390000011336.
HOGENOMiHOG000188277.
HOVERGENiHBG054036.
InParanoidiQ9TT15.
KOiK05862.
OMAiYGLMFTE.
OrthoDBiEOG7P8P8G.
TreeFamiTF315091.

Family and domain databases

Gene3Di2.40.160.10. 1 hit.
InterProiIPR023614. Porin_dom.
IPR001925. Porin_Euk.
IPR027246. Porin_Euk/Tom40.
IPR030270. VDAC1.
[Graphical view]
PANTHERiPTHR11743:SF13. PTHR11743:SF13. 1 hit.
PfamiPF01459. Porin_3. 1 hit.
[Graphical view]
PRINTSiPR00185. EUKARYTPORIN.
PROSITEiPS00558. EUKARYOTIC_PORIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9TT15-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVPPTYADL GKSARDVFTK GYGFGLIKLD LKTKSENGLE FTSSGSANTE
60 70 80 90 100
TTKVTGSLET KYRWTEYGLT FTEKWNTDNT LGTEITVEDQ LARGLKLTFD
110 120 130 140 150
SSFSPNTGKK NAKIKTGYKR EHINLGCDVD FDIAGPSIRG ALVLGYEGWL
160 170 180 190 200
AGYQMNFETA KSRVTQSNFA VGYKTDEFQL HTNVNDGTEF GGSIYQKVNK
210 220 230 240 250
KLETAVNLAW TAGNSNTRFG IAAKYQIDPD ACFSAKVNNS SLIGLGYTQT
260 270 280
LKPGIKLTLS ALLDGKNVNA GGHKLGLGLE FQA
Length:283
Mass (Da):30,741
Last modified:January 23, 2007 - v3
Checksum:i9CAE6D8D50A18BD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF209725 mRNA. Translation: AAF22835.1.
RefSeqiNP_001075544.1. NM_001082075.1.
XP_008253053.1. XM_008254831.1.
UniGeneiOcu.2411.

Genome annotation databases

EnsembliENSOCUT00000009371; ENSOCUP00000008083; ENSOCUG00000009369.
GeneIDi100008751.
KEGGiocu:100008751.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF209725 mRNA. Translation: AAF22835.1.
RefSeqiNP_001075544.1. NM_001082075.1.
XP_008253053.1. XM_008254831.1.
UniGeneiOcu.2411.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008083.

Proteomic databases

PRIDEiQ9TT15.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000009371; ENSOCUP00000008083; ENSOCUG00000009369.
GeneIDi100008751.
KEGGiocu:100008751.

Organism-specific databases

CTDi7416.

Phylogenomic databases

eggNOGiKOG3126. Eukaryota.
ENOG410ZBK1. LUCA.
GeneTreeiENSGT00390000011336.
HOGENOMiHOG000188277.
HOVERGENiHBG054036.
InParanoidiQ9TT15.
KOiK05862.
OMAiYGLMFTE.
OrthoDBiEOG7P8P8G.
TreeFamiTF315091.

Family and domain databases

Gene3Di2.40.160.10. 1 hit.
InterProiIPR023614. Porin_dom.
IPR001925. Porin_Euk.
IPR027246. Porin_Euk/Tom40.
IPR030270. VDAC1.
[Graphical view]
PANTHERiPTHR11743:SF13. PTHR11743:SF13. 1 hit.
PfamiPF01459. Porin_3. 1 hit.
[Graphical view]
PRINTSiPR00185. EUKARYTPORIN.
PROSITEiPS00558. EUKARYOTIC_PORIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Rae J.L.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: New Zealand white.
    Tissue: Corneal endothelium.

Entry informationi

Entry nameiVDAC1_RABIT
AccessioniPrimary (citable) accession number: Q9TT15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.