Q9Y277 · VDAC3_HUMAN
- ProteinVoltage-dependent anion-selective channel protein 3
- GeneVDAC3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids283 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (By similarity).
Involved in male fertility and sperm mitochondrial sheath formation (By similarity).
Involved in male fertility and sperm mitochondrial sheath formation (By similarity).
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular exosome | |
Cellular Component | membrane | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Cellular Component | pore complex | |
Cellular Component | synapse | |
Molecular Function | nucleotide binding | |
Molecular Function | porin activity | |
Molecular Function | voltage-gated monoatomic anion channel activity | |
Biological Process | adenine transport | |
Biological Process | behavioral fear response | |
Biological Process | learning | |
Biological Process | neuron-neuron synaptic transmission | |
Biological Process | sperm mitochondrial sheath assembly | |
Biological Process | spermatogenesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameVoltage-dependent anion-selective channel protein 3
- Short namesVDAC-3; hVDAC3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y277
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: May localize to non-mitochondrial membranes.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 26-35 | Beta stranded | ||||
Sequence: MVKIDLKTKS | ||||||
Transmembrane | 39-47 | Beta stranded | ||||
Sequence: VEFSTSGHA | ||||||
Transmembrane | 54-64 | Beta stranded | ||||
Sequence: ASGNLETKYKV | ||||||
Transmembrane | 69-76 | Beta stranded | ||||
Sequence: LTFTQKWN | ||||||
Transmembrane | 80-89 | Beta stranded | ||||
Sequence: TLGTEISWEN | ||||||
Transmembrane | 95-104 | Beta stranded | ||||
Sequence: LKLTLDTIFV | ||||||
Transmembrane | 111-120 | Beta stranded | ||||
Sequence: SGKLKASYKR | ||||||
Transmembrane | 123-130 | Beta stranded | ||||
Sequence: FSVGSNVD | ||||||
Transmembrane | 137-145 | Beta stranded | ||||
Sequence: TIYGWAVLA | ||||||
Transmembrane | 150-158 | Beta stranded | ||||
Sequence: LAGYQMSFD | ||||||
Transmembrane | 163-175 | Beta stranded | ||||
Sequence: KLSQNNFALGYKA | ||||||
Transmembrane | 178-185 | Beta stranded | ||||
Sequence: FQLHTHVN | ||||||
Transmembrane | 189-198 | Beta stranded | ||||
Sequence: EFGGSIYQKV | ||||||
Transmembrane | 202-211 | Beta stranded | ||||
Sequence: IETSINLAWT | ||||||
Transmembrane | 218-227 | Beta stranded | ||||
Sequence: RFGIAAKYML | ||||||
Transmembrane | 231-238 | Beta stranded | ||||
Sequence: TSLSAKVN | ||||||
Transmembrane | 242-251 | Beta stranded | ||||
Sequence: LIGLGYTQTL | ||||||
Transmembrane | 254-263 | Beta stranded | ||||
Sequence: GVKLTLSALI | ||||||
Transmembrane | 273-282 | Beta stranded | ||||
Sequence: HKVGLGFELE |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 271 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylcysteine | ||||
Sequence: C | |||||||
Chain | PRO_0000050512 | 2-283 | UniProt | Voltage-dependent anion-selective channel protein 3 | |||
Sequence: CNTPTYCDLGKAAKDVFNKGYGFGMVKIDLKTKSCSGVEFSTSGHAYTDTGKASGNLETKYKVCNYGLTFTQKWNTDNTLGTEISWENKLAEGLKLTLDTIFVPNTGKKSGKLKASYKRDCFSVGSNVDIDFSGPTIYGWAVLAFEGWLAGYQMSFDTAKSKLSQNNFALGYKAADFQLHTHVNDGTEFGGSIYQKVNEKIETSINLAWTAGSNNTRFGIAAKYMLDCRTSLSAKVNNASLIGLGYTQTLRPGVKLTLSALIDGKNFSAGGHKVGLGFELEA | |||||||
Modified residue | 4 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 4 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 12 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 15 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 20 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Cross-link | 53 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 61 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 90 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 109 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 110 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 163 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 165 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 188 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 241 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 241 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 250 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 266 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 266 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Cross-link | 274 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with ARMC12 in a TBC1D21-dependent manner. Interacts with MISFA.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y277 | VDAC1 P21796 | 4 | EBI-354196, EBI-354158 | |
BINARY | Q9Y277 | VDAC2 P45880 | 2 | EBI-354196, EBI-354022 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Domain
Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands.
Sequence similarities
Belongs to the eukaryotic mitochondrial porin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9Y277-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length283
- Mass (Da)30,659
- Last updated1999-11-01 v1
- ChecksumE03CBCEDA72A9783
Q9Y277-2
- Name2
- Differences from canonical
- 39-39: V → VM
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_005079 | 39 | in isoform 2 | |||
Sequence: V → VM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U90943 EMBL· GenBank· DDBJ | AAB93872.1 EMBL· GenBank· DDBJ | mRNA | ||
AF038962 EMBL· GenBank· DDBJ | AAC39876.1 EMBL· GenBank· DDBJ | mRNA | ||
BC056870 EMBL· GenBank· DDBJ | AAH56870.1 EMBL· GenBank· DDBJ | mRNA | ||
AH008073 EMBL· GenBank· DDBJ | AAD49610.1 EMBL· GenBank· DDBJ | Genomic DNA |