Summary: Eukaryotic porin
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This is the Wikipedia entry entitled "Voltage-dependent anion channel". More...
Voltage-dependent anion channel
| Identifiers | |||||||||
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| Symbol | Porin_3 | ||||||||
| Pfam | PF01459 | ||||||||
| InterPro | IPR001925 | ||||||||
| PROSITE | PDOC00483 | ||||||||
| TCDB | 1.B.8 | ||||||||
| OPM family | 210 | ||||||||
| OPM protein | 3emn | ||||||||
| CDD | cd07306 | ||||||||
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Voltage-dependent anion channels are a class of porin ion channel located on the outer mitochondrial membrane.[1]
This major protein of the outer mitochondrial membrane of eukaryotes. It forms a voltage-dependent anion-selective channel (VDAC) that behaves as a general diffusion pore for small hydrophilic molecules.[2][3][4][5] The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. VDAC facilitates the exchange of ions and molecules between mitochondria and cytosol and is regulated by the interactions with other proteins and small molecules.[6]
Contents |
[edit] Structure
This protein contains about 280 amino acids and its sequence is composed of between 12 to 16 beta-strands that span the mitochondrial outer membrane.[7]
Since its discovery in 1976, extensive function and structure analysis of VDAC proteins has been conducted. A prominent feature of the pore emerged: when reconstituted into planar lipid bilayers, there is a voltage-dependent switch between an anion-selective high-conductance state with high metabolite flux and a cation-selective low-conductance state with limited passage of metabolites.
More than 30 years after its initial discovery, in 2008, three independent structural projects of VDAC-1 were completed. The first was solved by multi-dimensional NMR spectroscopy. The second applied a hybrid approach using crystallographic data. The third was for mouse VDAC-1 crystals determined by X-ray crystallographic techniques. The three projects of the 3D structures of VDAC-1 revealed many structural features. First, VDAC-1 represents a new structural class of outer membrane β-barrel proteins with an odd number of strands. Another aspect is that the negatively charged side chain of residue E73 is oriented towards the hydrophobic membrane environment. The 19-stranded 3D structure obtained under different experimental sources by three different laboratories fits the EM and AFM data from native membrane sources and represents a biologically relevant state of VDAC-1.[6]
[edit] Examples
Yeast contains two members of this family (genes POR1 and POR2); vertebrates have at least three members (genes VDAC1, VDAC2 and VDAC3).[7]
Human proteins containing this domain include TOMM40, TOMM40L, VDAC1, VDAC2, and VDAC3.
[edit] References
- ^ Hoogenboom BW, Suda K, Engel A, Fotiadis D (2007). "The supramolecular assemblies of voltage-dependent anion channels in the native membrane". J. Mol. Biol. 370 (2): 246–55. doi:10.1016/j.jmb.2007.04.073. PMID 17524423.
- ^ Benz R (1994). "Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins". Biochim. Biophys. Acta 1197 (2): 167–196. PMID 8031826.
- ^ Mannella CA (1992). "The 'ins' and 'outs' of mitochondrial membrane channels". Trends Biochem. Sci. 17 (8): 315–320. doi:10.1016/0968-0004(92)90444-E. PMID 1384178.
- ^ Dihanich M (1990). "The biogenesis and function of eukaryotic porins". Experientia 46 (2): 146–153. doi:10.1007/BF02027310. PMID 1689252.
- ^ Forte M, Guy HR, Mannella CA (1987). "Molecular genetics of the VDAC ion channel: structural model and sequence analysis". J. Bioenerg. Biomembr. 19 (4): 341–350. doi:10.1007/BF00768537. PMID 2442148.
- ^ a b Hiller S, Abramson J, Mannella C, Wagner G, Zeth K (September 2010). "The 3D structures of VDAC represent a native conformation". Trends Biochem. Sci. 35 (9): 514–21. doi:10.1016/j.tibs.2010.03.005. PMC 2933295. PMID 20708406. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2933295.
- ^ a b Sampson MJ, Lovell RS, Davison DB, Craigen WJ (1996). "A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8". Genomics 36 (1): 192–196. doi:10.1006/geno.1996.0445. PMID 8812436.
[edit] External links
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This article incorporates text from the public domain Pfam and InterPro IPR001925
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Eukaryotic porin
No Pfam abstract.
External database links
| PANDIT: | PF01459 |
| PROSITE: | PDOC00483 |
| Pseudofam: | PF01459 |
| SYSTERS: | Porin_3 |
| Transporter classification: | 1.B.8 3.A.8 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR001925
The major protein of the outer mitochondrial membrane of eukaryotes is a porin that forms a voltage-dependent anion-selective channel (VDAC) that behaves as a general diffusion pore for small hydrophilic molecules [PUBMED:8031826, PUBMED:1384178, PUBMED:1689252, PUBMED:2442148]. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV.
This protein contains about 280 amino acids and its sequence is composed of between 12 to 16 beta-strands that span the mitochondrial outer membrane. Yeast contains two members of this family (genes POR1 and POR2); vertebrates have at least three members (genes VDAC1, VDAC2 and VDAC3) [PUBMED:8812436].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | mitochondrial outer membrane (GO:0005741) |
| Molecular function | voltage-gated anion channel activity (GO:0008308) |
| Biological process | anion transport (GO:0006820) |
| transmembrane transport (GO:0055085) | |
| regulation of anion transport (GO:0044070) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
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Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Prodom_3211 (release 99.1) & Pfam-B__3211 (release 7.5) |
| Previous IDs: | Euk_porin; |
| Type: | Family |
| Author: | Bateman A |
| Number in seed: | 92 |
| Number in full: | 859 |
| Average length of the domain: | 254.50 aa |
| Average identity of full alignment: | 22 % |
| Average coverage of the sequence by the domain: | 86.69 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 273 | ||||||||||||
| Family (HMM) version: | 17 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Archea
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Eukaryota
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Viruses
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Unclassified sequence
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence