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1.B.8.1.1
Voltage-dependent anion channel-1 (VDAC1; OMP2; Por1) porin.  It is a component of the mitochondrial permeability transition pore (mPTP) which includes cyclophilin D, VDAC and the adenine nucleotide translocator (TC subfamily 2.A.29.1) (Austin et al. 2013). Mitochondrial synthesis of cardiolipin (CL) and phosphatidylethanolamine requires the transport of their precursors, phosphatidic acid and phosphatidylserine, respectively, to the mitochondrial inner membrane. The Ups1-Mdm35 and Ups2-Mdm35 complexes transfer phosphatidic acid and phosphatidylserine, respectively, between the mitochondrial outer and inner membranes. A Ups1-independent CL accumulation pathway requires several mitochondrial proteins with unknown functions including Mdm31. Miyata et al. 2018 identified VDAC1 (Por1) as a protein that interacts with both Mdm31 and Mdm35. Depletion of the porins Por1 and Por2 destabilized Ups1 and Ups2, decreased CL levels by ~90%, and caused loss of Ups2-dependent phosphatidylethanolamine synthesis, but did not affect Ups2-independent phosphatidylethanolamine synthesis in mitochondria. Por1 mutations that affected its interactions with Mdm31 and Mdm35, but not respiratory growth, also decreased CL levels. Using HeLa cells, the authors showed that mammalian porins also function in mitochondrial CL metabolism. Thus, yeast porins function in mitochondrial phospholipid metabolism, and porin-mediated regulation of CL metabolism appears to be evolutionarily conserved. Targeted to mitocondria via a C-terminal hydrophobic β-strand terminated by a hydrophiic residue (Klinger et al. 2019).

Accession Number:P04840
Protein Name:OMP2 aka VDAC aka POR1 aka YNL055C aka N2441 aka YNL2441C
Length:283
Molecular Weight:30428.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Location1 / Topology2 / Orientation3: Mitochondrion outer membrane1
Substrate anions

Cross database links:

Genevestigator: P04840
eggNOG: fuNOG04899
HEGENOM: HBG396026
DIP: DIP-6453N
RefSeq: NP_014343.1   
Entrez Gene ID: 855669   
Pfam: PF01459   
KEGG: sce:YNL055C   

Gene Ontology

GO:0031307 C:integral to mitochondrial outer membrane
GO:0046930 C:pore complex
GO:0005515 F:protein binding
GO:0008308 F:voltage-gated anion channel activity
GO:0006820 P:anion transport
GO:0006915 P:apoptosis
GO:0007005 P:mitochondrion organization
GO:0055085 P:transmembrane transport

References (9)

[1] “Molecular cloning and sequencing of cDNA for yeast porin, an outer mitochondrial membrane protein: a search for targeting signal in the primary structure.”  Mihara K.et.al.   2408884
[2] “Molecular genetics of the VDAC ion channel: structural model and sequence analysis.”  Forte M.A.et.al.   2442148
[3] “The sequence of a 44 420 bp fragment located on the left arm of chromosome XIV from Saccharomyces cerevisiae.”  Bergez P.et.al.   8533472
[4] “”  Bergez P.et.al.   8904343
[5] “The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.”  Philippsen P.et.al.   9169873
[6] “Probing the structure of the mitochondrial channel, VDAC, by site-directed mutagenesis: a progress report.”  Blachly-Dyson E.et.al.   2478533
[7] “The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane.”  Lee A.C.et.al.   9435273
[8] “Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase.”  Reinders J.et.al.   17761666
[9] “A multidimensional chromatography technology for in-depth phosphoproteome analysis.”  Albuquerque C.P.et.al.   18407956

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

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FASTA formatted sequence
1:	MSPPVYSDIS RNINDLLNKD FYHATPAAFD VQTTTANGIK FSLKAKQPVK DGPLSTNVEA 
61:	KLNDKQTGLG LTQGWSNTNN LQTKLEFANL TPGLKNELIT SLTPGVAKSA VLNTTFTQPF 
121:	FTARGAFDLC LKSPTFVGDL TMAHEGIVGG AEFGYDISAG SISRYAMALS YFAKDYSLGA 
181:	TLNNEQITTV DFFQNVNAFL QVGAKATMNC KLPNSNVNIE FATRYLPDAS SQVKAKVSDS 
241:	GIVTLAYKQL LRPGVTLGVG SSFDALKLSE PVHKLGWSLS FDA