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P04840 (VDAC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial outer membrane protein porin 1
Alternative name(s):
Voltage-dependent anion-selective channel protein 1
Short name=VDAC-1
Gene names
Name:POR1
Synonyms:OMP2, VDAC1
Ordered Locus Names:YNL055C
ORF Names:N2441, YNL2441C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules. The channel 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. Is the major permeability fator of the mitochondrial outer membrane. Ref.10

Subunit structure

Interacts with AIM5, FCJ1 and MOS1. Ref.14

Subcellular location

Mitochondrion outer membrane.

Domain

Consists mainly of membrane-spanning sided beta-sheets. 19 strands distributed along the entire VDAC protein, have the potential to adopt transmembrane beta pleated sheet structures, which rolled together may form a "beta-barrel" type structure, possessing pore dimensions.

Sequence similarities

Belongs to the eukaryotic mitochondrial porin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 283282Mitochondrial outer membrane protein porin 1
PRO_0000050524

Amino acid modifications

Modified residue1091Phosphoserine Ref.11 Ref.13
Modified residue1171Phosphothreonine Ref.12

Experimental info

Mutagenesis191K → E: 2.5-fold reduction in steepness of voltage dependence. Ref.9
Mutagenesis511D → K: 2-fold increase in steepness of voltage dependence. Ref.9
Mutagenesis611K → E: Alters the selectivity of VDAC. Ref.8
Sequence conflict1181Q → E Ref.1
Sequence conflict1181Q → E Ref.2
Sequence conflict203 – 2075GAKAT → AKATM in AAA35208. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P04840 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: C99D03711AF9B54D

FASTA28330,428
        10         20         30         40         50         60 
MSPPVYSDIS RNINDLLNKD FYHATPAAFD VQTTTANGIK FSLKAKQPVK DGPLSTNVEA 

        70         80         90        100        110        120 
KLNDKQTGLG LTQGWSNTNN LQTKLEFANL TPGLKNELIT SLTPGVAKSA VLNTTFTQPF 

       130        140        150        160        170        180 
FTARGAFDLC LKSPTFVGDL TMAHEGIVGG AEFGYDISAG SISRYAMALS YFAKDYSLGA 

       190        200        210        220        230        240 
TLNNEQITTV DFFQNVNAFL QVGAKATMNC KLPNSNVNIE FATRYLPDAS SQVKAKVSDS 

       250        260        270        280 
GIVTLAYKQL LRPGVTLGVG SSFDALKLSE PVHKLGWSLS FDA 

« Hide

References

« Hide 'large scale' references
[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., Sato R.
EMBO J. 4:769-774(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular genetics of the VDAC ion channel: structural model and sequence analysis."
Forte M.A., Guy H.R., Mannella C.A.
J. Bioenerg. Biomembr. 19:341-350(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The sequence of a 44 420 bp fragment located on the left arm of chromosome XIV from Saccharomyces cerevisiae."
Bergez P., Doignon F., Crouzet M.
Yeast 11:967-974(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S288c / FY1676.
[4]Erratum
Bergez P., Doignon F., Crouzet M.
Yeast 12:297-297(1996) [PubMed] [Europe PMC] [Abstract]
[5]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]Bienvenut W.V., Peters C.
Submitted (MAY-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-40; 45-108; 125-132; 165-174; 206-234 AND 237-274, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Probing the structure of the mitochondrial channel, VDAC, by site-directed mutagenesis: a progress report."
Blachly-Dyson E., Peng S.Z., Colombini M., Forte M.A.
J. Bioenerg. Biomembr. 21:471-483(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-61.
[9]"Probing for the voltage sensor of the VDAC ion channel by site-directed mutagenesis."
Thomas L., Blachly-Dyson E., Colombini M., Forte M.A.
Biophys. J. 59:215A-215A(1991)
Cited for: MUTAGENESIS OF LYS-19 AND ASP-51.
[10]"The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane."
Lee A.C., Xu X., Blachly-Dyson E., Forte M.A., Colombini M.
J. Membr. Biol. 161:173-181(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[12]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria."
Hoppins S., Collins S.R., Cassidy-Stone A., Hummel E., Devay R.M., Lackner L.L., Westermann B., Schuldiner M., Weissman J.S., Nunnari J.
J. Cell Biol. 195:323-340(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AIM5; FCJ1 AND MOS1.
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02324 mRNA. Translation: CAA26184.1.
M34907 mRNA. Translation: AAA35208.1.
U12141 Genomic DNA. Translation: AAA99656.1.
Z71331 Genomic DNA. Translation: CAA95926.1.
BK006947 Genomic DNA. Translation: DAA10489.1.
PIRMMBYP. S58721.
RefSeqNP_014343.1. NM_001182894.1.

3D structure databases

ProteinModelPortalP04840.
SMRP04840. Positions 3-283.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35766. 190 interactions.
DIPDIP-6453N.
IntActP04840. 68 interactions.
MINTMINT-677066.
STRING4932.YNL055C.

Protein family/group databases

TCDB1.B.8.1.1. the mitochondrial and plastid porin (mpp) family.

2D gel databases

UCD-2DPAGEP04840.

Proteomic databases

PaxDbP04840.
PeptideAtlasP04840.

Protocols and materials databases

DNASU855669.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL055C; YNL055C; YNL055C.
GeneID855669.
KEGGsce:YNL055C.

Organism-specific databases

SGDS000005000. POR1.

Phylogenomic databases

eggNOGNOG243169.
GeneTreeENSGT00390000011336.
HOGENOMHOG000188277.
KOK15040.
OMAYGLMFTE.
OrthoDBEOG7GXPNQ.

Enzyme and pathway databases

BioCycYEAST:G3O-33087-MONOMER.
ReactomeREACT_118590. Mitochondrial Protein Import (yeast).
REACT_85873. Metabolism of proteins.

Gene expression databases

GenevestigatorP04840.

Family and domain databases

Gene3D2.40.160.10. 1 hit.
InterProIPR023614. Porin_dom.
IPR001925. Porin_Euk.
IPR027246. Porin_Euk/Tom40.
[Graphical view]
PfamPF01459. Porin_3. 1 hit.
[Graphical view]
PRINTSPR00185. EUKARYTPORIN.
PROSITEPS00558. EUKARYOTIC_PORIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979947.

Entry information

Entry nameVDAC1_YEAST
AccessionPrimary (citable) accession number: P04840
Secondary accession number(s): D6W1C3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 133 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families