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Protein

Voltage-dependent anion-selective channel protein 3

Gene

Vdac3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules.By similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

  • behavioral fear response Source: MGI
  • learning Source: MGI
  • neuron-neuron synaptic transmission Source: MGI
  • regulation of cilium assembly Source: InterPro
  • synaptic transmission Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Porin

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

NAD, Nucleotide-binding

Protein family/group databases

TCDBi1.B.8.1.2. the mitochondrial and plastid porin (mpp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent anion-selective channel protein 3
Short name:
VDAC-3
Short name:
mVDAC3
Alternative name(s):
Outer mitochondrial membrane protein porin 3
Gene namesi
Name:Vdac3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:106922. Vdac3.

Subcellular locationi

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

  • extracellular exosome Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • nucleus Source: MGI
  • pore complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 283282Voltage-dependent anion-selective channel protein 3PRO_0000050513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylcysteineCombined sources
Modified residuei12 – 121N6-acetyllysineCombined sources
Modified residuei15 – 151N6-acetyllysineCombined sources
Modified residuei20 – 201N6-acetyllysine; alternateCombined sources
Modified residuei20 – 201N6-succinyllysine; alternateBy similarity
Cross-linki53 – 53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki61 – 61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei67 – 671PhosphotyrosineBy similarity
Modified residuei90 – 901N6-acetyllysineCombined sources
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-linki163 – 163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei241 – 2411PhosphoserineBy similarity
Modified residuei266 – 2661N6-acetyllysine; alternateCombined sources
Cross-linki266 – 266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki274 – 274Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

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

EPDiQ60931.
MaxQBiQ60931.
PaxDbiQ60931.
PRIDEiQ60931.

PTM databases

iPTMnetiQ60931.
PhosphoSiteiQ60931.
SwissPalmiQ60931.

Expressioni

Tissue specificityi

Highest levels of expression detected in testis, less but still abundant expression in heart, kidney, brain, and skeletal muscle.

Gene expression databases

BgeeiQ60931.
CleanExiMM_VDAC3.
ExpressionAtlasiQ60931. baseline.
GenevisibleiQ60931. MM.

Interactioni

Protein-protein interaction databases

BioGridi204509. 3 interactions.
IntActiQ60931. 6 interactions.
MINTiMINT-1858022.
STRINGi10090.ENSMUSP00000009036.

Structurei

3D structure databases

ProteinModelPortaliQ60931.
SMRiQ60931. Positions 1-283.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiKOG3126. Eukaryota.
ENOG410ZBK1. LUCA.
GeneTreeiENSGT00390000011336.
HOGENOMiHOG000188277.
HOVERGENiHBG054036.
InParanoidiQ60931.
KOiK15041.
OrthoDBiEOG7P8P8G.
PhylomeDBiQ60931.

Family and domain databases

Gene3Di2.40.160.10. 1 hit.
InterProiIPR023614. Porin_dom.
IPR001925. Porin_Euk.
IPR027246. Porin_Euk/Tom40.
IPR030271. VDAC3.
[Graphical view]
PANTHERiPTHR11743:SF28. PTHR11743:SF28. 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.

Q60931-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCNTPTYCDL GKAAKDVFNK GYGFGMVKID LKTKSCSGVE FSTSGHAYTD
60 70 80 90 100
TGKASGNLET KYKVCNYGLT FTQKWNTDNT LGTEISWENK LAEGLKLTLD
110 120 130 140 150
TIFVPNTGKK SGKLKASYRR DCFSLGSNVD IDFSGPTIYG WAVLAFEGWL
160 170 180 190 200
AGYQMSFDTA KSKLSQNNFA LGYKAADFQL HTHVNDGTEF GGSIYQKVNE
210 220 230 240 250
RIETSINLAW TAGSNNTRFG IAAKYKLDCR TSLSAKVNNA SLIGLGYTQT
260 270 280
LRPGVKLTLS ALIDGKNFNA GGHKVGLGFE LEA
Length:283
Mass (Da):30,753
Last modified:November 1, 1996 - v1
Checksum:iA95AFD67C611228C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391V → VM in BAC39019 (PubMed:16141072).Curated
Sequence conflicti174 – 1741K → E in BAC39019 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30839 mRNA. Translation: AAB47776.1.
AK083785 mRNA. Translation: BAC39019.1.
BC004743 mRNA. Translation: AAH04743.1.
CCDSiCCDS22179.1.
RefSeqiNP_035826.1. NM_011696.2.
UniGeneiMm.227704.

Genome annotation databases

EnsembliENSMUST00000009036; ENSMUSP00000009036; ENSMUSG00000008892.
GeneIDi22335.
KEGGimmu:22335.
UCSCiuc012gbf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30839 mRNA. Translation: AAB47776.1.
AK083785 mRNA. Translation: BAC39019.1.
BC004743 mRNA. Translation: AAH04743.1.
CCDSiCCDS22179.1.
RefSeqiNP_035826.1. NM_011696.2.
UniGeneiMm.227704.

3D structure databases

ProteinModelPortaliQ60931.
SMRiQ60931. Positions 1-283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204509. 3 interactions.
IntActiQ60931. 6 interactions.
MINTiMINT-1858022.
STRINGi10090.ENSMUSP00000009036.

Protein family/group databases

TCDBi1.B.8.1.2. the mitochondrial and plastid porin (mpp) family.

PTM databases

iPTMnetiQ60931.
PhosphoSiteiQ60931.
SwissPalmiQ60931.

Proteomic databases

EPDiQ60931.
MaxQBiQ60931.
PaxDbiQ60931.
PRIDEiQ60931.

Protocols and materials databases

DNASUi22335.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000009036; ENSMUSP00000009036; ENSMUSG00000008892.
GeneIDi22335.
KEGGimmu:22335.
UCSCiuc012gbf.1. mouse.

Organism-specific databases

CTDi7419.
MGIiMGI:106922. Vdac3.

Phylogenomic databases

eggNOGiKOG3126. Eukaryota.
ENOG410ZBK1. LUCA.
GeneTreeiENSGT00390000011336.
HOGENOMiHOG000188277.
HOVERGENiHBG054036.
InParanoidiQ60931.
KOiK15041.
OrthoDBiEOG7P8P8G.
PhylomeDBiQ60931.

Miscellaneous databases

PROiQ60931.
SOURCEiSearch...

Gene expression databases

BgeeiQ60931.
CleanExiMM_VDAC3.
ExpressionAtlasiQ60931. baseline.
GenevisibleiQ60931. MM.

Family and domain databases

Gene3Di2.40.160.10. 1 hit.
InterProiIPR023614. Porin_dom.
IPR001925. Porin_Euk.
IPR027246. Porin_Euk/Tom40.
IPR030271. VDAC3.
[Graphical view]
PANTHERiPTHR11743:SF28. PTHR11743:SF28. 1 hit.
PfamiPF01459. Porin_3. 1 hit.
[Graphical view]
PRINTSiPR00185. EUKARYTPORIN.
PROSITEiPS00558. EUKARYOTIC_PORIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8."
    Sampson M.J., Lovell R.S., Davison D.B., Craigen W.J.
    Genomics 36:192-196(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Spinal ganglion.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 257-266, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2; LYS-12 AND LYS-20, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-20; LYS-90 AND LYS-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiVDAC3_MOUSE
AccessioniPrimary (citable) accession number: Q60931
Secondary accession number(s): Q8BNG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.