Q60932 (VDAC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Voltage-dependent anion-selective channel protein 1
Short name=VDAC-1
Short name=mVDAC1

Alternative name(s):
Outer mitochondrial membrane protein porin 1
Plasmalemmal porin
Voltage-dependent anion-selective channel protein 5
Short name=VDAC-5
Short name=mVDAC5

Gene names

Name:	Vdac1
Synonyms:	Vdac5

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	296 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It 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. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. Ref.2 Ref.7 Ref.12
Subunit structure	Interacts with hexokinases By similarity. Interacts with BCL2L1 By similarity. Interacts with BOP (via BH3 domain) By similarity.
Subcellular location	Isoform Mt-VDAC1: Mitochondrion outer membrane; Multi-pass membrane protein Ref.2. Isoform Pl-VDAC1: Cell membrane; Multi-pass membrane protein Ref.2.
Tissue specificity	High levels of expression detected in heart, kidney, brain, and skeletal muscle. Not expressed in testis. Ref.1
Domain	Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands. The helical N-terminus folds back into the pore opening and plays a role in voltage-gated channel activity By similarity.
Sequence similarities	Belongs to the eukaryotic mitochondrial porin family.

Ontologies

Keywords
Biological process	Apoptosis Ion transport Transport
Cellular component	Cell membrane Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane beta strand
Ligand	NAD Nucleotide-binding
Molecular function	Porin
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW behavioral fear response Inferred from mutant phenotype PubMed 11907043. Source: MGI learning Inferred from mutant phenotype PubMed 11907043. Source: MGI neuron-neuron synaptic transmission Inferred from mutant phenotype PubMed 11907043. Source: MGI
Cellular_component	mitochondrial inner membrane Inferred from direct assay PubMed 12865426. Source: MGI mitochondrial nucleoid Inferred from electronic annotation. Source: Compara mitochondrial outer membrane Inferred from sequence orthology PubMed 17376863. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell pore complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW porin activity Inferred from electronic annotation. Source: UniProtKB-KW voltage-gated anion channel activity Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Pl-VDAC1 (identifier: Q60932-1)

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.

Isoform Mt-VDAC1 (identifier: Q60932-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.

Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2 (By similarity).

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 296

296

Voltage-dependent anion-selective channel protein 1

PRO_0000050500

Regions

Transmembrane

39 – 46

8

Beta stranded

Transmembrane

52 – 61

10

Beta stranded

Transmembrane

67 – 77

11

Beta stranded

Transmembrane

82 – 89

8

Beta stranded

Transmembrane

93 – 101

9

Beta stranded

Transmembrane

108 – 117

10

Beta stranded

Transmembrane

123 – 132

10

Beta stranded

Transmembrane

136 – 145

10

Beta stranded

Transmembrane

149 – 158

10

Beta stranded

Transmembrane

162 – 171

10

Beta stranded

Transmembrane

178 – 188

11

Beta stranded

Transmembrane

191 – 198

8

Beta stranded

Transmembrane

202 – 211

10

Beta stranded

Transmembrane

215 – 223

9

Beta stranded

Transmembrane

230 – 239

10

Beta stranded

Transmembrane

244 – 251

8

Beta stranded

Transmembrane

255 – 264

10

Beta stranded

Transmembrane

268 – 276

9

Beta stranded

Transmembrane

286 – 296

11

Beta stranded

Nucleotide binding

255 – 257

3

NAD By similarity

Nucleotide binding

273 – 277

5

NAD By similarity

Sites

Site

86

1

Involved in hexokinase binding By similarity

Amino acid modifications

Modified residue

14

1

N-acetylmethionine; in isoform Mt-VDAC1 By similarity

Modified residue

26

1

Phosphoserine By similarity

Modified residue

33

1

N6-acetyllysine Ref.8

Modified residue

41

1

N6-acetyllysine Ref.8

Modified residue

74

1

N6-acetyllysine Ref.8

Modified residue

80

1

Phosphotyrosine Ref.9

Modified residue

114

1

Phosphoserine By similarity

Modified residue

117

1

Phosphoserine Ref.10 Ref.11

Modified residue

150

1

Phosphoserine By similarity

Modified residue

208

1

Phosphotyrosine Ref.9

Modified residue

237

1

N6-acetyllysine Ref.8

Modified residue

279

1

N6-acetyllysine By similarity

Natural variations

Alternative sequence

1 – 13

13

Missing in isoform Mt-VDAC1.

VSP_005075

Secondary structure

1

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296

Helix Strand Turn

Details...

Helix

20 – 22

3

Helix

25 – 32

8

Beta strand

39 – 45

7

Beta strand

49 – 61

13

Turn

62 – 64

3

Beta strand

67 – 77

11

Turn

78 – 81

4

Beta strand

82 – 89

8

Beta strand

94 – 105

12

Beta strand

108 – 116

9

Turn

118 – 120

3

Beta strand

123 – 133

11

Beta strand

136 – 144

9

Beta strand

150 – 159

10

Beta strand

162 – 171

10

Turn

172 – 175

4

Beta strand

176 – 187

12

Beta strand

189 – 198

10

Turn

199 – 201

3

Beta strand

202 – 210

9

Beta strand

212 – 224

13

Beta strand

227 – 238

12

Beta strand

241 – 251

11

Beta strand

254 – 265

12

Beta strand

268 – 279

12

Turn

281 – 283

3

Beta strand

287 – 295

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform Pl-VDAC1 [UniParc]. Last modified December 1, 2000. Version 3. Checksum: C0710C1717063B32	FASTA	296	32,351
	10 20 30 40 50 60 MCSFFLVLLL WQNMAVPPTY ADLGKSARDV FTKGYGFGLI KLDLKTKSEN GLEFTSSGSA 70 80 90 100 110 120 NTETTKVNGS LETKYRWTEY GLTFTEKWNT DNTLGTEITV EDQLARGLKL TFDSSFSPNT 130 140 150 160 170 180 GKKNAKIKTG YKREHINLGC DVDFDIAGPS IRGALVLGYE GWLAGYQMNF ETSKSRVTQS 190 200 210 220 230 240 NFAVGYKTDE FQLHTNVNDG TEFGGSIYQK VNKKLETAVN LAWTAGNSNT RFGIAAKYQV 250 260 270 280 290 DPDACFSAKV NNSSLIGLGY TQTLKPGIKL TLSALLDGKN VNAGGHKLGL GLEFQA
	Isoform Mt-VDAC1 [UniParc]. Checksum: D32B05B8A8D75732	FASTA	283	30,756
	10 20 30 40 50 60 MAVPPTYADL GKSARDVFTK GYGFGLIKLD LKTKSENGLE FTSSGSANTE TTKVNGSLET 70 80 90 100 110 120 KYRWTEYGLT FTEKWNTDNT LGTEITVEDQ LARGLKLTFD SSFSPNTGKK NAKIKTGYKR 130 140 150 160 170 180 EHINLGCDVD FDIAGPSIRG ALVLGYEGWL AGYQMNFETS KSRVTQSNFA VGYKTDEFQL 190 200 210 220 230 240 HTNVNDGTEF GGSIYQKVNK KLETAVNLAW TAGNSNTRFG IAAKYQVDPD ACFSAKVNNS 250 260 270 280 SLIGLGYTQT LKPGIKLTLS ALLDGKNVNA GGHKLGLGLE FQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, characterization, and mapping of two mouse mitochondrial voltage-dependent anion channel isoforms." Sampson M.J., Lovell R.S., Craigen W.J. Genomics 33:283-288(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MT-VDAC1), TISSUE SPECIFICITY. Tissue: Brain.
[2]	"Evidence for secretory pathway localization of a voltage-dependent anion channel isoform." Buettner R., Papoutsoglou G., Scemes E., Spray D.C., Dermietzel R. Proc. Natl. Acad. Sci. U.S.A. 97:3201-3206(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS MT-VDAC1 AND PL-VDAC1), FUNCTION, SUBCELLULAR LOCATION.
[3]	"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] (ISOFORM MT-VDAC1). Strain: C57BL/6J and NOD. Tissue: Amnion, Embryonic kidney, Embryonic stomach and Thymus.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	"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] (ISOFORM MT-VDAC1). Strain: FVB/N. Tissue: Liver.
[6]	Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 34-41; 46-66; 77-106; 110-123; 134-174; 177-210; 214-231; 238-279 AND 288-296, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[7]	"Voltage-dependent anion channel-1 (VDAC-1) contributes to ATP release and cell volume regulation in murine cells." Okada S.F., O'Neal W.K., Huang P., Nicholas R.A., Ostrowski L.E., Craigen W.J., Lazarowski E.R., Boucher R.C. J. Gen. Physiol. 124:513-526(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-41; LYS-74 AND LYS-237, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-80 AND TYR-208, MASS SPECTROMETRY. Tissue: Brain.
[10]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, MASS SPECTROMETRY. Tissue: Brain cortex.
[11]	"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, MASS SPECTROMETRY. Tissue: Liver.
[12]	"The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating." Ujwal R., Cascio D., Colletier J.-P., Faham S., Zhang J., Toro L., Ping P., Abramson J. Proc. Natl. Acad. Sci. U.S.A. 105:17742-17747(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 14-296, FUNCTION, TOPOLOGY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U30840 mRNA. Translation: AAB47777.1.
AK168672 mRNA. Translation: BAE40522.1.
AK169671 mRNA. Translation: BAE41292.1.
AK169354 mRNA. Translation: BAE41103.1.
AK169282 mRNA. Translation: BAE41040.1.
AK169160 mRNA. Translation: BAE40939.1.
AL645589 Genomic DNA. Translation: CAI24939.1.
AL645589 Genomic DNA. Translation: CAM19812.1.
BC092257 mRNA. Translation: AAH92257.1.

IPI

IPI00122549.
IPI00230540.

RefSeq

NP_035824.1. NM_011694.4.

UniGene

Mm.3555.
Mm.470023.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EMN	X-ray	2.30	X	14-296	[»]

ProteinModelPortal

Q60932.

SMR

Q60932. Positions 14-296.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q60932. 7 interactions.

PTM databases

PhosphoSite

Q60932.

2D gel databases

REPRODUCTION-2DPAGE

Q60932.

SWISS-2DPAGE

Q60932.

Proteomic databases

PaxDb

Q60932.

PRIDE

Q60932.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000020673; ENSMUSP00000020673; ENSMUSG00000020402.
ENSMUST00000102758; ENSMUSP00000099819; ENSMUSG00000020402.

GeneID

22333.

KEGG

mmu:22333.

UCSC

uc007ivm.1. mouse.

Organism-specific databases

CTD

7416.

MGI

MGI:106919. Vdac1.

Phylogenomic databases

eggNOG

NOG243169.

GeneTree

ENSGT00390000011336.

HOGENOM

HOG000188277.

HOVERGEN

HBG054036.

InParanoid

B1ASZ9.

KO

K05862.

OMA

QKMAVPP.

Gene expression databases

ArrayExpress

Q60932.

Bgee

Q60932.

CleanEx

MM_VDAC1.

Genevestigator

Q60932.

GermOnline

ENSMUSG00000020402. Mus musculus.

Family and domain databases

Gene3D

2.40.160.10. 1 hit.

InterPro

IPR023614. Porin_dom.
IPR001925. Porin_Euk.
IPR027246. Porin_Euk/Tom40.
[Graphical view]

Pfam

PF01459. Porin_3. 1 hit.
[Graphical view]

PRINTS

PR00185. EUKARYTPORIN.

PROSITE

PS00558. EUKARYOTIC_PORIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

VDAC1. mouse.

EvolutionaryTrace

Q60932.

NextBio

302575.

SOURCE

Search...

Entry information

Entry name

VDAC1_MOUSE

Accession

Primary (citable) accession number: Q60932
Secondary accession number(s): B1ASZ9, Q5SVC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	December 1, 2000
Last modified:	April 3, 2013
This is version 112 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program