[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1038/sj.ejhg.5200198; PubMed=9781040 [NCBI, ExPASy, EBI, Israel, Japan] Rahmani Z., Maunoury C., Siddiqui A.; "Isolation of a novel human voltage-dependent anion channel gene."; Eur. J. Hum. Genet. 6:337-340(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Umbilical cord blood; DOI=10.1073/pnas.95.14.8175; PubMed=9653160 [NCBI, ExPASy, EBI, Israel, Japan] Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.; "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."; Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-253. DOI=10.1007/s003359901158; PubMed=10501981 [NCBI, ExPASy, EBI, Israel, Japan] Decker W.K., Bowles K.R., Schatte E.C., Towbin J.A., Craigen W.J.; "Revised fine mapping of the human voltage-dependent anion channel loci by radiation hybrid analysis."; Mamm. Genome 10:1041-1042(1999).
[5]	ALTERNATIVE SPLICING. DOI=10.1006/mgme.2000.2987; PubMed=10833333 [NCBI, ExPASy, EBI, Israel, Japan] Decker W.K., Craigen W.J.; "The tissue-specific, alternatively spliced single ATG exon of the type 3 voltage-dependent anion channel gene does not create a truncated protein isoform in vivo."; Mol. Genet. Metab. 70:69-74(2000).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195, AND MASS SPECTROMETRY. DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan] Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.; "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; Nat. Biotechnol. 23:94-101(2005).

Comments

FUNCTION: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (By similarity).
INTERACTION:
P49662:CASP4; NbExp=1; IntAct=EBI-354196, EBI-1057327;
SUBCELLULAR LOCATION: Mitochondrion outer membrane.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name 1

Isoform ID Q9Y277-1

This is the isoform sequence displayed in this entry.

Name 2

Isoform ID Q9Y277-2

Features which should be applied to build the isoform sequence: VSP_005079.
TISSUE SPECIFICITY: Widely expressed. Highest in testis.
DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands (By similarity).
SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U90943; AAB93872.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF038962; AAC39876.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC056870; AAH56870.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151682; AAD49610.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151679; AAD49610.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151681; AAD49610.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001129166.1; -.
NP_005653.3; -.

UniGene

Hs.655340

3D structure databases

ModBase

Q9Y277.

Protein-protein interaction databases

IntAct

Q9Y277; 9.

PTM databases

PhosphoSite

Q9Y277; -.

Organism-specific databases

GC08P042368; -.

HIX0007479; -.

HGNC:12674; VDAC3.

610029; gene. [NCBI / EBI]

PharmGKB

PA37297; -.

GeneCards

Q9Y277.

Gene expression databases

ArrayExpress

Q9Y277; -.

CleanEx

HS_VDAC3; -.

GermOnline

ENSG00000078668; Homo sapiens.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005741;	Cellular component: mitochondrial outer membrane (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008308;	Molecular function: voltage-gated anion channel activity (traceable author statement from UniProtKB).
GO:0015853;	Biological process: adenine transport (traceable author statement from ProtInc).
GO:0006820;	Biological process: anion transport (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001925; Porin_Euk.
Graphical view of domain structure.

Pfam

PF01459; Porin_3; 1.
Pfam graphical view of domain structure.

PRINTS

PR00185; EUKARYTPORIN.

PROSITE

PS00558; EUKARYOTIC_PORIN; 1.

Proteomic databases

PeptideAtlas

Q9Y277; -.

Proteomics databases

PRIDE

Q9Y277; -.

Genome annotation databases

Ensembl

ENSG00000078668; Homo sapiens. [Contig view]

GeneID

7419; -.

KEGG

hsa:7419; -.

Phylogenomic databases

HOGENOM

Q9Y277; -.

HOVERGEN

Q9Y277; -.

Other

DrugBank

DB01375; Dihydroxyaluminium.

Q9Y277; -.

29048; -.

VDAC3; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Alternative splicing; Ion transport; Membrane; Mitochondrion; Mitochondrion outer membrane; NAD; Nucleotide-binding; Phosphoprotein; Porin; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 283`	`283`	`Voltage-dependent anion-selective channel protein 3.`	`PRO_0000050512`
`TRANSMEM`	`26 35`	`10`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`39 47`	`9`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`54 64`	`11`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`69 76`	`8`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`80 89`	`10`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`95 104`	`10`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`111 120`	`10`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`123 130`	`8`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`137 145`	`9`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`150 158`	`9`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`163 175`	`13`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`178 185`	`8`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`189 198`	`10`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`202 211`	`10`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`218 227`	`10`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`231 238`	`8`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`242 251`	`10`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`254 263`	`10`	`Transmembrane beta-strand (By similarity).`
`TRANSMEM`	`273 282`	`10`	`Transmembrane beta-strand (By similarity).`
`NP_BIND`	`242 244`	`3`	`NAD (By similarity).`
`NP_BIND`	`260 264`	`5`	`NAD (By similarity).`
`MOD_RES`	`20 20`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`33 33`		`Phosphothreonine (By similarity).`
`MOD_RES`	`48 48`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`61 61`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`195 195`		`Phosphotyrosine.`
`MOD_RES`	`241 241`		`Phosphoserine (By similarity).`
`VAR_SEQ`	`39 39`		`V -> VM (in isoform 2).`	`VSP_005079`

Sequence information

Length: 283 AA [This is the length of the unprocessed precursor]

Molecular weight: 30659 Da [This is the MW of the unprocessed precursor]

CRC64: E03CBCEDA72A9783 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MCNTPTYCDL GKAAKDVFNK GYGFGMVKID LKTKSCSGVE FSTSGHAYTD TGKASGNLET 

        70         80         90        100        110        120 
KYKVCNYGLT FTQKWNTDNT LGTEISWENK LAEGLKLTLD TIFVPNTGKK SGKLKASYKR 

       130        140        150        160        170        180 
DCFSVGSNVD IDFSGPTIYG WAVLAFEGWL AGYQMSFDTA KSKLSQNNFA LGYKAADFQL 

       190        200        210        220        230        240 
HTHVNDGTEF GGSIYQKVNE KIETSINLAW TAGSNNTRFG IAAKYMLDCR TSLSAKVNNA 

       250        260        270        280 
SLIGLGYTQT LRPGVKLTLS ALIDGKNFSA GGHKVGLGFE LEA

Q9Y277 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools