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VDAC3_HUMAN
ID   VDAC3_HUMAN             Reviewed;         283 AA.
AC   Q9Y277; Q9UIS0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 190.
DE   RecName: Full=Voltage-dependent anion-selective channel protein 3;
DE            Short=VDAC-3;
DE            Short=hVDAC3;
DE   AltName: Full=Outer mitochondrial membrane protein porin 3;
GN   Name=VDAC3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=9781040; DOI=10.1038/sj.ejhg.5200198;
RA   Rahmani Z., Maunoury C., Siddiqui A.;
RT   "Isolation of a novel human voltage-dependent anion channel gene.";
RL   Eur. J. Hum. Genet. 6:337-340(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Umbilical cord blood;
RX   PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA   Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA   He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA   Wang Y.-X., Chen S.-J., Chen Z.;
RT   "Identification of genes expressed in human CD34(+) hematopoietic
RT   stem/progenitor cells by expressed sequence tags and efficient full-length
RT   cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-253.
RX   PubMed=10501981; DOI=10.1007/s003359901158;
RA   Decker W.K., Bowles K.R., Schatte E.C., Towbin J.A., Craigen W.J.;
RT   "Revised fine mapping of the human voltage-dependent anion channel loci by
RT   radiation hybrid analysis.";
RL   Mamm. Genome 10:1041-1042(1999).
RN   [5]
RP   ALTERNATIVE SPLICING.
RX   PubMed=10833333; DOI=10.1006/mgme.2000.2987;
RA   Decker W.K., Craigen W.J.;
RT   "The tissue-specific, alternatively spliced single ATG exon of the type 3
RT   voltage-dependent anion channel gene does not create a truncated protein
RT   isoform in vivo.";
RL   Mol. Genet. Metab. 70:69-74(2000).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-20 AND LYS-90, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   UBIQUITINATION AT LYS-53; LYS-61; LYS-109; LYS-110; LYS-163; LYS-266 AND
RP   LYS-274.
RX   PubMed=25621951; DOI=10.1038/ncb3097;
RA   Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
RA   Kirkpatrick D.S., Bingol B., Corn J.E.;
RT   "USP30 and parkin homeostatically regulate atypical ubiquitin chains on
RT   mitochondria.";
RL   Nat. Cell Biol. 17:160-169(2015).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [12]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=27641616; DOI=10.1038/srep33516;
RA   Marginedas-Freixa I., Hattab C., Bouyer G., Halle F., Chene A.,
RA   Lefevre S.D., Cambot M., Cueff A., Schmitt M., Gamain B., Lacapere J.J.,
RA   Egee S., Bihel F., Le Van Kim C., Ostuni M.A.;
RT   "TSPO ligands stimulate ZnPPIX transport and ROS accumulation leading to
RT   the inhibition of P. falciparum growth in human blood.";
RL   Sci. Rep. 6:33516-33516(2016).
CC   -!- FUNCTION: Forms a channel through the mitochondrial outer membrane that
CC       allows diffusion of small hydrophilic molecules.
CC       {ECO:0000250|UniProtKB:P21796}.
CC   -!- SUBUNIT: Interacts with ARMC12 in a TBC1D21-dependent manner (By
CC       similarity). {ECO:0000250|UniProtKB:Q60931}.
CC   -!- INTERACTION:
CC       Q9Y277; P21796: VDAC1; NbExp=2; IntAct=EBI-354196, EBI-354158;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P21796}. Membrane {ECO:0000269|PubMed:27641616}.
CC       Note=May localize to non-mitochondrial membranes.
CC       {ECO:0000269|PubMed:27641616}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y277-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y277-2; Sequence=VSP_005079;
CC   -!- TISSUE SPECIFICITY: Expressed in erythrocytes (at protein level)
CC       (PubMed:27641616). Widely expressed. Highest in testis
CC       (PubMed:9781040). {ECO:0000269|PubMed:27641616,
CC       ECO:0000269|PubMed:9781040}.
CC   -!- DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19
CC       beta-strands. {ECO:0000250|UniProtKB:P21796}.
CC   -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC       and enhancement of mitophagy. Deubiquitinated by USP30.
CC       {ECO:0000269|PubMed:25621951}.
CC   -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC       {ECO:0000305}.
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DR   EMBL; U90943; AAB93872.1; -; mRNA.
DR   EMBL; AF038962; AAC39876.1; -; mRNA.
DR   EMBL; BC056870; AAH56870.1; -; mRNA.
DR   EMBL; AH008073; AAD49610.1; -; Genomic_DNA.
DR   CCDS; CCDS47850.1; -. [Q9Y277-2]
DR   CCDS; CCDS6131.1; -. [Q9Y277-1]
DR   RefSeq; NP_001129166.1; NM_001135694.2. [Q9Y277-2]
DR   RefSeq; NP_005653.3; NM_005662.6. [Q9Y277-1]
DR   AlphaFoldDB; Q9Y277; -.
DR   SMR; Q9Y277; -.
DR   BioGRID; 113262; 309.
DR   IntAct; Q9Y277; 58.
DR   MINT; Q9Y277; -.
DR   STRING; 9606.ENSP00000428845; -.
DR   ChEMBL; CHEMBL4523505; -.
DR   DrugBank; DB01375; Aluminium monostearate.
DR   DrugBank; DB06098; PRLX 93936.
DR   GlyGen; Q9Y277; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y277; -.
DR   PhosphoSitePlus; Q9Y277; -.
DR   SwissPalm; Q9Y277; -.
DR   BioMuta; VDAC3; -.
DR   DMDM; 12643945; -.
DR   UCD-2DPAGE; Q9Y277; -.
DR   CPTAC; CPTAC-448; -.
DR   CPTAC; CPTAC-449; -.
DR   EPD; Q9Y277; -.
DR   jPOST; Q9Y277; -.
DR   MassIVE; Q9Y277; -.
DR   MaxQB; Q9Y277; -.
DR   PaxDb; Q9Y277; -.
DR   PeptideAtlas; Q9Y277; -.
DR   PRIDE; Q9Y277; -.
DR   ProteomicsDB; 85680; -. [Q9Y277-1]
DR   ProteomicsDB; 85681; -. [Q9Y277-2]
DR   Antibodypedia; 11458; 223 antibodies from 29 providers.
DR   DNASU; 7419; -.
DR   Ensembl; ENST00000022615.9; ENSP00000022615.4; ENSG00000078668.14. [Q9Y277-1]
DR   Ensembl; ENST00000521158.5; ENSP00000428845.1; ENSG00000078668.14. [Q9Y277-2]
DR   GeneID; 7419; -.
DR   KEGG; hsa:7419; -.
DR   MANE-Select; ENST00000022615.9; ENSP00000022615.4; NM_005662.7; NP_005653.3.
DR   UCSC; uc003xpc.4; human. [Q9Y277-1]
DR   CTD; 7419; -.
DR   DisGeNET; 7419; -.
DR   GeneCards; VDAC3; -.
DR   HGNC; HGNC:12674; VDAC3.
DR   HPA; ENSG00000078668; Group enriched (heart muscle, skeletal muscle, tongue).
DR   MIM; 610029; gene.
DR   neXtProt; NX_Q9Y277; -.
DR   OpenTargets; ENSG00000078668; -.
DR   PharmGKB; PA37297; -.
DR   VEuPathDB; HostDB:ENSG00000078668; -.
DR   eggNOG; KOG3126; Eukaryota.
DR   GeneTree; ENSGT00950000182869; -.
DR   HOGENOM; CLU_044399_2_0_1; -.
DR   InParanoid; Q9Y277; -.
DR   OMA; ITLTEKW; -.
DR   OrthoDB; 938262at2759; -.
DR   PhylomeDB; Q9Y277; -.
DR   TreeFam; TF315091; -.
DR   PathwayCommons; Q9Y277; -.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-8949215; Mitochondrial calcium ion transport.
DR   SignaLink; Q9Y277; -.
DR   BioGRID-ORCS; 7419; 34 hits in 1082 CRISPR screens.
DR   ChiTaRS; VDAC3; human.
DR   GeneWiki; VDAC3; -.
DR   GenomeRNAi; 7419; -.
DR   Pharos; Q9Y277; Tbio.
DR   PRO; PR:Q9Y277; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9Y277; protein.
DR   Bgee; ENSG00000078668; Expressed in Brodmann (1909) area 23 and 213 other tissues.
DR   ExpressionAtlas; Q9Y277; baseline and differential.
DR   Genevisible; Q9Y277; HS.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008308; F:voltage-gated anion channel activity; IBA:GO_Central.
DR   GO; GO:0015853; P:adenine transport; TAS:ProtInc.
DR   GO; GO:1902017; P:regulation of cilium assembly; IEA:InterPro.
DR   CDD; cd07306; Porin3_VDAC; 1.
DR   Gene3D; 2.40.160.10; -; 1.
DR   InterPro; IPR023614; Porin_dom_sf.
DR   InterPro; IPR001925; Porin_Euk.
DR   InterPro; IPR027246; Porin_Euk/Tom40.
DR   InterPro; IPR030271; VDAC3.
DR   PANTHER; PTHR11743; PTHR11743; 1.
DR   PANTHER; PTHR11743:SF28; PTHR11743:SF28; 1.
DR   Pfam; PF01459; Porin_3; 1.
DR   PRINTS; PR00185; EUKARYTPORIN.
DR   PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Ion transport; Isopeptide bond;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; NAD;
KW   Nucleotide-binding; Phosphoprotein; Porin; Reference proteome;
KW   Transmembrane; Transmembrane beta strand; Transport; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:25944712"
FT   CHAIN           2..283
FT                   /note="Voltage-dependent anion-selective channel protein 3"
FT                   /id="PRO_0000050512"
FT   TRANSMEM        26..35
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        39..47
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        54..64
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        69..76
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        80..89
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        95..104
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        111..120
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        123..130
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        137..145
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        150..158
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        163..175
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        178..185
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        189..198
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        202..211
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        218..227
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        231..238
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        242..251
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        254..263
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   TRANSMEM        273..282
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   BINDING         242..244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   BINDING         260..264
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21796"
FT   MOD_RES         2
FT                   /note="N-acetylcysteine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:25944712"
FT   MOD_RES         4
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60931"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60931"
FT   MOD_RES         20
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         90
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R1Z0"
FT   MOD_RES         266
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q60931"
FT   CROSSLNK        53
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:25621951"
FT   CROSSLNK        61
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:25621951"
FT   CROSSLNK        109
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:25621951"
FT   CROSSLNK        110
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:25621951"
FT   CROSSLNK        163
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:25621951"
FT   CROSSLNK        266
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000269|PubMed:25621951"
FT   CROSSLNK        274
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:25621951"
FT   VAR_SEQ         39
FT                   /note="V -> VM (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005079"
SQ   SEQUENCE   283 AA;  30659 MW;  E03CBCEDA72A9783 CRC64;
     MCNTPTYCDL GKAAKDVFNK GYGFGMVKID LKTKSCSGVE FSTSGHAYTD TGKASGNLET
     KYKVCNYGLT FTQKWNTDNT LGTEISWENK LAEGLKLTLD TIFVPNTGKK SGKLKASYKR
     DCFSVGSNVD IDFSGPTIYG WAVLAFEGWL AGYQMSFDTA KSKLSQNNFA LGYKAADFQL
     HTHVNDGTEF GGSIYQKVNE KIETSINLAW TAGSNNTRFG IAAKYMLDCR TSLSAKVNNA
     SLIGLGYTQT LRPGVKLTLS ALIDGKNFSA GGHKVGLGFE LEA
 
 
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