VDAC3_RAT
ID VDAC3_RAT Reviewed; 283 AA.
AC Q9R1Z0; Q6GSZ1; Q9ESR2; Q9JI31; Q9WTU2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Voltage-dependent anion-selective channel protein 3;
DE Short=VDAC-3;
DE Short=rVDAC3;
DE AltName: Full=Outer mitochondrial membrane protein porin 3;
GN Name=Vdac3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Ascitic tumor;
RX PubMed=10998068; DOI=10.1046/j.1432-1327.2000.01687.x;
RA Shinohara Y., Ishida T., Hino M., Yamazaki N., Baba Y., Terada H.;
RT "Characterization of porin isoforms expressed in tumor cells.";
RL Eur. J. Biochem. 267:6067-6073(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Lens;
RA Rae J.L.;
RT "Ion channels in the lens.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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 [MRNA] OF 10-283 (ISOFORMS 1 AND 2).
RC TISSUE=Heart;
RX PubMed=9714728; DOI=10.1016/s0167-4781(98)00088-8;
RA Anflous K., Blondel O., Bernard A., Khrestchatisky M., Ventura-Clapier R.;
RT "Characterization of rat porin isoforms: cloning of a cardiac type-3
RT variant encoding an additional methionine at its putative N-terminal
RT region.";
RL Biochim. Biophys. Acta 1399:47-50(1998).
RN [5]
RP PROTEIN SEQUENCE OF 29-34 AND 236-245, PHOSPHORYLATION AT THR-33 AND
RP SER-241, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=17478130; DOI=10.1016/j.bbapap.2007.03.012;
RA Distler A.M., Kerner J., Hoppel C.L.;
RT "Post-translational modifications of rat liver mitochondrial outer membrane
RT proteins identified by mass spectrometry.";
RL Biochim. Biophys. Acta 1774:628-636(2007).
RN [6]
RP PROTEIN SEQUENCE OF 54-63; 97-109 AND 257-266, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
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 -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P21796}. Membrane
CC {ECO:0000250|UniProtKB:Q9Y277}. Note=May localize to non-mitochondrial
CC membranes. {ECO:0000250|UniProtKB:Q9Y277}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=RVDAC3;
CC IsoId=Q9R1Z0-1; Sequence=Displayed;
CC Name=2; Synonyms=RVDAC3V;
CC IsoId=Q9R1Z0-2; Sequence=VSP_005080;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed with strong
CC expression in atrium and ascitic tumor, lower levels in brain and very
CC low levels in liver and kidney. Isoform 2 is also widely expressed with
CC highest levels in brain but no expression in kidney. Also expressed in
CC flagella of epididymal sperm. {ECO:0000269|PubMed:10998068,
CC ECO:0000269|PubMed:19423663}.
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:0000250|UniProtKB:Q9Y277}.
CC -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC {ECO:0000305}.
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DR EMBL; AB039664; BAB13475.1; -; mRNA.
DR EMBL; AF268469; AAF80117.1; -; mRNA.
DR EMBL; BC061780; AAH61780.1; -; mRNA.
DR EMBL; AF048829; AAD22722.1; -; mRNA.
DR EMBL; AF048830; AAD22723.1; -; mRNA.
DR RefSeq; NP_112645.1; NM_031355.1. [Q9R1Z0-1]
DR AlphaFoldDB; Q9R1Z0; -.
DR SMR; Q9R1Z0; -.
DR BioGRID; 249748; 5.
DR IntAct; Q9R1Z0; 3.
DR MINT; Q9R1Z0; -.
DR STRING; 10116.ENSRNOP00000046203; -.
DR CarbonylDB; Q9R1Z0; -.
DR iPTMnet; Q9R1Z0; -.
DR PhosphoSitePlus; Q9R1Z0; -.
DR SwissPalm; Q9R1Z0; -.
DR jPOST; Q9R1Z0; -.
DR PaxDb; Q9R1Z0; -.
DR PRIDE; Q9R1Z0; -.
DR DNASU; 83532; -.
DR GeneID; 83532; -.
DR KEGG; rno:83532; -.
DR UCSC; RGD:621577; rat. [Q9R1Z0-1]
DR CTD; 7419; -.
DR RGD; 621577; Vdac3.
DR eggNOG; KOG3126; Eukaryota.
DR InParanoid; Q9R1Z0; -.
DR OrthoDB; 938262at2759; -.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q9R1Z0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
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:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; ISO:RGD.
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; Direct protein sequencing;
KW Ion transport; Isopeptide bond; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; NAD; Nucleotide-binding; Phosphoprotein;
KW Porin; Reference proteome; Transmembrane; Transmembrane beta strand;
KW Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y277"
FT CHAIN 2..283
FT /note="Voltage-dependent anion-selective channel protein 3"
FT /id="PRO_0000050517"
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:0000250|UniProtKB:Q9Y277"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y277"
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:0000250|UniProtKB:Q9Y277"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17478130"
FT MOD_RES 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y277"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17478130"
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:0000250|UniProtKB:Q9Y277"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y277"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y277"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y277"
FT VAR_SEQ 39
FT /note="V -> VM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9714728"
FT /id="VSP_005080"
FT CONFLICT 128
FT /note="K -> N (in Ref. 2; AAF80117 and 3; AAH61780)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 30798 MW; 38002466B6557864 CRC64;
MCSTPTYCDL GKAAKDVFNK GYGFGMVKID LKTKSCSGVE FSTSGHAYTD TGKASGNLET
KYKVCNYGLI FTQKWNTDNT LGTEISWENK LAEGLKLTVD TIFVPNTGKK SGKLKASYRR
DCFSVGSKVD IDFSGPTIYG WAVLAFEGWL AGYQMSFDTA KSKLCQNNFA LGYKAEDFQL
HTHVNDGTEF GGSIYQRVNE KIETSINLAW TAGSNNTRFG IAAKYRLDCR TSLSAKVNNA
SLIGLGYTQS LRPGVKLTLS ALVDGKNFNA GGHKVGLGFE LEA
