ID VDAC3_RABIT Reviewed; 283 AA.
AC Q9TT13;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Voltage-dependent anion-selective channel protein 3;
DE Short=VDAC-3;
DE AltName: Full=Outer mitochondrial membrane protein porin 3;
GN Name=VDAC3;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Cornea;
RA Rae J.L.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms a channel through the mitochondrial outer membrane that
CC allows diffusion of small hydrophilic molecules (By similarity).
CC Involved in male fertility and sperm mitochondrial sheath formation (By
CC similarity). {ECO:0000250|UniProtKB:P21796,
CC ECO:0000250|UniProtKB:Q60931}.
CC -!- SUBUNIT: Interacts with ARMC12 in a TBC1D21-dependent manner. Interacts
CC with MISFA. {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 -!- 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; AF209727; AAF22837.1; -; mRNA.
DR RefSeq; NP_001075545.1; NM_001082076.1.
DR AlphaFoldDB; Q9TT13; -.
DR SMR; Q9TT13; -.
DR STRING; 9986.ENSOCUP00000017992; -.
DR PaxDb; 9986-ENSOCUP00000017992; -.
DR GeneID; 100008752; -.
DR KEGG; ocu:100008752; -.
DR CTD; 7419; -.
DR eggNOG; KOG3126; Eukaryota.
DR HOGENOM; CLU_044399_2_0_1; -.
DR InParanoid; Q9TT13; -.
DR OMA; KGYHFGV; -.
DR OrthoDB; 2897965at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:GOC.
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 monoatomic anion channel activity; IEA:InterPro.
DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; IEA:Ensembl.
DR GO; GO:0120317; P:sperm mitochondrial sheath assembly; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd07306; Porin3_VDAC; 1.
DR Gene3D; 2.40.160.10; Porin; 1.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR001925; Porin_Euk.
DR InterPro; IPR027246; Porin_Euk/Tom40.
DR PANTHER; PTHR11743; VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL; 1.
DR PANTHER; PTHR11743:SF28; VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL PROTEIN 3; 1.
DR Pfam; PF01459; Porin_3; 1.
DR PRINTS; PR00185; EUKARYTPORIN.
DR PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; 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_0000050516"
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 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y277"
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: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"
SQ SEQUENCE 283 AA; 30652 MW; BC0C5616366090A0 CRC64;
MCNTPTYCDL GKAAKDVFNK GYGFGMVKID LRTKSCSGVE FSTSGHAYTD TGKASGNLET
KYKVCNYGLT FTQKWNTDNT LGTEISLENK LAEGLKLTLD TIFVPNTGKK SGKLKASYKR
DCFSLGSNVD IDFSGPTIYG WAVLAFEGWL AGYQMSFDTA KSKLSQNNFA LGYKAADFQL
HTHVNDGTEF GGSIYQKVNE KIETSINLAW TAGSNNTRFG IAAKYKLDCR TSLSAKVNNA
SLIGLGYTQT LRPGVKLTLS ALIDGKNFNA GGHKVGLGFE LEA
//
