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VDAC3_RABIT
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   03-AUG-2022, entry version 111.
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.
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   -!- 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   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; ITLTEKW; -.
DR   OrthoDB; 938262at2759; -.
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: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; IEA:InterPro.
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   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
 
 
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