VDAC2_MELGA
ID VDAC2_MELGA Reviewed; 282 AA.
AC P82013;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Voltage-dependent anion-selective channel protein 2;
DE Short=VDAC-2;
DE AltName: Full=Outer mitochondrial membrane protein porin 2;
GN Name=VDAC2;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Skeletal muscle;
RA Hesse D., Strutz N., Kratzin H.D., Thinnes F.P., Hilschmann N.;
RL Submitted (SEP-1999) to UniProtKB.
RN [2]
RP PROTEIN SEQUENCE OF 20-27; 34-60; 74-92; 96-108; 166-173; 218-223; 256-265
RP AND 274-282.
RC TISSUE=Skeletal muscle {ECO:0000303|PubMed:10527528};
RX PubMed=10527528; DOI=10.1006/abio.1999.4265;
RA Reymann S., Kiafard Z., Rohm B., Strutz N., Hesse D., Kratzin H.D.,
RA Zimmermann B., Thinnes F.P., Hilschmann N.;
RT "Purification procedure and monoclonal antibodies: two instruments for
RT research on vertebrate porins.";
RL Anal. Biochem. 274:289-295(1999).
CC -!- FUNCTION: Forms a channel through the mitochondrial outer membrane that
CC allows diffusion of small hydrophilic molecules (By similarity). The
CC channel adopts an open conformation at low or zero membrane potential
CC and a closed conformation at potentials above 30-40 mV (By similarity).
CC The open state has a weak anion selectivity whereas the closed state is
CC cation-selective (By similarity). Binds various lipids, including the
CC sphingolipid ceramide, the phospholipid phosphatidylcholine, and the
CC sterol cholesterol (By similarity). Binding of ceramide may be required
CC to trigger the Binding of ceramide promotes the mitochondrial outer
CC membrane permeabilization (MOMP) apoptotic pathway (By similarity).
CC {ECO:0000250|UniProtKB:P45880}.
CC -!- SUBUNIT: Interacts with hexokinases (By similarity).
CC {ECO:0000250|UniProtKB:P21796}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P45880}. Membrane
CC {ECO:0000250|UniProtKB:P45880}. Note=May localize to non-mitochondrial
CC membranes. {ECO:0000250|UniProtKB:P45880}.
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:P45880}.
CC -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P82013; -.
DR SMR; P82013; -.
DR InParanoid; P82013; -.
DR Proteomes; UP000001645; Unplaced.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS: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; 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; IPR030277; VDAC2.
DR PANTHER; PTHR11743; PTHR11743; 1.
DR PANTHER; PTHR11743:SF12; PTHR11743:SF12; 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; Direct protein sequencing; 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 CHAIN 1..282
FT /note="Voltage-dependent anion-selective channel protein 2"
FT /id="PRO_0000050510"
FT TRANSMEM 25..34
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 38..46
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 53..63
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 68..75
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 79..88
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 94..103
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 110..119
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 122..129
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 136..144
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 149..157
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 162..174
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 177..184
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 188..197
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 201..210
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 217..226
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 230..237
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 241..250
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 253..262
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 272..281
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT BINDING 241..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT BINDING 259..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT SITE 72
FT /note="Critical for channel structural stability and
FT gating"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT SITE 72
FT /note="Involved in ceramide and phosphatidylcholine
FT binding"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 108
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 265
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21796"
SQ SEQUENCE 282 AA; 30067 MW; 88ECCF19ABCA004F CRC64;
AIPPSYADLG KSARDIFNKG YGFGLVKLDV KTKSASGVEF TTSGSSNTDT GKVNGSLETK
YKWAEYGLTF TEKWNTDNTL GTEIAIEDQI AKGLKLTFDT TFSPNTGKKS GKIKSAYKRE
CLNLGCDVDF DFAGPAIHGS AVFGYEGWLA GYQMTFDSAK SKLTRNNFSV GYKTGDFQLH
TNVNDGSEFG GSIYQKVSDN LETAVNLAWT AGSNSTRFGI AAKYKLDSTA SISAKVNNSS
LVGVGYTQTL RPGVKLTLSA LIDGKSINAG GHKLGLGLEL EA
