VDAC2_PIG
ID VDAC2_PIG Reviewed; 294 AA.
AC Q9MZ15;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Voltage-dependent anion-selective channel protein 2;
DE Short=VDAC-2;
GN Name=VDAC2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RA Rae J.L.;
RT "Ion channels in the lens.";
RL Submitted (MAY-2000) 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). 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 promotes the
CC Binding of ceramide promotes the mitochondrial outer membrane
CC permeabilization (MOMP) apoptotic pathway (By similarity).
CC {ECO:0000250|UniProtKB:P45880}.
CC -!- SUBUNIT: Interacts with hexokinases (By similarity). Interacts with
CC ARMC12 in a TBC1D21-dependent manner (By similarity). Interacts with
CC KLC3 (By similarity). Interacts with SPATA33 (By similarity). Interacts
CC with PPP3CC in a SPATA33-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P21796, ECO:0000250|UniProtKB:Q60930}.
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}.
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 EMBL; AF268462; AAF78964.1; -; mRNA.
DR RefSeq; NP_999534.1; NM_214369.1.
DR AlphaFoldDB; Q9MZ15; -.
DR SMR; Q9MZ15; -.
DR STRING; 9823.ENSSSCP00000011005; -.
DR iPTMnet; Q9MZ15; -.
DR PeptideAtlas; Q9MZ15; -.
DR PRIDE; Q9MZ15; -.
DR GeneID; 397659; -.
DR KEGG; ssc:397659; -.
DR CTD; 7417; -.
DR eggNOG; KOG3126; Eukaryota.
DR InParanoid; Q9MZ15; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0097001; F:ceramide binding; ISS:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISS:UniProtKB.
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:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Ion transport; Isopeptide bond; Lipid-binding; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; NAD; Nucleotide-binding;
KW Phosphoprotein; Porin; Reference proteome; Transmembrane;
KW Transmembrane beta strand; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CHAIN 2..294
FT /note="Voltage-dependent anion-selective channel protein 2"
FT /id="PRO_0000050507"
FT TRANSMEM 37..46
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 50..58
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 65..75
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 80..87
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 91..100
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 106..115
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 122..131
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 134..141
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 148..156
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 161..169
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 174..186
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 189..196
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 200..209
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 213..222
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 229..238
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 242..249
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 265..274
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 284..293
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT BINDING 253..255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT BINDING 271..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT SITE 85
FT /note="Involved in ceramide and phosphatidylcholine
FT binding"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT MOD_RES 31
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT MOD_RES 31
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60930"
FT MOD_RES 78
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 120
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60930"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 277
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P45880"
SQ SEQUENCE 294 AA; 31593 MW; AB64322C28C724D3 CRC64;
MATHGQTCPR PMCIPPSYAD LGKAARDIFN KGFGFGLVKL DVKTKSCSGV EFSTSGSSNT
DTGKVTGTLE TKYKWCEYGL TFTEKWNTDN TLGTEIAIED QICQGLKLTF DTTFSPNTGK
KSGKIKSSYK RECVNLGCDV DFDFAGPAIH GSAVFGYEGW LAGYQMTFDS AKSKLTRNNF
AVGYRTGDFQ LHTNVNDGTE FGGSIYQKVC EDLDTSVNLA WTSGTNCTRF GIAAKYQLDP
TASISAKVNN SSLIGVGYTQ TLRPGVKLTL SALVDGKSIN AGGHKLGLAL ELEA
