VDAC2_MESAU
ID VDAC2_MESAU Reviewed; 295 AA.
AC P86223; A0A1U7R165;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Voltage-dependent anion-selective channel protein 2 {ECO:0000250|UniProtKB:P45880};
DE Short=VDAC-2 {ECO:0000250|UniProtKB:P45880};
DE AltName: Full=Outer mitochondrial membrane protein porin 2 {ECO:0000250|UniProtKB:P45880};
GN Name=VDAC2 {ECO:0000250|UniProtKB:P45880};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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). 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|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:0000255}.
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DR RefSeq; XP_005083579.1; XM_005083522.2.
DR AlphaFoldDB; P86223; -.
DR SMR; P86223; -.
DR STRING; 10036.XP_005083579.1; -.
DR GeneID; 101826831; -.
DR CTD; 7417; -.
DR eggNOG; KOG3126; Eukaryota.
DR OrthoDB; 938262at2759; -.
DR Proteomes; UP000189706; 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.
PE 1: Evidence at protein 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 CHAIN 1..295
FT /note="Voltage-dependent anion-selective channel protein 2"
FT /id="PRO_0000394307"
FT TRANSMEM 38..47
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 51..59
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 66..76
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 81..88
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 92..101
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 107..116
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 123..132
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 135..142
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..170
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 175..187
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 190..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 214..223
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 230..239
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 243..250
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 266..275
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT TRANSMEM 285..294
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT BINDING 254..256
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT BINDING 272..276
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 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60930"
FT MOD_RES 121
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60930"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 278
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 73
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P45880"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P45880"
SQ SEQUENCE 295 AA; 31770 MW; 4E72B45EEFF6B7EE CRC64;
MADCCVRTCP RPMCIPPSYA DLGKAARDIF NKGFGFGLVK LDVKTKSCSG VEFSTSGSSN
TDTGKVSGTL ETKYKWCEYG LTFTEKWNTD NTLGTEIAIE DQICQGLKLT FDTTFSPNTG
KKSGKIKSAY KRECINLGCD VDFDFAGPAI HGSAVFGYEG WLAGYQMTFD SAKSKLTRSN
FAVGYRTGDF QLHTNVNNGT EFGGSIYQKV CEDFDTSVNL AWTSGTNCTR FGIAAKYQLD
PTASISAKVN NSSLIGVGYT QTLRPGVKLT LSALVDGKSF NAGGHKLGLA LELEA
