VDAC2_RAT
ID VDAC2_RAT Reviewed; 295 AA.
AC P81155; Q9JI32;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Voltage-dependent anion-selective channel protein 2;
DE Short=VDAC-2;
DE AltName: Full=B36-VDAC;
DE AltName: Full=Outer mitochondrial membrane protein porin 2;
GN Name=Vdac2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 63-96 AND 190-203.
RC TISSUE=Hippocampus;
RX PubMed=1373732; DOI=10.1016/s0021-9258(18)42496-9;
RA Bureau M.H., Khrestchatisky M., Heeren M.A., Zambrowicz E.B., Kim H.,
RA Grisar T.M., Colombini M., Tobin A.J., Olsen R.W.;
RT "Isolation and cloning of a voltage-dependent anion channel-like Mr 36,000
RT polypeptide from mammalian brain.";
RL J. Biol. Chem. 267:8679-8684(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Ascitic tumor;
RX PubMed=10998068; DOI=10.1046/j.1432-1327.2000.01687.x;
RA Shinohara Y., Ishida T., Hino M., Yamazaki N., Baba Y., Terada H.;
RT "Characterization of porin isoforms expressed in tumor cells.";
RL Eur. J. Biochem. 267:6067-6073(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lens;
RA Rae J.L.;
RT "Ion channels in the lens.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 47-121; 179-230 AND 237-278, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 236-243, PHOSPHORYLATION AT TYR-237, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=17478130; DOI=10.1016/j.bbapap.2007.03.012;
RA Distler A.M., Kerner J., Hoppel C.L.;
RT "Post-translational modifications of rat liver mitochondrial outer membrane
RT proteins identified by mass spectrometry.";
RL Biochim. Biophys. Acta 1774:628-636(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Highly expressed in heart, kidney, brain and
CC ascitic tumor with very low levels in liver. Expressed in the head
CC region of epididymal sperm. {ECO:0000269|PubMed:10998068,
CC ECO:0000269|PubMed:19423663}.
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; AB039663; BAB13474.1; -; mRNA.
DR EMBL; AF268468; AAF80116.1; -; mRNA.
DR EMBL; BC063164; AAH63164.1; -; mRNA.
DR PIR; A38102; A38102.
DR RefSeq; NP_112644.1; NM_031354.1.
DR RefSeq; XP_006251723.1; XM_006251661.2.
DR AlphaFoldDB; P81155; -.
DR SMR; P81155; -.
DR BioGRID; 249747; 6.
DR IntAct; P81155; 6.
DR MINT; P81155; -.
DR STRING; 10116.ENSRNOP00000018462; -.
DR CarbonylDB; P81155; -.
DR iPTMnet; P81155; -.
DR PhosphoSitePlus; P81155; -.
DR SwissPalm; P81155; -.
DR World-2DPAGE; 0004:P81155; -.
DR jPOST; P81155; -.
DR PaxDb; P81155; -.
DR PRIDE; P81155; -.
DR GeneID; 83531; -.
DR KEGG; rno:83531; -.
DR UCSC; RGD:621576; rat.
DR CTD; 7417; -.
DR RGD; 621576; Vdac2.
DR VEuPathDB; HostDB:ENSRNOG00000013505; -.
DR eggNOG; KOG3126; Eukaryota.
DR HOGENOM; CLU_044399_2_0_1; -.
DR InParanoid; P81155; -.
DR OMA; PWSWRLN; -.
DR OrthoDB; 938262at2759; -.
DR PhylomeDB; P81155; -.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR PRO; PR:P81155; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000013505; Expressed in heart and 20 other tissues.
DR Genevisible; P81155; RN.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0006820; P:anion transport; ISO:RGD.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:RGD.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0032272; P:negative regulation of protein polymerization; ISO:RGD.
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 Lipid-binding; Membrane; Mitochondrion; Mitochondrion outer membrane; NAD;
KW Nucleotide-binding; Phosphoprotein; Porin; Reference proteome;
KW Transmembrane; Transmembrane beta strand; Transport; Ubl conjugation.
FT CHAIN 1..295
FT /note="Voltage-dependent anion-selective channel protein 2"
FT /id="PRO_0000050509"
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:P45880"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60930"
FT MOD_RES 79
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60932"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21796"
FT MOD_RES 121
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60930"
FT MOD_RES 237
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17478130"
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 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 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 CONFLICT 12
FT /note="P -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 31746 MW; 59582738AF84507F CRC64;
MAECCVPVCQ RPICIPPPYA 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
