VDAC2_XENLA
ID VDAC2_XENLA Reviewed; 282 AA.
AC P81004;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Voltage-dependent anion-selective channel protein 2;
DE Short=VDAC-2;
DE AltName: Full=Outer mitochondrial membrane protein porin;
GN Name=vdac2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP PROTEIN SEQUENCE.
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).
RN [2]
RP PROTEIN SEQUENCE OF 84-90 AND 274-282, ACETYLATION AT ALA-1, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Oocyte;
RX PubMed=10687956; DOI=10.1016/s1357-2725(99)00124-7;
RA Steinacker P., Awni L.A., Becker S., Cole T., Reymann S., Hesse D.,
RA Kratzin H.D., Morris-Wortmann C., Schwarzer C., Thinnes F.P.,
RA Hilschmann N.;
RT "The plasma membrane of Xenopus laevis oocytes contains voltage-dependent
RT anion-selective porin channels.";
RL Int. J. Biochem. Cell Biol. 32:225-234(2000).
CC -!- FUNCTION: Forms a channel through the mitochondrial outer membrane that
CC allows diffusion of small hydrophilic molecules. The channel adopts an
CC open conformation at low or zero membrane potential and a closed
CC conformation at potentials above 30-40 mV. The open state has a weak
CC anion selectivity whereas the closed state is cation-selective (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with hexokinases. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle and oocytes.
CC {ECO:0000269|PubMed:10687956}.
CC -!- DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed by 19
CC beta-strands. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P81004; -.
DR SMR; P81004; -.
DR iPTMnet; P81004; -.
DR Proteomes; UP000186698; Genome assembly.
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 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; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; NAD; Nucleotide-binding;
KW Porin; Reference proteome; Transmembrane; Transmembrane beta strand;
KW Transport.
FT CHAIN 1..282
FT /note="Voltage-dependent anion-selective channel protein 2"
FT /id="PRO_0000050518"
FT TRANSMEM 25..34
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 38..46
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 53..63
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 68..75
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 79..88
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 94..103
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..119
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 122..129
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 136..144
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 149..157
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 162..174
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 177..184
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 188..197
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 201..210
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 217..226
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 230..237
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 241..250
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 253..262
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TRANSMEM 272..281
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT BINDING 241..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 259..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 72
FT /note="Involved in hexokinase binding"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:10687956"
SQ SEQUENCE 282 AA; 30071 MW; B0309215D81FF313 CRC64;
AVPPSYADLG KSARDIFNKG YGFGLVKLDV KTKSATGVEF TTSGTSNTDS GKVNGSLETK
YKWGEYGLTF TEKWNTDNTL GTEIAIEDQI AKGLKLTFDT TFSPNTGKKS GKVKAAYKQE
YVNLGCDVDF DFAGPAIHGS AVVGYEGWLA GYQMTFDSAK SKLTKNNFAV GYKTGDFQLH
TNVNDGSEFA GSIYQKVSDK METAVNLAWT SGNNSTRFGI AAKYQLDSHA AISAKVNNSS
LVGVGYTQTL RPGVKLTLSA LVDGKNINAG GHKLGLGLEL EA
