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VDAC2_BOVIN
ID   VDAC2_BOVIN             Reviewed;         294 AA.
AC   P68002; Q5E9A2; Q9MYV7; Q9TT14;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   03-AUG-2022, entry version 117.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
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.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=11311949; DOI=10.1016/s0167-4781(01)00199-3;
RA   Hinsch K.-D., Asmarinah X., Hinsch E., Konrad L.;
RT   "VDAC2 (porin-2) expression pattern and localization in the bovine
RT   testis.";
RL   Biochim. Biophys. Acta 1518:329-333(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Kidney;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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; AF268465; AAF80102.1; -; mRNA.
DR   EMBL; AJ288914; CAB94711.2; -; mRNA.
DR   EMBL; BT021018; AAX09035.1; -; mRNA.
DR   EMBL; BC102904; AAI02905.1; -; mRNA.
DR   RefSeq; NP_776911.2; NM_174486.3.
DR   AlphaFoldDB; P68002; -.
DR   SMR; P68002; -.
DR   IntAct; P68002; 1.
DR   STRING; 9913.ENSBTAP00000017251; -.
DR   PaxDb; P68002; -.
DR   PeptideAtlas; P68002; -.
DR   PRIDE; P68002; -.
DR   Ensembl; ENSBTAT00000017251; ENSBTAP00000017251; ENSBTAG00000012975.
DR   GeneID; 282120; -.
DR   KEGG; bta:282120; -.
DR   CTD; 7417; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012975; -.
DR   VGNC; VGNC:36783; VDAC2.
DR   eggNOG; KOG3126; Eukaryota.
DR   GeneTree; ENSGT00950000182869; -.
DR   HOGENOM; CLU_044399_2_0_1; -.
DR   InParanoid; P68002; -.
DR   OMA; PWSWRLN; -.
DR   OrthoDB; 938262at2759; -.
DR   TreeFam; TF315091; -.
DR   Reactome; R-BTA-5689880; Ub-specific processing proteases.
DR   Proteomes; UP000009136; Chromosome 28.
DR   Bgee; ENSBTAG00000012975; Expressed in cardiac atrium and 105 other tissues.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:AgBase.
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; IBA:GO_Central.
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_0000050504"
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"
FT   CONFLICT        4
FT                   /note="Y -> H (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        7
FT                   /note="N -> T (in Ref. 1; AAF80102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        289
FT                   /note="A -> P (in Ref. 2; CAB94711)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   294 AA;  31620 MW;  C8660DEAB9F02E27 CRC64;
     MATYGQNCAR PMCIPPSYAD LGKAARDIFN KGFGFGLVKL DVKTKSCSGV EFSTSGSSNT
     DTGKVTGTLE TKYKWCEYGL TFTEKWNTDN TLGTEIAIED QICQGLKLTF DTTFSPNTGK
     KSGKIKSSYK RECINLGCDV DFDFAGPAIH GSAVFGYEGW LAGYQMTFDS AKSKLTRNNF
     AVGYRTGDFQ LHTNVNDGTE FGGSIYQKVC EDLDTSVNLA WTSGTNCTRF GIAAKYQLDP
     TASISAKVNN SSLIGVGYTQ TLRPGVKLTL SALVDGKSIN AGGHKLGLAL ELEA
 
 
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