Detail Information of Protein

Basic Information:

Symbol Vdac1
Synonyms Vdac5
Protein Name Voltage-dependent anion-selective channel protein 1 (VDAC-1) (mVDAC1) (Outer mitochondrial membrane protein porin 1) (Plasmalemmal porin) (Voltage-dependent anion-selective channel protein 5) (VDAC-5) (mVDAC5)
Species Mouse
Entrez ID 22333
Uniprot ID Q60932
Membrane Contact Site ER-MT; MT-ER
Location (from literature) MT
Cell line/Tissue C57BL6 mice; Mouse testes; Retinal ganglion cells; Mouse brains and retinas; RGCs; HRECs; Mouse livers; MEFs; Mouse T cell; C2C12 myoblasts
Experimental Method Low throughput experimental methods
Protein Sequence
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Complex Information:

Complex ID Subunit of complex Subcellular location Species More
CMCS00107 Itpr3; Hspa9; Vdac1; Park7 ER-MT; MT-ER Mouse more
CMCS00161 Tgm2; Vdac1; Itpr1; Hspa9 ER-MT; MT-ER Mouse more
CMCS00175 Vdac1; Itpr1; Hspa9 ER-MT; MT-ER Mouse more
CMCS00177 Vdac1; Gsk3b ER-MT; MT-ER Mouse more
CMCS00266 Itpr3; Hspa9; Vdac1; Pdk4 ER-MT; MT-ER Mouse more

Expression Overview of Vdac1:

Homology Information of Vdac1:

Uniprot ID Q60932
EggNOG KOG3126
HOGENOM CLU_044399_2_0_1
OrthoDB 2897965at2759
TreeFam TF315091
GeneTree ENSGT00950000182869

References:

Pubmed ID 31767755
DOI 10.1073/pnas.1906565116
Description DJ-1 regulates the integrity and function of ER-mitochondria association through interaction with IP3R3-GRP75-VDAC1.
Description of experimental evidence The protein was validated by western blotting, electron microscopy, co-immunoprecipitation assays, PLA, Blue-Native and SDS-PAGE 2D separation in C57BL6 mice, and suggests that impaired ER-mitochondria association could contribute to the pathogenesis of PD.
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Pubmed ID 29785746
DOI 10.1002/pmic.201700478
Description By Andromeda search engine against the decoy UniProt-mouse database and Swiss-Prot human database, which yielded 2,808 proteins from mouse testes (mT),2,478 proteins from mouse brain (mB) and 2,155 proteins from human testes (hT).
Description of experimental evidence The protein was validated by TEM and LC -MS/MS analyses in mouse testes.
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Pubmed ID 28522876
DOI 10.1038/s41598-017-02213-1
Description Using this method, 1313 non-redundant proteins were identified in the MAM.
Description of experimental evidence The protein was validated by proteomic analysis, long gradient nano-reverse-phase liquid chromatography, mass spectrometry and bioinformatics analysis in RGCs, HRECs, mouse brains and retinas.
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Pubmed ID 30590033
DOI 10.1016/j.celrep.2018.11.094
Description GRP75 localizes in mitochondria-associated membranes (MAMs) and acts as a bridging molecule between the two organelles by assembling the IP3R-GRP75-VDAC complex, which is involved in the transport of Ca2+ from the endoplasmic reticulum (ER) to mitochondria.
Description of experimental evidence The protein was validated by western blot analysis, Co-IP and PLA in mouse livers and MEFs.
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Pubmed ID 29523440
DOI 10.1016/j.immuni.2018.02.012
Description Rapid activation of Akt by mTORC2 led to inhibition of Gsk-3b at mitochondria-ER junctions, enabling recruitment of hexokinase I (HK-I) to the mitochondrial channel, VDAC.
Description of experimental evidence The protein was validated by metabolomics, flow cytometry, immunoblots, electron microscopy, proximity ligation assay and confocal imaging in neuronal mouse T cell, which underpins the metabolic reprogramming needed for memory CD8+ T cells to rapidly acquire effector function.
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Pubmed ID 24947355
DOI 10.2337/db13-1751
Description Mitochondria-associated endoplasmic reticulum (ER) membranes (MAMs) are functional domains between both organelles involved in Ca2+ exchange, through the voltage-dependent anion channel (VDAC)-1/glucose-regulated protein 75 (Grp75)/inositol 1,4,5-triphosphate receptor (IP3R)-1 complex, and regulating energy metabolism.
Description of experimental evidence The protein was validated by immunofluorescence, duolink II in situ PLA and western blot in mouse livers, which regulates energy metabolism.
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Pubmed ID 30523025
DOI 10.2337/db18-0363
Description Here, we demonstrate that PDK4 interacts with and stabilizes the IP3R1-GRP75-VDAC1 complex at the MAM interface.
Description of experimental evidence The protein was validated by in situ proximity ligation assay, immunofluorescence analysis, coimmunoprecipitation, transmission electron microscopy and immunoblotting in C2C12 myoblasts, which augments ER–Mitochondria contact to dampen skeletal muscle insulin signaling during obesity.
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Contact zhy1001@alu.uestc.edu.cn or yangzhang@cdutcm.edu.cn
© Department of Bioinformatics