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Overview

Uniprot IDP45880
Protein NameNon-selective voltage-gated ion channel VDAC2
Gene NameVDAC2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
120 TFSPNTGKKSGKIKS
121 FSPNTGKKSGKIKSS
277 LSALVDGKSINAGGH
31 AARDIFNKGFGFGLV
72 VTGTLETKYKWCEYG
74 GTLETKYKWCEYGLT

Function

Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane (PubMed:8420959). The channel adopts an open conformation at zero mV and a closed conformation at both positive and negative potentials (PubMed:8420959). There are two populations of channels; the main that functions in a lower open-state conductance with lower ion selectivity, that switch, in a voltage-dependent manner, from the open to a low-conducting 'closed' state and the other that has a normal ion selectivity in the typical high conductance, 'open' state (PubMed:8420959). Binds various lipids, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterols cholesterol and oxysterol (PubMed:31015432). Binding of ceramide promotes the mitochondrial outer membrane permeabilization (MOMP) apoptotic pathway (PubMed:31015432). Associates with the translocase of the outer mitochondrial membrane (TOM) complex and PINK1 kinase at depolarized mitochondria, this interaction stabilizes PINK1 at the outer mitochondrial membrane and triggers downstream mitophagy by the recruitment of the E3 ubiquitin ligase PRKN (PubMed:40080546)

Protein Sequence

10 MATHGQTCAR 20 PMCIPPSYAD 30 LGKAARDIFN 40 KGFGFGLVKL 50 DVKTKSCSGV 60 EFSTSGSSNT 70 DTGKVTGTLE 80 TKYKWCEYGL 90 TFTEKWNTDN 100 TLGTEIAIED 110 QICQGLKLTF 120 DTTFSPNTGK 130 KSGKIKSSYK 140 RECINLGCDV 150 DFDFAGPAIH 160 GSAVFGYEGW 170 LAGYQMTFDS 180 AKSKLTRNNF 190 AVGYRTGDFQ 200 LHTNVNDGTE 210 FGGSIYQKVC 220 EDLDTSVNLA 230 WTSGTNCTRF 240 GIAAKYQLDP 250 TASISAKVNN 260 SSLIGVGYTQ 270 TLRPGVKLTL 280 SALVDGKSIN 290 AGGHKVGLAL ELEA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0001669 acrosomal vesicle
Cellular Component GO:0016020 membrane
Cellular Component GO:0045121 membrane raft
Cellular Component GO:0031966 mitochondrial membrane
Cellular Component GO:0042645 mitochondrial nucleoid
Cellular Component GO:0005741 mitochondrial outer membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005634 nucleus
Cellular Component GO:0046930 pore complex
Cellular Component GO:0097225 sperm midpiece
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0097001 ceramide binding
Molecular Function GO:0015485 cholesterol binding
Molecular Function GO:0008142 oxysterol binding
Molecular Function GO:0031210 phosphatidylcholine binding
Molecular Function GO:0017128 phospholipid scramblase activity
Molecular Function GO:0015288 porin activity
Molecular Function GO:0008308 voltage-gated monoatomic anion channel activity
Molecular Function GO:0005244 voltage-gated monoatomic ion channel activity
Biological Process GO:0007339 binding of sperm to zona pellucida
Biological Process GO:0097345 mitochondrial outer membrane permeabilization
Biological Process GO:1990542 mitochondrial transmembrane transport
Biological Process GO:0006820 monoatomic anion transport
Biological Process GO:0045332 phospholipid translocation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[4] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.