Protein Name:
ADP/ATP translocase 2
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UniprotKB/SwissProt ID: P51881 (P51881)
Gene Name:
Slc25a5
Organism: Mus musculus (Mouse)
Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:31341297). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity (PubMed:31341297, PubMed:31489369). Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis (PubMed:31341297). Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A5/ANT2 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity) (PubMed:31341297). Proton transporter activity requires free fatty acids as cofactor, but does not transport it (PubMed:31341297). Probably mediates mitochondrial uncoupling in tissues that do not express UCP1 (PubMed:31341297). Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death (PubMed:31489369). It is however unclear if SLC25A5/ANT2 constitutes a pore-forming component of mPTP or regulates it (PubMed:31489369). Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (PubMed:31618756). As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation (By similarity)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Mitochondrion inner membrane. Membrane
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Graphical Visualization of S-nitrosylation Sites:
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The S-nitrosylation sites of P51881
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
129 |
SGGAAGATSL C FVYPLDFART |
CCHHHHHHHH H HHHHHHHHHH |
1.86% |
21278135
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| 2 |
160 |
AEREFKGLGD C LVKIYKSDGI |
CCHHHHHHHH H HHHHHHHHHH |
4.46% |
22178444
20925432
21278135
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| 3 |
257 |
TDIMYTGTLD C WRKIARDEGS |
CCHHHHHHHH H HHHHHHHHHH |
4.21% |
24926564
20925432
21278135
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| 4 |
57 |
ADKQYKGIID C VVRIPKEQGV |
CCHHHHHHHH H HHHHHHHHHH |
1.83% |
21278135
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