Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase.
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Tom22 is the central preprotein receptor of the TOM complex, binding preproteins through both its cytosolic and intermembrane space domains and stably associated with the Tom40 channel.
"The central receptor Tom22 binds preproteins through both its cytosolic domain and its intermembrane space domain and is stably associated with the channel protein Tom40"
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Tom22 is required for the higher-level organization of the TOM machinery and for tight control of Tom40 channel gating.
"In the absence of Tom22, the translocase dissociates into core complexes, representing the basic import units, but lacks a tight control of channel gating."
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Tom22's cytosolic domain serves as the docking point for the peripheral receptors Tom20 and Tom70 onto the TOM/GIP core.
"its cytosolic domain serves as docking point for the peripheral receptors Tom20 and Tom70."
Multistep assembly of the protein import channel of the mitochondrial outer membrane.
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Tom40 is first targeted to the OMM via the receptor proteins Tom20 and Tom22, supporting Tom22's role in protein insertion into the outer membrane.
"the channel-lining Tom40 is first targeted to the membrane via the receptor proteins Tom20 and Tom22; it then assembles with Tom5 to form the 250 kDa intermediate exposed to the intermembrane space."
Biogenesis of yeast mitochondrial cytochrome c: a unique relationship to the TOM machinery.
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tom22 mutants have greatly reduced cytochrome c levels, supporting Tom22's role in TOM-mediated import beyond canonical matrix presequence routes.
"Mitochondria lacking the central receptor and organizing protein Tom22 contain greatly reduced levels of cytochrome c."
Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17.
Large-scale identification of yeast integral membrane protein interactions.
Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins.
Integral membrane proteins in the mitochondrial outer membrane of Saccharomyces cerevisiae.
Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics.
The mitochondrial TOM complex is required for tBid/Bax-induced cytochrome c release.
The mitochondrial contact site complex, a determinant of mitochondrial architecture.
The cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeast.
Coupling of mitochondrial import and export translocases by receptor-mediated supercomplex formation.
Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae.
The social and structural architecture of the yeast protein interactome.
Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex.
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Tom22 is a core, essential subunit of the GIP complex stably associated with Tom40.
"The receptor Tom22 stably associates with Tom40, the main component of the GIP, in a complex with a molecular weight of approximately 400,000 ( approximately 400K), while the other receptors, Tom20 and Tom70, are more loosely associated with this GIP complex and can be found in distinct subcomplexes."
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The TOM/GIP complex containing Tom40, Tom22, and three small Tom proteins forms the central unit of the OMM import machinery.
"The GIP complex, containing Tom40, Tom22, and three small Tom proteins, forms the central unit of the outer membrane import machinery."
TOM40:TOM70 complex translocates proteins from the cytosol to the mitochondrial intermembrane space
Formation of MIB complex containing the MICOS complex
Falcon deep research report for human TOMM22 (used as ortholog reference for yeast Tom22)
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TOMM22 functions as the central receptor of the TOM complex, recognizing mitochondrial precursor proteins and transferring them toward the Tom40 import pore.
"TOMM22 functions as a **major preprotein-binding site** and **organizational scaffold** for the TOM complex, helping recognize mitochondrial precursor proteins and transfer them toward the **Tom40 import pore**."