BCS1_N |
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| SMART accession number: | SM01024
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| Description: |
This domain is found at the N terminal of the mitochondrial ATPase BSC1. It encodes the import and intramitochondrial sorting for the protein. |
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| Interpro abstract (IPR014851): |
This domain is found at the N-terminal of the mitochondrial ATPase BSC1. It encodes the import and intramitochondrial sorting for the protein [(PUBMED:12640110)].
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| Family alignment: |
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There are 268
BCS1_N domains in 268 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Cellular role (predicted cellular role)
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Cellular role: interaction
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Stan T, Brix J, Schneider-Mergener J, Pfanner N, Neupert W, Rapaport D
- Mitochondrial protein import: recognition of internal import signals ofBCS1 by the TOM complex.
- Mol Cell Biol. 2003; 23: 2239-50
- Display abstract
BCS1, a component of the inner membrane of mitochondria, belongs to thegroup of proteins with internal, noncleavable import signals. Import andintramitochondrial sorting of BCS1 are encoded in the N-terminal 126 aminoacid residues. Three sequence elements were identified in this region,namely, the transmembrane domain (amino acid residues 51 to 68), apresequence type helix (residues 69 to 83), and an import auxiliary region(residues 84 to 126). The transmembrane domain is not required for stablebinding to the TOM complex. The Tom receptors (Tom70, Tom22 and Tom20), asdetermined by peptide scan analysis, interact with the presequence-likehelix, yet the highest binding was to the third sequence element. Wepropose that the initial recognition of BCS1 precursor at the surface ofthe organelle mainly depends on the auxiliary region and does not requirethe transmembrane domain. This essential region represents a novel type ofsignal with targeting and sorting functions. It is recognized by all threeknown mitochondrial import receptors, demonstrating their capacity todecode various targeting signals. We suggest that the BCS1 precursorcrosses the TOM complex as a loop structure and that once the precursoremerges from the TOM complex, all three structural elements are essentialfor the intramitochondrial sorting to the inner membrane.
- Links (links to other resources describing this domain)
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to expand nodes. To display all proteins with a BCS1_N domain in a specific node, click on it.