Summary: Iron-containing outer mitochondrial membrane protein N-terminus
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Iron-containing outer mitochondrial membrane protein N-terminus Provide feedback
MitoNEET_N is the N-terminal region of the MitoNEET and Miner-type proteins that carry a zf-CDGSH, PF09360 redox-active 2Fe-2S cluster. The whole protein regulates oxidative capacity. The domain is an anchor sequence that tethers the protein to the outer membrane.
Wiley SE, Murphy AN, Ross SA, van der Geer P, Dixon JE; , Proc Natl Acad Sci U S A. 2007;104:5318-5323.: MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity. PUBMED:17376863 EPMC:17376863
Wiley SE, Paddock ML, Abresch EC, Gross L, van der Geer P, Nechushtai R, Murphy AN, Jennings PA, Dixon JE; , J Biol Chem. 2007;282:23745-23749.: The outer mitochondrial membrane protein mitoNEET contains a novel redox-active 2Fe-2S cluster. PUBMED:17584744 EPMC:17584744
Paddock ML, Wiley SE, Axelrod HL, Cohen AE, Roy M, Abresch EC, Capraro D, Murphy AN, Nechushtai R, Dixon JE, Jennings PA; , Proc Natl Acad Sci U S A. 2007;104:14342-14347.: MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone. PUBMED:17766440 EPMC:17766440
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR019610
The CDGSH iron sulphur domain are a group of iron-sulphur (Fe-S) clusters and a unique 39 amino acid CDGSH domain [C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H].
The CDGSH iron sulphur domain protein (also referred to as mitoNEET) is an integral membrane protein located in the outer mitochondrial membrane and whose function may be to transport iron into the mitochondria [PUBMED:17766440]. Iron in turn is essential for the function of several mitochondrial enzymes.
This entry represents the N-terminal of the mitoNEET and Miner-type proteins that carry a CDGSH-type cluster-binding domain (INTERPRO) that coordinate a redox-active 2Fe-2S cluster.
In the outer mitochondrian membrane (OMM), the CDGSH 2Fe-2S-containing domain is oriented towards the cytoplasm and is tethered to the mitochondrial membrane by the N-terminal domain found in higher vertebrates [PUBMED:17584744, PUBMED:17766440, PUBMED:17376863]. The whole protein regulates oxidative capacity and may function in electron transfer, for instance in redox reactions with metabolic intermediates, cofactors and/or proteins localized at the OMM.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||intracellular membrane-bounded organelle (GO:0043231)|
|Molecular function||2 iron, 2 sulfur cluster binding (GO:0051537)|
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Curation and family details
|Seed source:||Wiley S|
|Number in seed:||9|
|Number in full:||136|
|Average length of the domain:||53.10 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||42.79 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||4|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the MitoNEET_N domain has been found. There are 3 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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