Summary: Mitochondrial carrier protein
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Mitochondrial carrier Edit Wikipedia article
Mitochondrial ADP/ATP carrier
A variety of substrate carrier proteins, which are involved in energy transfer, have been found in the inner membranes of mitochondria and other eukaryotic organelles such as the peroxisome. Such proteins include: ADP, ATP carrier protein (ADP-ATP translocase); 2-oxoglutarate/malate carrier protein (SLC25A11); phosphate carrier protein (SLC25A3); tricarboxylate transport protein (SLC25A1, or citrate transport protein); Graves disease carrier protein (SLC25A16); yeast mitochondrial proteins MRS3 and MRS4; yeast mitochondrial FAD carrier protein; and many others.
All known mitochondrial carriers are encoded by nuclear genes. Most contain a primary structure exhibiting regions of 100 homologous amino acid repeats, and both the N and C termini face the intermembrane space. There are six definable transmembrane domains in each carrier. All carriers also contain a common sequence, referred to as the MCF motif, in each repeated region, with some variation in one or two signature sequences.
Amongst the members of the mitochondrial carrier family that have been identified, it is the ADP/ATP carrier (AAC) that is responsible for importing ADP into the mitochondria and exporting ATP out of the mitochondria and into the cytosol following synthesis. The AAC is an integral membrane protein that is synthesised lacking a cleavable presequence, but instead contains internal targeting information. It forms a dimer of two identical subunits and consists of a basket shaped structure with six transmembrane helices that are tilted with respect to the membrane, 3 of them "kinked" at the level of proline residues.
Examples of transported compounds include:
- citrate - SLC25A1
- ornithine - SLC25A2, SLC25A15
- phosphate - SLC25A3, SLC25A23, SLC25A24, SLC25A25
- adenine nucleotide - SLC25A4, SLC25A5, SLC25A6, SLC25A31
- dicarboxylate - SLC25A10
- oxoglutarate - SLC25A11
- glutamate - SLC25A22
Human proteins containing this domain include:
- HDMCP, LOC153328, MCART1, MCART2, MCART6, MTCH1, MTCH2
- UCP1, UCP2, UCP3
- SLC25A1, SLC25A3, SLC25A4, SLC25A5, SLC25A6, SLC25A10, SLC25A11, SLC25A12, SLC25A13, SLC25A14, SLC25A16, SLC25A17, SLC25A18, SLC25A19, SLC25A21, SLC25A22, SLC25A23, SLC25A24, SLC25A25, SLC25A26, SLC25A27, SLC25A28, SLC25A29, SLC25A30, SLC25A31, SLC25A32, SLC25A33, SLC25A34, SLC25A35, SLC25A36, SLC25A37, SLC25A38, SLC25A39, SLC25A40, SLC25A41, SLC25A42, SLC25A43, SLC25A44, SLC25A45, SLC25A46
- Nury H, Dahout-Gonzalez C, Trézéguet V, Lauquin GJ, Brandolin G, Pebay-Peyroula E (2006). "Relations between structure and function of the mitochondrial ADP/ATP carrier". Annu. Rev. Biochem. 75: 713–41. doi:10.1146/annurev.biochem.75.103004.142747. PMID 16756509.
- Klingenberg M (1990). "Mechanism and evolution of the uncoupling protein of brown adipose tissue". Trends Biochem. Sci. 15 (3): 108–112. doi:10.1016/0968-0004(90)90194-G. PMID 2158156.
- Walker JE (1992). "The mitochondrial transporter family". Curr. Opin. Struct. Biol. 2 (4): 519–526. doi:10.1016/0959-440X(92)90081-H.
- Kuan J, Saier Jr MH (1993). "Expansion of the mitochondrial carrier family". Res. Microbiol. 144 (8): 671–672. doi:10.1016/0923-2508(93)90073-B. PMID 8140286.
- Lawson JE, Nelson DR, Klingenberg M, Douglas MG (1993). "Site-directed mutagenesis of the yeast mitochondrial ADP/ATP translocator. Six arginines and one lysine are essential". J. Mol. Biol. 230 (4): 1159–1170. doi:10.1006/jmbi.1993.1233. PMID 8487299.
- Palmieri F (1994). "Mitochondrial carrier proteins". FEBS Lett. 346 (1): 48–54. doi:10.1016/0014-5793(94)00329-7. PMID 8206158.
- Jank B, Schweyen RJ, Link TA, Habermann B (1993). "PMP47, a peroxisomal homologue of mitochondrial solute carrier proteins". Trends Biochem. Sci. 18 (11): 427–428. doi:10.1016/0968-0004(93)90141-9. PMID 8291088.
- Endres M, Neupert W, Brunner M (June 1999). "Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex". EMBO J. 18 (12): 3214–21. doi:10.1093/emboj/18.12.3214. PMC 1171402. PMID 10369662.
- Ryan MT, Müller H, Pfanner N (July 1999). "Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane". J. Biol. Chem. 274 (29): 20619–27. doi:10.1074/jbc.274.29.20619. PMID 10400693.
- Falconi M, Chillemi G, Di Marino D, D'Annessa I, Morozzo della Rocca B, Palmieri L, Desideri A (November 2006). "Structural dynamics of the mitochondrial ADP/ATP carrier revealed by molecular dynamics simulation studies". Proteins 65 (3): 681–91. doi:10.1002/prot.21102. PMID 16988954.
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Internal database links
|SCOOP:||HMD DUF3764 PrcB_C Fuseless|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR018108
A variety of substrate carrier proteins that are involved in energy transfer are found in the inner mitochondrial membrane or integral to the membrane of other eukaryotic organelles such as the peroxisome [PUBMED:2158156, PUBMED:8140286, PUBMED:8487299, PUBMED:8206158, PUBMED:8291088]. Such proteins include: ADP, ATP carrier protein (ADP/ATP translocase); 2-oxoglutarate/malate carrier protein; phosphate carrier protein; tricarboxylate transport protein (or citrate transport protein); Graves disease carrier protein; yeast mitochondrial proteins MRS3 and MRS4; yeast mitochondrial FAD carrier protein; and many others. Structurally, these proteins can consist of up to three tandem repeats of a domain of approximately 100 residues, each domain containing two transmembrane regions.
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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|Number in seed:||161|
|Number in full:||47534|
|Average length of the domain:||94.40 aa|
|Average identity of full alignment:||21 %|
|Average coverage of the sequence by the domain:||74.17 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||24|
|Download:||download the raw HMM for this family|
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Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
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The tree shows the occurrence of this domain across different species. More...
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Mito_carr domain has been found. There are 30 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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