Summary: ATP synthase D chain, mitochondrial (ATP5H)
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ATP5H Edit Wikipedia article
| ATP synthase D chain, mitochondrial | |||||||||
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| Identifiers | |||||||||
| Symbol | ATP5H | ||||||||
| Pfam | PF05873 | ||||||||
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ATP synthase subunit d, mitochondrial is an enzyme that in humans is encoded by the ATP5H gene.[1][2]
Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The F0 seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the d subunit of the F0 complex. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. In addition, three pseudogenes are located on chromosomes 9, 12 and 15.[2]
[edit] References
- ^ Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Nov 2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res 10 (10): 154660. doi:10.1101/gr.140200. PMC 310934. PMID 11042152. //www.ncbi.nlm.nih.gov/pmc/articles/PMC310934/.
- ^ a b "Entrez Gene: ATP5H ATP synthase, H+ transporting, mitochondrial F0 complex, subunit d". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10476.
[edit] Further reading
- Kinosita K, Yasuda R, Noji H (2003). "F1-ATPase: a highly efficient rotary ATP machine.". Essays Biochem. 35: 318. PMID 12471886.
- Oster G, Wang H (2003). "Rotary protein motors.". Trends Cell Biol. 13 (3): 11421. doi:10.1016/S0962-8924(03)00004-7. PMID 12628343.
- Leyva JA, Bianchet MA, Amzel LM (2003). "Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review).". Mol. Membr. Biol. 20 (1): 2733. doi:10.1080/0968768031000066532. PMID 12745923.
- Higuti T, Kuroiwa K, Miyazaki S, et al. (1994). "The complete amino acid sequence of subunit d of rat liver mitochondrial H(+)-ATP synthase.". J. Biochem. 114 (5): 7147. PMID 7509337.
- Elston T, Wang H, Oster G (1998). "Energy transduction in ATP synthase.". Nature 391 (6666): 5103. doi:10.1038/35185. PMID 9461222.
- Wang H, Oster G (1998). "Energy transduction in the F1 motor of ATP synthase.". Nature 396 (6708): 27982. doi:10.1038/24409. PMID 9834036.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.ncbi.nlm.nih.gov/pmc/articles/PMC139241/.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 405. doi:10.1038/ng1285. PMID 14702039.
- Cross RL (2004). "Molecular motors: turning the ATP motor.". Nature 427 (6973): 4078. doi:10.1038/427407b. PMID 14749816.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 21217. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. //www.ncbi.nlm.nih.gov/pmc/articles/PMC528928/.
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ATP synthase D chain, mitochondrial (ATP5H) Provide feedback
This family consists of several ATP synthase D chain, mitochondrial (ATP5H) proteins. Subunit d has no extensive hydrophobic sequences, and is not apparently related to any subunit described in the simpler ATP synthases in bacteria and chloroplasts [1,2].
Literature references
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Walker JE, Runswick MJ, Poulter L; , J Mol Biol 1987;197:89-100.: ATP synthase from bovine mitochondria. The characterization and sequence analysis of two membrane-associated sub-units and of the corresponding cDNAs. PUBMED:2890767 EPMC:2890767
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Higuti T, Kuroiwa K, Miyazaki S, Yoshihara Y, Toda H, Kakuno T, Sakiyama F; , J Biochem (Tokyo) 1993;114:714-717.: The complete amino acid sequence of subunit d of rat liver mitochondrial H(+)-ATP synthase. PUBMED:7509337 EPMC:7509337
Internal database links
| SCOOP: | Vps54 |
External database links
| PANDIT: | PF05873 |
| Pseudofam: | PF05873 |
| SYSTERS: | Mt_ATP-synt_D |
This tab holds annotation information from the InterPro database.
InterPro entry IPR008689
Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.
There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [PUBMED:15473999, PUBMED:15078220]. The different types include:
- F-ATPases (F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
- V-ATPases (V1V0-ATPases), which are primarily found in eukaryotic vacuoles and catalyse ATP hydrolysis to transport solutes and lower pH in organelles.
- A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases (though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases).
- P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
- E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.
F-ATPases (also known as F1F0-ATPase, or H(+)-transporting two-sector ATPase) (EC) are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), nine in mitochondria (A-G, F6, F8). Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits, while in the F0 complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the F0 rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis [PUBMED:11309608]. These ATPases can also work in reverse to hydrolyse ATP to create a proton gradient.
This entry represents subunit D from the F0 complex in F-ATPases found in mitochondria. The D subunit is part of the peripheral stalk that links the F1 and F0 complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In mitochondria, the peripheral stalk is composed of one copy each of subunits OSCP (oligomycin sensitivity conferral protein), F6, B and D [PUBMED:16045926]. There is no homologue of subunit D in bacterial or chloroplast F-ATPase, whose peripheral stalks are composed of one copy of the delta subunit (homologous to OSCP), and two copies of subunit B in bacteria, or one copy each of subunits B and B' in chloroplasts and photosynthetic bacteria.
More information about this protein can be found at Protein of the Month: ATP Synthases [PUBMED:].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) (GO:0000276) |
| Molecular function | hydrogen ion transmembrane transporter activity (GO:0015078) |
| Biological process | ATP synthesis coupled proton transport (GO:0015986) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
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| Seed (5) |
Full (370) |
Representative proteomes | NCBI (361) |
Meta (1) |
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| RP15 (67) |
RP35 (113) |
RP55 (179) |
RP75 (234) |
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| PP/heatmap | 1 | |||||||
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (5) |
Full (370) |
Representative proteomes | NCBI (361) |
Meta (1) |
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| RP15 (67) |
RP35 (113) |
RP55 (179) |
RP75 (234) |
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| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_9814 (release 8.0) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Moxon SJ |
| Number in seed: | 5 |
| Number in full: | 370 |
| Average length of the domain: | 149.30 aa |
| Average identity of full alignment: | 28 % |
| Average coverage of the sequence by the domain: | 75.57 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 161 | ||||||||||||
| Family (HMM) version: | 7 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
Structures
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 Mt_ATP-synt_D 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence