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3  structures 281  species 2  interactions 370  sequences 8  architectures

Family: Mt_ATP-synt_D (PF05873)

Summary: ATP synthase D chain, mitochondrial (ATP5H)

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This is the Wikipedia entry entitled "ATP5H". More...

ATP5H Edit Wikipedia article

ATP synthase, H+ transporting, mitochondrial Fo complex, subunit d
Identifiers
Symbols ATP5H; ATPQ
External IDs MGI1918929 HomoloGene130552 GeneCards: ATP5H Gene
EC number 3.6.1.14
RNA expression pattern
PBB GE ATP5H 210149 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 10476 71679
Ensembl ENSG00000167863 n/a
UniProt O75947 n/a
RefSeq (mRNA) NM_001003785 NM_027862
RefSeq (protein) NP_001003785 NP_082138
Location (UCSC) Chr 17:
73.03 – 73.04 Mb
n/a
PubMed search [1] [2]
ATP synthase D chain, mitochondrial
Identifiers
Symbol ATP5H
Pfam PF05873

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]

References[edit]

  1. ^ 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): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152. 
  2. ^ a b "Entrez Gene: ATP5H ATP synthase, H+ transporting, mitochondrial F0 complex, subunit d". 

Further reading[edit]



This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

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

  1. 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

  2. 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

External database links

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

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Domain organisation

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Alignments

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Representative proteomes NCBI
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RP55
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RP75
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  Seed
(5)
Full
(370)
Representative proteomes NCBI
(361)
Meta
(1)
RP15
(67)
RP35
(113)
RP55
(179)
RP75
(234)
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  Seed
(5)
Full
(370)
Representative proteomes NCBI
(361)
Meta
(1)
RP15
(67)
RP35
(113)
RP55
(179)
RP75
(234)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Curation and family details

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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 View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.3 21.3
Trusted cut-off 21.3 21.3
Noise cut-off 20.6 21.2
Model length: 161
Family (HMM) version: 7
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Species distribution

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Interactions

There are 2 interactions for this family. More...

Mt_ATP-synt_B Mt_ATP-synt_D

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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