Summary: Gastric H+/K+-ATPase, N terminal domain
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ATPase, Na+/K+ transporting, alpha 1 Edit Wikipedia article
|, ATPase, Na+/K+ transporting, alpha 1, ATPase Na+/K+ transporting subunit alpha 1|
|Gastric H+/K+-ATPase, N terminal domain|
tfe-induded structure of the n-terminal domain of pig gastric h/k-atpase
The protein encoded by this gene belongs to the family of P-type cation transport ATPases, and to the subfamily of Na+/K+-ATPases. Na+/K+-ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The catalytic subunit of Na+/K+-ATPase is encoded by multiple genes. This gene encodes an alpha 1 subunit. Alternatively spliced transcript variants encoding different isoforms have been identified.
- GRCh38: Ensembl release 89: ENSG00000163399 - Ensembl, May 2017
- GRCm38: Ensembl release 89: ENSMUSG00000033161 - Ensembl, May 2017
- "Human PubMed Reference:".
- "Mouse PubMed Reference:".
- "Entrez Gene: ATP1A1 ATPase, Na+/K+ transporting, alpha 1 polypeptide".
- Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E (December 2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell & Melanoma Research. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
- Beuschlein F, Boulkroun S, Osswald A, Wieland T, Nielsen HN, Lichtenauer UD, Penton D, Schack VR, Amar L, Fischer E, Walther A, Tauber P, Schwarzmayr T, Diener S, Graf E, Allolio B, Samson-Couterie B, Benecke A, Quinkler M, Fallo F, Plouin PF, Mantero F, Meitinger T, Mulatero P, Jeunemaitre X, Warth R, Vilsen B, Zennaro MC, Strom TM, Reincke M (April 2013). "Somatic mutations in ATP1A1 and ATP2B3 lead to aldosterone-producing adenomas and secondary hypertension". Nature Genetics. 45 (4): 440–4, 444e1–2. doi:10.1038/ng.2550. PMID 23416519.
- Lingrel JB, Orlowski J, Shull MM, Price EM (1990). "Molecular genetics of Na,K-ATPase". Progress in Nucleic Acid Research and Molecular Biology. 38: 37–89. doi:10.1016/S0079-6603(08)60708-4. PMID 2158121.
- Dunbar LA, Caplan MJ (August 2001). "Ion pumps in polarized cells: sorting and regulation of the Na+, K+- and H+, K+-ATPases". The Journal of Biological Chemistry. 276 (32): 29617–20. doi:10.1074/jbc.R100023200. PMID 11404365.
- Wangemann P (March 2002). "K+ cycling and the endocochlear potential". Hearing Research. 165 (1-2): 1–9. doi:10.1016/S0378-5955(02)00279-4. PMID 12031509.
- Xie Z, Cai T (May 2003). "Na+-K+--ATPase-mediated signal transduction: from protein interaction to cellular function". Molecular Interventions. 3 (3): 157–68. doi:10.1124/mi.3.3.157. PMID 14993422.
- Shull MM, Pugh DG, Lingrel JB (March 1990). "The human Na, K-ATPase alpha 1 gene: characterization of the 5'-flanking region and identification of a restriction fragment length polymorphism". Genomics. 6 (3): 451–60. doi:10.1016/0888-7543(90)90475-A. PMID 1970326.
- Herrera VL, Ruiz-Opazo N (August 1990). "Alteration of alpha 1 Na+,K(+)-ATPase 86Rb+ influx by a single amino acid substitution". Science. 249 (4972): 1023–6. doi:10.1126/science.1975705. PMID 1975705.
- Kawakami K, Ohta T, Nojima H, Nagano K (August 1986). "Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence". Journal of Biochemistry. 100 (2): 389–97. PMID 2430951.
- Yang-Feng TL, Schneider JW, Lindgren V, Shull MM, Benz EJ, Lingrel JB, Francke U (February 1988). "Chromosomal localization of human Na+, K+-ATPase alpha- and beta-subunit genes". Genomics. 2 (2): 128–38. doi:10.1016/0888-7543(88)90094-8. PMID 2842249.
- Sverdlov ED, Broude NE, Sverdlov VE, Monastyrskaya GS, Grishin AV, Petrukhin KE, Akopyanz NS, Modyanov NN (August 1987). "Family of Na+,K+-ATPase genes. Intra-individual tissue-specific restriction fragment length polymorphism". FEBS Letters. 221 (1): 129–33. doi:10.1016/0014-5793(87)80366-6. PMID 2887455.
- Chehab FF, Kan YW, Law ML, Hartz J, Kao FT, Blostein R (November 1987). "Human placental Na+,K+-ATPase alpha subunit: cDNA cloning, tissue expression, DNA polymorphism, and chromosomal localization". Proceedings of the National Academy of Sciences of the United States of America. 84 (22): 7901–5. doi:10.1073/pnas.84.22.7901. PMC . PMID 2891135.
- Monastyrskaya GS, Broude NE, Allikmets RL, Melkov AM, Malyshev IV, Dulubova IE, Petrukhin KE (March 1987). "The family of human Na+,K+-ATPase genes. A partial nucleotide sequence related to the alpha-subunit". FEBS Letters. 213 (1): 73–80. doi:10.1016/0014-5793(87)81467-9. PMID 3030810.
- Shull MM, Lingrel JB (June 1987). "Multiple genes encode the human Na+,K+-ATPase catalytic subunit". Proceedings of the National Academy of Sciences of the United States of America. 84 (12): 4039–43. doi:10.1073/pnas.84.12.4039. PMC . PMID 3035563.
- Sverdlov ED, Monastyrskaya GS, Broude NE, Allikmets RL, Melkov AM, Malyshev IV, Dulobova IE, Petrukhin KE (June 1987). "The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit". FEBS Letters. 217 (2): 275–8. doi:10.1016/0014-5793(87)80677-4. PMID 3036582.
- Ruiz A, Bhat SP, Bok D (April 1995). "Characterization and quantification of full-length and truncated Na,K-ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal pigment epithelium". Gene. 155 (2): 179–84. doi:10.1016/0378-1119(94)00812-7. PMID 7536695.
- Hundal HS, Maxwell DL, Ahmed A, Darakhshan F, Mitsumoto Y, Klip A (1995). "Subcellular distribution and immunocytochemical localization of Na,K-ATPase subunit isoforms in human skeletal muscle". Molecular Membrane Biology. 11 (4): 255–62. doi:10.3109/09687689409160435. PMID 7711835.
- Feschenko MS, Sweadner KJ (June 1995). "Structural basis for species-specific differences in the phosphorylation of Na,K-ATPase by protein kinase C". The Journal of Biological Chemistry. 270 (23): 14072–7. doi:10.1074/jbc.270.23.14072. PMID 7775468.
- Ruiz-Opazo N, Barany F, Hirayama K, Herrera VL (September 1994). "Confirmation of mutant alpha 1 Na,K-ATPase gene and transcript in Dahl salt-sensitive/JR rats". Hypertension. 24 (3): 260–70. doi:10.1161/01.hyp.24.3.260. PMID 8082931.
- Zahler R, Gilmore-Hebert M, Baldwin JC, Franco K, Benz EJ (July 1993). "Expression of alpha isoforms of the Na,K-ATPase in human heart". Biochimica et Biophysica Acta. 1149 (2): 189–94. doi:10.1016/0005-2736(93)90200-J. PMID 8391840.
- Wang J, Schwinger RH, Frank K, Müller-Ehmsen J, Martin-Vasallo P, Pressley TA, Xiang A, Erdmann E, McDonough AA (October 1996). "Regional expression of sodium pump subunits isoforms and Na+-Ca++ exchanger in the human heart". The Journal of Clinical Investigation. 98 (7): 1650–8. doi:10.1172/JCI118960. PMC . PMID 8833915.
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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.
Gastric H+/K+-ATPase, N terminal domain Provide feedback
Members of this family adopt an alpha-helical conformation under hydrophobic conditions. The domain contains tyrosine residues, phosphorylation of which regulates the function of the ATPase. Additionally, the domain also interacts with various structural proteins, including the spectrin-binding domain of ankyrin III .
Fujitani N, Kanagawa M, Aizawa T, Ohkubo T, Kaya S, Demura M, Kawano K, Nishimura S, Taniguchi K, Nitta K; , Biochem Biophys Res Commun. 2003;300:223-229.: Structure determination and conformational change induced by tyrosine phosphorylation of the N-terminal domain of the alpha-chain of pig gastric H+/K+-ATPase. PUBMED:12480547 EPMC:12480547
This tab holds annotation information from the InterPro database.
InterPro entry IPR015127
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 (ATP synthases, 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 eukaryotes and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane [PUBMED:20450191]. They are also found in bacteria [PUBMED:9741106].
- 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 [PUBMED:18937357, PUBMED:1385979].
- 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.
P-ATPases (also known as E1-E2 ATPases) (EC) are found in bacteria and in a number of eukaryotic plasma membranes and organelles [PUBMED:9419228]. P-ATPases function to transport a variety of different compounds, including ions and phospholipids, across a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases, which transport specific types of ion: H+, Na+, K+, Mg2+, Ca2+, Ag+ and Ag2+, Zn2+, Co2+, Pb2+, Ni2+, Cd2+, Cu+ and Cu2+. P-ATPases can be composed of one or two polypeptides, and can usually assume two main conformations called E1 and E2.
This entry represents the N-terminal domain found in gastric H+/K+-transporter ATPases. This domain adopts an alpha-helical conformation under hydrophobic conditions. The domain contains tyrosine residues, phosphorylation of which regulates the function of the ATPase. Additionally, the domain also interacts with various structural proteins, including the spectrin-binding domain of ankyrin III [PUBMED:12480547].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||membrane (GO:0016020)|
|Molecular function||magnesium ion binding (GO:0000287)|
|potassium:proton exchanging ATPase activity (GO:0008900)|
|ATP binding (GO:0005524)|
|Biological process||ATP hydrolysis coupled proton transport (GO:0015991)|
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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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.
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|Author:||Mistry J , Sammut SJ|
|Number in seed:||2|
|Number in full:||70|
|Average length of the domain:||40.90 aa|
|Average identity of full alignment:||83 %|
|Average coverage of the sequence by the domain:||3.97 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the More....
This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.
How the sunburst is generated
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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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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 H-K_ATPase_N domain has been found. There are 6 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 sequence.
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