Summary: Gastric H+/K+-ATPase, N terminal domain
This is the Wikipedia entry entitled "ATPase, Na+/K+ transporting, alpha 1". More...
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ATPase, Na+/K+ transporting, alpha 1 Edit Wikipedia article
|ATPase, Na+/K+ transporting, alpha 1 polypeptide|
PDB rendering based on 1mo7.
|External IDs||ChEMBL: GeneCards:|
|RNA expression pattern|
|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.
- "Entrez Gene: ATP1A1 ATPase, Na+/K+ transporting, alpha 1 polypeptide".
- Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
- Lingrel JB, Orlowski J, Shull MM, Price EM (1990). "Molecular genetics of Na,K-ATPase.". Prog. Nucleic Acid Res. Mol. Biol. 38: 37–89. doi:10.1016/S0079-6603(08)60708-4. PMID 2158121.
- Dunbar LA, Caplan MJ (2001). "Ion pumps in polarized cells: sorting and regulation of the Na+, K+- and H+, K+-ATPases.". J. Biol. Chem. 276 (32): 29617–20. doi:10.1074/jbc.R100023200. PMID 11404365.
- Wangemann P (2002). "K+ cycling and the endocochlear potential.". Hear. Res. 165 (1-2): 1–9. doi:10.1016/S0378-5955(02)00279-4. PMID 12031509.
- Xie Z, Cai T (2004). "Na+-K+--ATPase-mediated signal transduction: from protein interaction to cellular function.". Mol. Interv. 3 (3): 157–68. doi:10.1124/mi.3.3.157. PMID 14993422.
- Shull MM, Pugh DG, Lingrel JB (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 (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 (1986). "Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence.". J. Biochem. 100 (2): 389–97. PMID 2430951.
- Yang-Feng TL, Schneider JW, Lindgren V, et al. (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, et al. (1987). "Family of Na+,K+-ATPase genes. Intra-individual tissue-specific restriction fragment length polymorphism.". FEBS Lett. 221 (1): 129–33. doi:10.1016/0014-5793(87)80366-6. PMID 2887455.
- Chehab FF, Kan YW, Law ML, et al. (1987). "Human placental Na+,K+-ATPase alpha subunit: cDNA cloning, tissue expression, DNA polymorphism, and chromosomal localization.". Proc. Natl. Acad. Sci. U.S.A. 84 (22): 7901–5. doi:10.1073/pnas.84.22.7901. PMC 299443. PMID 2891135.
- Ovchinnikov YuA, Monastyrskaya GS, Broude NE, et al. (1987). "The family of human Na+,K+-ATPase genes. A partial nucleotide sequence related to the alpha-subunit.". FEBS Lett. 213 (1): 73–80. doi:10.1016/0014-5793(87)81467-9. PMID 3030810.
- Shull MM, Lingrel JB (1987). "Multiple genes encode the human Na+,K+-ATPase catalytic subunit.". Proc. Natl. Acad. Sci. U.S.A. 84 (12): 4039–43. doi:10.1073/pnas.84.12.4039. PMC 305017. PMID 3035563.
- Sverdlov ED, Monastyrskaya GS, Broude NE, et al. (1987). "The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit.". FEBS Lett. 217 (2): 275–8. doi:10.1016/0014-5793(87)80677-4. PMID 3036582.
- Ruiz A, Bhat SP, Bok D (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, et al. (1995). "Subcellular distribution and immunocytochemical localization of Na,K-ATPase subunit isoforms in human skeletal muscle.". Mol. Membr. Biol. 11 (4): 255–62. doi:10.3109/09687689409160435. PMID 7711835.
- Feschenko MS, Sweadner KJ (1995). "Structural basis for species-specific differences in the phosphorylation of Na,K-ATPase by protein kinase C.". J. Biol. Chem. 270 (23): 14072–7. doi:10.1074/jbc.270.23.14072. PMID 7775468.
- Ruiz-Opazo N, Barany F, Hirayama K, Herrera VL (1994). "Confirmation of mutant alpha 1 Na,K-ATPase gene and transcript in Dahl salt-sensitive/JR rats.". Hypertension 24 (3): 260–70. PMID 8082931.
- Zahler R, Gilmore-Hebert M, Baldwin JC, et al. (1993). "Expression of alpha isoforms of the Na,K-ATPase in human heart.". Biochim. Biophys. Acta 1149 (2): 189–94. doi:10.1016/0005-2736(93)90200-J. PMID 8391840.
- Wang J, Schwinger RH, Frank K, et al. (1996). "Regional expression of sodium pump subunits isoforms and Na+-Ca++ exchanger in the human heart.". J. Clin. Invest. 98 (7): 1650–8. doi:10.1172/JCI118960. PMC 507599. 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
External database links
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 (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.
P-ATPases (sometime 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, each of which transports a specific type 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].
More information about this protein can be found at Protein of the Month: ATP Synthases [PUBMED:].
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)|
|hydrogen:potassium-exchanging ATPase activity (GO:0008900)|
|ATP binding (GO:0005524)|
|Biological process||ATP hydrolysis coupled proton transport (GO:0015991)|
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Curation and family details
|Author:||Mistry J, Sammut SJ|
|Number in seed:||5|
|Number in full:||35|
|Average length of the domain:||41.00 aa|
|Average identity of full alignment:||88 %|
|Average coverage of the sequence by the domain:||4.36 %|
|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:||6|
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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 2 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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