Primary Information |
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BoMiProt ID | Bomi9285 |
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Protein Name | Sodium/potassium-transporting ATPase subunit alpha-2/Sodium pump subunit alpha-2/Na(+)/K(+) ATPase alpha-2 subunit |
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Organism | Bos taurus |
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Uniprot ID | A2VDL6 |
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Milk Fraction | Whey,MFGM |
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Aminoacid Length | 1020 |
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Molecular Weight | 112179 |
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FASTA Sequence |
Download |
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Gene Name | ATP1A2 |
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Gene ID | 515161 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | The Na+/K+-ATPases are transmembrane ion pumps important for maintenance of ion gradients across the plasma membrane that serve to support multiple cellular functions, such as membrane potentials, regulation of cellular volume and pH, and co-transport of signaling transmitters in all animal cells. |
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Biochemical Properties | Na+/K+- ATPase is involved in regulating signaling pathways, such as the membrane-associated non-receptor tyrosine kinase Src, activation of Ras/Raf/ERK1/2, phosphate inositol 3-kinase (PI3K), PI3K-dependent protein kinase B, phospholipase C, [Ca2+]i oscillations [27–29], and gene transcription (Egr-1, Fos, June, Nr4a2, Hes1 and Gabre) |
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PTMs | Phosphorylation at Ser/Thr |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|A2VDL6|AT1A2_BOVIN Sodium/potassium-transporting ATPase subunit alpha-2 OS=Bos taurus OX=9913 GN=ATP1A2 PE=1 SV=1
MGRGAGREYS*10PAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKG
LTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAFGIQAAME
DEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVVREGEKMQINA
EEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNI
CFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFL
GVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLE
AVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALS
RIAGLCNRAVFKAGQENIS*339VSKRDTAGDAS*450ESALLKCIELSCGSVRKMRDRNPKVAEIPF
NSTNKYQLSIHEREDS*496PQSHVLVMKGAPERILDRCSSILVQGKEIPLDKEMQDAFQNAYL
ELGGLGERVLGFCQLNLPS*559AKFPRGFKFDT*570DELNFPTEKLCFVGLMS*587MIDPPRAAVPDAV
GKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKAC
VVHGSDLKDMTS*672EQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSP
ALKKADIGIAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSN
IPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAES*826DIMKRQPRNPQTDK
LVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRSMNDLEDSYG
QEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNS*940VFQQGMKNKILIFGLLEETA
LAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY |
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Predicted Disorder Regions | (7-36) |
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DisProt Annotation | |
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TM Helix Prediction | 8TMHs; (94-116),(128-146), (289-311), (320-342),(785-807),(849-871),(950-968),(980-998) |
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Additional Comments | During ischemia, Na+/K+-ATPase-related functions will naturally increase the energy demand of the Na+/K+-ATPase ion pump. |
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Bibliography | 1.Ellman, Ditte Gry; Isaksen, Toke Jost; Lund, Minna Christiansen; Dursun, Safinaz; Wirenfeldt, Martin; Jørgensen, Louise Helskov; Lykke-Hartmann, Karin; Lambertsen, Kate Lykke (2017). The loss-of-function disease-mutation G301R in the Na+/K+-ATPase α2 isoform decreases lesion volume and improves functional outcome after acute spinal cord injury in mice. BMC Neuroscience, 18(1), 66–. doi:10.1186/s12868-017-0385-9. 2.Aperia A. New roles for an old enzyme: Na, K-ATPase emerges as an interesting drug target. J Intern Med. 2007;261(1):44–52. 3.Liu J, Xie ZJ. The sodium pump and cardiotonic steroids-induced signal transduction protein kinases and calcium-signaling microdomain in regulation of transporter trafcking. Biochim Biophys Acta. 2010;1802(12):1237–45. 4.Schoner W, Scheiner-Bobis G. Endogenous and exogenous cardiac glycosides: their roles in hypertension, salt metabolism, and cell growth. Am J Physiol Cell Physiol. 2007;293(2):C509–36. 5.Hardingham GE, Chawla S, Johnson CM, Bading H. Distinct functions of nuclear and cytoplasmic calcium in the control of gene expression. Nature. 1997;385(6613):260–5 |