Search by BoMiProt ID - Bomi9285


Primary Information

BoMiProt ID Bomi9285
Protein Name Sodium/potassium-transporting ATPase subunit alpha-2/Sodium pump subunit alpha-2/Na(+)/K(+) ATPase alpha-2 subunit
Organism Bos taurus
Uniprot IdA2VDL6
Milk FractionWhey,MFGM
Aminoacid Length 1020
Molecular Weight 112179
Fasta Sequence https://www.uniprot.org/uniprot/A2VDL6.fasta
Gene Name ATP1A2
Gene Id 515161
Protein Existence Status reviewed

Secondary Information

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. 
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)
PTMs Phosphorylation at Ser/Thr
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
Predicted Disorder Regions (7-36)
DisProt Annotation
TM Helix Prediction 8TMHs; (94-116),(128-146), (289-311), (320-342),(785-807),(849-871),(950-968),(980-998)
Additional Comments During ischemia, Na+/K+-ATPase-related functions will naturally increase the energy demand of the Na+/K+-ATPase ion pump.
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