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Showing Protein Sodium/potassium-transporting ATPase subunit alpha-3 (HMDBP01416)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 7 metabolites
Identification
HMDB Protein ID HMDBP01416
Secondary Accession Numbers
  • 6712
Name Sodium/potassium-transporting ATPase subunit alpha-3
Synonyms
  1. Na(+)/K(+) ATPase alpha(III) subunit
  2. Na(+)/K(+) ATPase alpha-3 subunit
  3. Sodium pump subunit alpha-3
Gene Name ATP1A3
Protein Type Unknown
Biological Properties
General Function Involved in ATP binding
Specific Function This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Pathways
  • 3-Methylthiofentanyl Action Pathway
  • Acebutolol Action Pathway
  • Aldosterone-regulated sodium reabsorption
  • Alfentanil Action Pathway
  • Alprenolol Action Pathway
  • Alvimopan Action Pathway
  • Amiloride Action Pathway
  • Amiodarone Action Pathway
  • Amlodipine Action Pathway
  • Anileridine Action Pathway
  • Arbutamine Action Pathway
  • Atenolol Action Pathway
  • Bendroflumethiazide Action Pathway
  • Benzocaine Action Pathway
  • Betaxolol Action Pathway
  • Bevantolol Action Pathway
  • Bile secretion
  • Bisoprolol Action Pathway
  • Blue diaper syndrome
  • Bopindolol Action Pathway
  • Bumetanide Action Pathway
  • Bupivacaine Action Pathway
  • Bupranolol Action Pathway
  • Buprenorphine Action Pathway
  • Carbohydrate digestion and absorption
  • Cardiac muscle contraction
  • Carfentanil Action Pathway
  • Carteolol Action Pathway
  • Carvedilol Action Pathway
  • Chloroprocaine Action Pathway
  • Chlorothiazide Action Pathway
  • Chlorthalidone Action Pathway
  • Citalopram Action Pathway
  • Cocaine Action Pathway
  • Codeine Action Pathway
  • Cyclothiazide Action Pathway
  • Cystinuria
  • Desipramine Action Pathway
  • Dezocine Action Pathway
  • Dibucaine Action Pathway
  • Dihydromorphine Action Pathway
  • Diltiazem Action Pathway
  • Dimethylthiambutene Action Pathway
  • Diphenoxylate Action Pathway
  • Disopyramide Action Pathway
  • Dobutamine Action Pathway
  • Endocrine and other factor-regulated calcium reabsorption
  • Epinephrine Action Pathway
  • Eplerenone Action Pathway
  • Escitalopram Action Pathway
  • Esmolol Action Pathway
  • Ethacrynic Acid Action Pathway
  • Ethylmorphine Action Pathway
  • Felodipine Action Pathway
  • Fentanyl Action Pathway
  • Flecainide Action Pathway
  • Fluoxetine Action Pathway
  • Fosphenytoin (Antiarrhythmic) Action Pathway
  • Furosemide Action Pathway
  • Gastric acid secretion
  • Glucose Transporter Defect (SGLT2)
  • Hartnup Disorder
  • Heroin Action Pathway
  • Hydrochlorothiazide Action Pathway
  • Hydrocodone Action Pathway
  • Hydroflumethiazide Action Pathway
  • Hydromorphone Action Pathway
  • Ibutilide Action Pathway
  • Iminoglycinuria
  • Imipramine Action Pathway
  • Indapamide Action Pathway
  • Insulin secretion
  • Isoprenaline Action Pathway
  • Isradipine Action Pathway
  • Ketobemidone Action Pathway
  • Kidney Function
  • Labetalol Action Pathway
  • Lactose Degradation
  • Lactose Intolerance
  • Levallorphan Action Pathway
  • Levobunolol Action Pathway
  • Levobupivacaine Action Pathway
  • Levomethadyl Acetate Action Action Pathway
  • Levorphanol Action Pathway
  • Lidocaine (Antiarrhythmic) Action Pathway
  • Lidocaine (Local Anaesthetic) Action Pathway
  • Lysinuric Protein Intolerance
  • Lysinuric protein intolerance (LPI)
  • Mepivacaine Action Pathway
  • Methadone Action Pathway
  • Methadyl Acetate Action Pathway
  • Methyclothiazide Action Pathway
  • Metipranolol Action Pathway
  • Metolazone Action Pathway
  • Metoprolol Action Pathway
  • Mexiletine Action Pathway
  • Mineral absorption
  • Morphine Action Pathway
  • Muscle/Heart Contraction
  • Nadolol Action Pathway
  • Nalbuphine Action Pathway
  • Naloxone Action Pathway
  • Naltrexone Action Pathway
  • Nebivolol Action Pathway
  • Nicotine Action Pathway
  • Nifedipine Action Pathway
  • Nimodipine Action Pathway
  • Nisoldipine Action Pathway
  • Nitrendipine Action Pathway
  • Oxprenolol Action Pathway
  • Oxybuprocaine Action Pathway
  • Oxycodone Action Pathway
  • Oxymorphone Action Pathway
  • Pancreatic secretion
  • Penbutolol Action Pathway
  • Pentazocine Action Pathway
  • Phenytoin (Antiarrhythmic) Action Pathway
  • Pindolol Action Pathway
  • Polythiazide Action Pathway
  • Practolol Action Pathway
  • Prilocaine Action Pathway
  • Procainamide (Antiarrhythmic) Action Pathway
  • Procaine Action Pathway
  • Proparacaine Action Pathway
  • Propoxyphene Action Pathway
  • Propranolol Action Pathway
  • Protein digestion and absorption
  • Proximal tubule bicarbonate reclamation
  • Quinethazone Action Pathway
  • Quinidine Action Pathway
  • Remifentanil Action Pathway
  • Ropivacaine Action Pathway
  • Salivary secretion
  • Sotalol Action Pathway
  • Spironolactone Action Pathway
  • Sufentanil Action Pathway
  • Timolol Action Pathway
  • Tocainide Action Pathway
  • Torsemide Action Pathway
  • Tramadol Action Action Pathway
  • Trehalose Degradation
  • Triamterene Action Pathway
  • Trichlormethiazide Action Pathway
  • Verapamil Action Pathway
Reactions Not Available
GO Classification
Biological Process
ATP biosynthetic process
response to drug
adult locomotory behavior
visual learning
ionotropic glutamate receptor signaling pathway
memory
Cellular Component
endoplasmic reticulum
Golgi apparatus
nucleus
sodium:potassium-exchanging ATPase complex
synapse
myelin sheath
axon
Component
membrane
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
binding
catalytic activity
hydrolase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
transmembrane transporter activity
substrate-specific transmembrane transporter activity
ion transmembrane transporter activity
cation transmembrane transporter activity
inorganic cation transmembrane transporter activity
monovalent inorganic cation transmembrane transporter activity
transporter activity
atpase activity, coupled to transmembrane movement of ions
atpase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
hydrolase activity, acting on acid anhydrides
Molecular Function
metal ion binding
ATP binding
sodium:potassium-exchanging ATPase activity
Process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
purine nucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate biosynthetic process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
establishment of localization
transport
monovalent inorganic cation transport
ion transport
atp biosynthetic process
cation transport
Cellular Location
  1. Membrane
  2. Multi-pass membrane protein
Gene Properties
Chromosome Location 19
Locus 19q13.31
SNPs ATP1A3
Gene Sequence 
>3042 bp
ATGGGGGACAAGAAAGATGACAAGGACTCACCCAAGAAGAACAAGGGCAAGGAGCGCCGG
GACCTGGATGACCTCAAGAAGGAGGTGGCTATGACAGAGCACAAGATGTCAGTGGAAGAG
GTCTGCCGGAAATACAACACAGACTGTGTGCAGGGTTTGACCCACAGCAAAGCCCAGGAG
ATCCTGGCCCGGGATGGGCCTAACGCACTCACGCCACCGCCTACCACCCCAGAGTGGGTC
AAGTTTTGCCGGCAGCTCTTCGGGGGCTTCTCCATCCTGCTGTGGATCGGGGCTATCCTC
TGCTTCCTGGCCTACGGTATCCAGGCGGGCACCGAGGACGACCCCTCTGGTGACAACCTG
TACCTGGGCATCGTGCTGGCGGCCGTGGTGATCATCACTGGCTGCTTCTCCTACTACCAG
GAGGCCAAGAGCTCCAAGATCATGGAGTCCTTCAAGAACATGGTGCCCCAGCAAGCCCTG
GTGATCCGGGAAGGTGAGAAGATGCAGGTGAACGCTGAGGAGGTGGTGGTCGGGGACCTG
GTGGAGATCAAGGGTGGAGACCGAGTGCCAGCTGACCTGCGGATCATCTCAGCCCACGGC
TGCAAGGTGGACAACTCCTCCCTGACTGGCGAATCCGAGCCCCAGACTCGCTCTCCCGAC
TGCACGCACGACAACCCCTTGGAGACTCGGAACATCACCTTCTTTTCCACCAACTGTGTG
GAAGGCACGGCTCGGGGCGTGGTGGTGGCCACGGGCGACCGCACTGTCATGGGCCGTATC
GCCACCCTGGCATCAGGGCTGGAGGTGGGCAAGACGCCCATCGCCATCGAGATTGAGCAC
TTCATCCAGCTCATCACCGGCGTGGCTGTCTTCCTGGGTGTCTCCTTCTTCATCCTCTCC
CTCATTCTCGGATACACCTGGCTTGAGGCTGTCATCTTCCTCATCGGCATCATCGTGGCC
AATGTCCCAGAGGGTCTGCTGGCCACTGTCACTGTGTGTCTGACGCTGACCGCCAAGCGC
ATGGCCCGGAAGAACTGCCTGGTGAAGAACCTGGAGGCTGTAGAAACCCTGGGCTCCACG
TCCACCATCTGCTCAGATAAGACAGGGACCCTCACTCAGAACCGCATGACAGTCGCCCAC
ATGTGGTTTGACAACCAGATCCACGAGGCTGACACCACTGAGGACCAGTCAGGGACCTCA
TTTGACAAGAGTTCGCACACCTGGGTGGCCCTGTCTCACATCGCTGGGCTCTGCAATCGC
GCTGTCTTCAAGGGTGGTCAGGACAACATCCCTGTGCTCAAGAGGGATGTGGCTGGGGAT
GCGTCTGAGTCTGCCCTGCTCAAGTGCATCGAGCTGTCCTCTGGCTCCGTGAAGCTGATG
CGTGAACGCAACAAGAAAGTGGCTGAGATTCCCTTCAATTCCACCAACAAATACCAGCTC
TCCATCCATGAGACCGAGGACCCCAACGACAACCGATACCTGCTGGTGATGAAGGGTGCC
CCCGAGCGCATCCTGGACCGCTGCTCCACCATCCTGCTACAGGGCAAGGAGCAGCCTCTG
GACGAGGAAATGAAGGAGGCCTTCCAGAATGCCTACCTTGAGCTCGGTGGCCTGGGCGAG
CGCGTGCTTGGTTTCTGCCATTATTACCTGCCCGAGGAGCAGTTCCCCAAGGGCTTTGCC
TTCGACTGTGATGACGTGAACTTCACCACGGACAACCTCTGCTTTGTGGGCCTCATGTCC
ATGATCGACCCACCCCGGGCAGCCGTCCCTGACGCGGTGGGCAAGTGTCGCAGCGCAGGC
ATCAAGGTCATCATGGTCACCGGCGATCACCCCATCACGGCCAAGGCCATTGCCAAGGGT
GTGGGCATCATCTCTGAGGGCAACGAGACTGTGGAGGACATCGCCGCCCGGCTCAACATT
CCCGTCAGCCAGGTTAACCCCCGGGATGCCAAGGCCTGCGTGATCCACGGCACCGACCTC
AAGGACTTCACCTCCGAGCAAATCGACGAGATCCTGCAGAATCACACCGAGATCGTCTTC
GCCCGCACATCCCCCCAGCAGAAGCTCATCATTGTGGAGGGCTGTCAGAGACAGGGTGCA
ATTGTGGCTGTGACCGGGGATGGTGTGAACGACTCCCCCGCTCTGAAGAAGGCCGACATT
GGGGTGGCCATGGGCATCGCTGGCTCTGACGTCTCCAAGCAGGCAGCTGACATGATCCTG
CTGGACGACAACTTTGCCTCCATCGTCACAGGGGTGGAGGAGGGCCGCCTGATCTTCGAC
AACCTAAAGAAGTCCATTGCCTACACCCTGACCAGCAATATCCCGGAGATCACGCCCTTC
CTGCTGTTCATCATGGCCAACATCCCGCTGCCCCTGGGCACCATCACCATCCTCTGCATC
GATCTGGGCACTGACATGGTCCCTGCCATCTCACTGGCGTACGAGGCTGCCGAAAGCGAC
ATCATGAAGAGACAGCCCAGGAACCCGCGGACGGACAAATTGGTCAATGAGAGACTCATC
AGCATGGCCTACGGGCAGATTGGAATGATCCAGGCTCTCGGTGGCTTCTTCTCTTACTTT
GTGATCCTGGCAGAAAATGGCTTCTTGCCCGGCAACCTGGTGGGCATCCGGCTGAACTGG
GATGACCGCACCGTCAATGACCTGGAAGACAGTTACGGGCAGCAGTGGACATACGAGCAG
AGGAAGGTGGTGGAGTTCACCTGCCACACGGCCTTCTTTGTGAGCATCGTTGTCGTCCAG
TGGGCCGATCTGATCATCTGCAAGACCCGGAGGAACTCGGTCTTCCAGCAGGGCATGAAG
AACAAGATCCTGATCTTCGGGCTGTTTGAGGAGACGGCCCTGGCTGCCTTCCTGTCCTAC
TGCCCCGGCATGGACGTGGCCCTGCGCATGTACCCTCTCAAGCCCAGCTGGTGGTTCTGT
GCCTTCCCCTACAGTTTCCTCATCTTCGTCTACGACGAAATCCGCAAACTCATCCTGCGC
AGGAACCCAGGGGGTTGGGTGGAGAAGGAAACCTACTACTGA
Protein Properties
Number of Residues 1013
Molecular Weight 113132.965
Theoretical pI 5.389
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Sodium/potassium-transporting ATPase subunit alpha-3
MGDKKDDKDSPKKNKGKERRDLDDLKKEVAMTEHKMSVEEVCRKYNTDCVQGLTHSKAQE
ILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAGTEDDPSGDNL
YLGIVLAAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIREGEKMQVNAEEVVVGDL
VEIKGGDRVPADLRIISAHGCKVDNSSLTGESEPQTRSPDCTHDNPLETRNITFFSTNCV
EGTARGVVVATGDRTVMGRIATLASGLEVGKTPIAIEIEHFIQLITGVAVFLGVSFFILS
LILGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGST
STICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGTSFDKSSHTWVALSHIAGLCNR
AVFKGGQDNIPVLKRDVAGDASESALLKCIELSSGSVKLMRERNKKVAEIPFNSTNKYQL
SIHETEDPNDNRYLLVMKGAPERILDRCSTILLQGKEQPLDEEMKEAFQNAYLELGGLGE
RVLGFCHYYLPEEQFPKGFAFDCDDVNFTTDNLCFVGLMSMIDPPRAAVPDAVGKCRSAG
IKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVIHGTDL
KDFTSEQIDEILQNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADI
GVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPF
LLFIMANIPLPLGTITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLVNERLI
SMAYGQIGMIQALGGFFSYFVILAENGFLPGNLVGIRLNWDDRTVNDLEDSYGQQWTYEQ
RKVVEFTCHTAFFVSIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSY
CPGMDVALRMYPLKPSWWFCAFPYSFLIFVYDEIRKLILRRNPGGWVEKETYY
GenBank ID Protein 14424520
UniProtKB/Swiss-Prot ID P13637
UniProtKB/Swiss-Prot Entry Name AT1A3_HUMAN
PDB IDs Not Available
GenBank Gene ID BC009282
GeneCard ID ATP1A3
GenAtlas ID ATP1A3
HGNC ID HGNC:801
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Sverdlov ED, Monastyrskaya GS, Broude NE, Ushkaryov YuA, Allikmets RL, Melkov AM, Smirnov YuV, Malyshev IV, Dulobova IE, Petrukhin KE, et al.: The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit. FEBS Lett. 1987 Jun 15;217(2):275-8. [PubMed:3036582 ]
  3. Ovchinnikov YuA, Monastyrskaya GS, Broude NE, Ushkaryov YuA, Melkov AM, Smirnov YuV, Malyshev IV, Allikmets RL, Kostina MB, Dulubova IE, et al.: Family of human Na+, K+-ATPase genes. Structure of the gene for the catalytic subunit (alpha III-form) and its relationship with structural features of the protein. FEBS Lett. 1988 Jun 6;233(1):87-94. [PubMed:2838329 ]
  4. Sverdlov ED, Monastyrskaia GS, Broude NE, Ushkarev IuA, Melkov AM: [The family of human Na+,K+-ATPase genes. Structure of the gene for isozyme alphaII]. Dokl Akad Nauk SSSR. 1987;297(6):1488-94. [PubMed:2834163 ]
  5. Ovchinnikov YuA, Monastyrskaya GS, Broude NE, Allikmets RL, Ushkaryov YuA, Melkov AM, Smirnov YuV, Malyshev IV, Dulubova IE, Petrukhin KE, et al.: The family of human Na+,K+-ATPase genes. A partial nucleotide sequence related to the alpha-subunit. FEBS Lett. 1987 Mar 9;213(1):73-80. [PubMed:3030810 ]
  6. de Carvalho Aguiar P, Sweadner KJ, Penniston JT, Zaremba J, Liu L, Caton M, Linazasoro G, Borg M, Tijssen MA, Bressman SB, Dobyns WB, Brashear A, Ozelius LJ: Mutations in the Na+/K+ -ATPase alpha3 gene ATP1A3 are associated with rapid-onset dystonia parkinsonism. Neuron. 2004 Jul 22;43(2):169-75. [PubMed:15260953 ]