ATPase, Na+/K+ transporting, alpha 1

ATP1A1

Identifiers

ATP1A1, ATPase, Na+/K+ transporting, alpha 1, ATPase Na+/K+ transporting subunit alpha 1

External IDs

MGI: 88105 HomoloGene: 564 GeneCards: ATP1A1

Gene ontology
Molecular function	• steroid hormone binding • nucleotide binding • chaperone binding • protein domain specific binding • phosphatase activity • ADP binding • potassium ion binding • sodium ion binding • sodium:potassium-exchanging ATPase activity • metal ion binding • phosphatidylinositol 3-kinase binding • protein binding • ankyrin binding • hydrolase activity • ATP binding • protein kinase binding
Cellular component	• integral component of membrane • extracellular vesicle • endosome • Golgi apparatus • membrane • intercalated disc • T-tubule • melanosome • myelin sheath • plasma membrane • protein complex • sodium:potassium-exchanging ATPase complex • basolateral plasma membrane • apical plasma membrane • endoplasmic reticulum • caveola • membrane raft • sarcolemma • extracellular exosome • postsynaptic density of dendrite
Biological process	• cellular response to steroid hormone stimulus • regulation of cardiac conduction • membrane hyperpolarization • regulation of sodium ion transport • regulation of the force of heart contraction • negative regulation of heart contraction • sodium ion transport • cellular sodium ion homeostasis • sodium ion export from cell • cell communication by electrical coupling involved in cardiac conduction • response to glycoside • ion transport • cellular potassium ion homeostasis • regulation of blood pressure • potassium ion transport • positive regulation of heart contraction • ion transmembrane transport • cellular response to mechanical stimulus • regulation of cardiac muscle cell contraction • membrane repolarization • positive regulation of striated muscle contraction • potassium ion import • negative regulation of glucocorticoid biosynthetic process • membrane repolarization during cardiac muscle cell action potential • relaxation of cardiac muscle • response to drug • dephosphorylation • potassium ion import across plasma membrane • establishment or maintenance of transmembrane electrochemical gradient • ATP hydrolysis coupled transmembrane transport • cardiac muscle cell action potential involved in contraction • transport
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


476


11928

Ensembl


ENSG00000163399


ENSMUSG00000033161

UniProt


P05023 Q5TC02


Q8VDN2

RefSeq (mRNA)


NM_000701 NM_001001586 NM_001160233 NM_001160234


NM_144900

RefSeq (protein)


NP_000692 NP_001153705 NP_001153706


NP_659149

Location (UCSC)

Chr 1: 116.37 – 116.41 Mb

Chr 3: 101.58 – 101.6 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Gastric H⁺/K⁺-ATPase, N terminal domain

tfe-induded structure of the n-terminal domain of pig gastric h/k-atpase

Identifiers

Symbol

H-K_ATPase_N

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Sodium/potassium-transporting ATPase subunit alpha-1 is an enzyme that in humans is encoded by the ATP1A1 gene.^[3]

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.^[3]

In melanocytic cells ATP1A1 gene expression may be regulated by MITF.^[4]

Clinical relevance

Mutations in this gene have been associated with aldosterone-producing adenomas and secondary hypertension. (PMID 23416519).

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 "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. PMID 19067971. doi:10.1111/j.1755-148X.2008.00505.x.

Lingrel JB, Orlowski J, Shull MM, Price EM (1990). "Molecular genetics of Na,K-ATPase.". Prog. Nucleic Acid Res. Mol. Biol. 38: 37–89. PMID 2158121. doi:10.1016/S0079-6603(08)60708-4.
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. PMID 11404365. doi:10.1074/jbc.R100023200.
Wangemann P (2002). "K⁺ cycling and the endocochlear potential.". Hear. Res. 165 (1-2): 1–9. PMID 12031509. doi:10.1016/S0378-5955(02)00279-4.
Xie Z, Cai T (2004). "Na⁺-K⁺--ATPase-mediated signal transduction: from protein interaction to cellular function.". Mol. Interv. 3 (3): 157–68. PMID 14993422. doi:10.1124/mi.3.3.157.
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. PMID 1970326. doi:10.1016/0888-7543(90)90475-A.
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. PMID 1975705. doi:10.1126/science.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. PMID 2842249. doi:10.1016/0888-7543(88)90094-8.
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. PMID 2887455. doi:10.1016/0014-5793(87)80366-6.
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. PMC 299443 . PMID 2891135. doi:10.1073/pnas.84.22.7901.
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. PMID 3030810. doi:10.1016/0014-5793(87)81467-9.
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. PMC 305017 . PMID 3035563. doi:10.1073/pnas.84.12.4039.
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. PMID 3036582. doi:10.1016/0014-5793(87)80677-4.
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. PMID 7536695. doi:10.1016/0378-1119(94)00812-7.
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. PMID 7711835. doi:10.3109/09687689409160435.
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. PMID 7775468. doi:10.1074/jbc.270.23.14072.
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. doi:10.1161/01.hyp.24.3.260.
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. PMID 8391840. doi:10.1016/0005-2736(93)90200-J.
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. PMC 507599 . PMID 8833915. doi:10.1172/JCI118960.

PDB gallery

1mo7: ATPase

1mo8: ATPase

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

3.6.2

3.6.3-4: ATPase

3.6.3

Cu++ (3.6.3.4)	Menkes/ATP7A Wilson/ATP7B
Ca+ (3.6.3.8)	SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2
Na+/K+ (3.6.3.9)	ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4
H+/K+ (3.6.3.10)	ATP4A
Other P-type ATPase	ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_αi GNAI1 GNAI2 GNAI3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13 Transducin GNAT1 GNAT2 Gustducin GNAT3
3.6.5.2: Small GTPase > Ras superfamily	Rho family of GTPases: Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 2 3 RhoG RhoBTB 1 2 RhoH Rho A B C Rnd 1 2 3 RhoDF RhoF RhoD other: Ras HRAS KRAS NRAS Rab RAB23 RAB27 Arf ARF6 SAR1B ARL13B ARL6 Ran Rheb Rap RGK
3.6.5.3: Protein-synthesizing GTPase	Prokaryotic IF-2 EF-Tu EF-G Eukaryotic
3.6.5.5-6: Polymerization motors	Dynamin Tubulin

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ATPase, Na+/K+ transporting, alpha 1

Clinical relevance

References

Further reading