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Sequence of AT1A1_RAT

EC Number:7.2.2.13

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Na+/K+-exchanging ATPase
P06685
Rattus norvegicus
1023
113054
Reaction
ATP + H2O + Na+[side 1] + K+[side 2] = ADP + phosphate + Na+[side 2] + K+[side 1]
Other sequences found for EC No. 7.2.2.13

General information:

Sequence
show sequence in fasta format
   0 MGKGVGRDKY EPAAVSEHGD KKSKKAKKER DMDELKKEVS MDDHKLSLDE LHRKYGTDLS
  60 RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SMLLWIGAIL CFLAYGIRSA
 120 TEEEPPNDDL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI
 180 NAEDVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR
 240 NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV
 300 FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
 360 LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWFA
 420 LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI EVCCGSVMEM REKYTKIVEI
 480 PFNSTNKYQL SIHKNPNASE PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN
 540 AYLELGGLGE RVLGFCHLLL PDEQFPEGFQ FDTDEVNFPV DNLCFVGLIS MIDPPRAAVP
 600 DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVNQVNPRDA
 660 KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN
 720 DSPALKKADI GVAMGIVGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL
 780 TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK
 840 TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRETW DDRWINDVED
 900 SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE
 960 ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE
1020 TYY
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
7648
Shull G.E.,Greeb J.,Lingrel J.B.
Molecular cloning of three distinct forms of the Na+,K+-ATPase alpha-subunit from rat brain.
Biochemistry
25
8125-8132
1986
7649
Hara Y.,Urayama O.,Kawakami K.,Nojima H.,Nagamune H.,Kojima T.,Ohta T.,Nagano K.,Nakao M.
Primary structures of two types of alpha-subunit of rat brain Na+,K+,-ATPase deduced from cDNA sequences.
J. Biochem.
102
43-58
1987
7650
Herrera V.L.M.,Emanuel J.R.,Ruiz-Opazo N.,Levenson R.,Nadal-Ginard B.
Three differentially expressed Na,K-ATPase alpha subunit isoforms: structural and functional implications.
J. Cell Biol.
105
1855-1865
1987
7651
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
7653
Schneider J.W.,Mercer R.W.,Caplan M.,Emanuel J.R.,Sweadner K.J.,Benz E.J. Jr.,Levenson R.
Molecular cloning of rat brain Na,K-ATPase alpha-subunit cDNA.
Proc. Natl. Acad. Sci. U.S.A.
82
6357-6361
1985
7654
Yagawa Y.,Kawakami K.,Nagano K.
Cloning and analysis of the 5'-flanking region of rat Na+/K(+)-ATPase alpha 1 subunit gene.
Biochim. Biophys. Acta
1049
286-292
1990
7655
Fisone G.,Cheng S.X.-J.,Nairn A.C.,Czernik A.J.,Hemmings H.C. Jr.,Hoeoeg J.-O.,Bertorello A.M.,Kaiser R.,Bergman T.,Joernvall H.,Aperia A.,Greengard P.
Identification of the phosphorylation site for cAMP-dependent protein kinase on Na+,K(+)-ATPase and effects of site-directed mutagenesis.
J. Biol. Chem.
269
9368-9373
1994
7656
Cheng X.J.,Hoeoeg J.O.,Nairn A.C.,Greengard P.,Aperia A.
Regulation of rat Na(+)-K(+)-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA.
Am. J. Physiol.
273
0-0
1997
7657
Feraille E.,Carranza M.L.,Gonin S.,Beguin P.,Pedemonte C.,Rousselot M.,Caverzasio J.,Geering K.,Martin P.Y.,Favre H.
Insulin-induced stimulation of Na+,K(+)-ATPase activity in kidney proximal tubule cells depends on phosphorylation of the alpha-subunit at Tyr-10.
Mol. Biol. Cell
10
2847-2859
1999
7658
Feschenko M.S.,Sweadner K.J.
Structural basis for species-specific differences in the phosphorylation of Na,K-ATPase by protein kinase C.
J. Biol. Chem.
270
14072-14077
1995
7659
Yudowski G.A.,Efendiev R.,Pedemonte C.H.,Katz A.I.,Berggren P.-O.,Bertorello A.M.
Phosphoinositide-3 kinase binds to a proline-rich motif in the Na+, K+-ATPase alpha subunit and regulates its trafficking.
Proc. Natl. Acad. Sci. U.S.A.
97
6556-6561
2000
7660
Crambert G.,Li C.,Claeys D.,Geering K.
FXYD3 (Mat-8), a new regulator of Na,K-ATPase.
Mol. Biol. Cell
16
2363-2371
2005
7661
Pavlovic D.,Fuller W.,Shattock M.J.
The intracellular region of FXYD1 is sufficient to regulate cardiac Na/K ATPase.
FASEB J.
21
1539-1546
2007
7662
Sjostrom M.,Stenstrom K.,Eneling K.,Zwiller J.,Katz A.I.,Takemori H.,Bertorello A.M.
SIK1 is part of a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process.
Proc. Natl. Acad. Sci. U.S.A.
104
16922-16927
2007
7663
Fuller W.,Howie J.,McLatchie L.M.,Weber R.J.,Hastie C.J.,Burness K.,Pavlovic D.,Shattock M.J.
FXYD1 phosphorylation in vitro and in adult rat cardiac myocytes: threonine 69 is a novel substrate for protein kinase C.
Am. J. Physiol.
296
0-0
2009
7664
Lundby A.,Secher A.,Lage K.,Nordsborg N.B.,Dmytriyev A.,Lundby C.,Olsen J.V.
Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.
Nat. Commun.
3
876-876
2012
7665
Wypijewski K.J.,Howie J.,Reilly L.,Tulloch L.B.,Aughton K.L.,McLatchie L.M.,Shattock M.J.,Calaghan S.C.,Fuller W.
A separate pool of cardiac phospholemman that does not regulate or associate with the sodium pump: multimers of phospholemman in ventricular muscle.
J. Biol. Chem.
288
13808-13820
2013
7666
Lassuthova P.,Rebelo A.P.,Ravenscroft G.,Lamont P.J.,Davis M.R.,Manganelli F.,Feely S.M.,Bacon C.,Brozkova D.S.,Haberlova J.,Mazanec R.,Tao F.,Saghira C.,Abreu L.,Courel S.,Powell E.,Buglo E.,Bis D.M.,Baxter M.F.,Ong R.W.,Marns L.,Lee Y.C.,Bai Y.,Isom D.G.,Barro-Soria R.,Chung K.W.,Scherer S.S.,Larsson H.P.,Laing N.G.,Choi B.O.,Seeman P.,Shy M.E.,Santoro L.,Zuchner S.
Mutations in ATP1A1 Cause Dominant Charcot-Marie-Tooth Type 2.
Am. J. Hum. Genet.
102
505-514
2018
7667
Schlingmann K.P.,Bandulik S.,Mammen C.,Tarailo-Graovac M.,Holm R.,Baumann M.,Koenig J.,Lee J.J.Y.,Droegemoeller B.,Imminger K.,Beck B.B.,Altmueller J.,Thiele H.,Waldegger S.,Van't Hoff W.,Kleta R.,Warth R.,van Karnebeek C.D.M.,Vilsen B.,Bockenhauer D.,Konrad M.
Germline de novo mutations in ATP1A1 cause renal hypomagnesemia, refractory seizures, and intellectual disability.
Am. J. Hum. Genet.
103
808-816
2018
7668
Lerner M.,Lemke D.,Bertram H.,Schillers H.,Oberleithner H.,Caplan M.J.,Reinhardt J.
An extracellular loop of the human non-gastric H,K-ATPase alpha-subunit is involved in apical plasma membrane polarization.
Cell. Physiol. Biochem.
18
75-84
2006
7669
Hilge M.,Siegal G.,Vuister G.W.,Guntert P.,Gloor S.M.,Abrahams J.P.
ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase.
Nat. Struct. Biol.
10
468-474
2003