Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Sodium/potassium-transporting ATPase subunit alpha-1 (Na( )/K( ) ATPase alpha-1 subunit) (EC 3.6.3.9) (Sodium pump subunit alpha-1)

 AT1A1_RAT               Reviewed;        1023 AA.
P06685; Q64609;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
28-FEB-2018, entry version 189.
RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-1;
Short=Na(+)/K(+) ATPase alpha-1 subunit;
EC=3.6.3.9;
AltName: Full=Sodium pump subunit alpha-1;
Flags: Precursor;
Name=Atp1a1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain, and Kidney;
PubMed=3028470; DOI=10.1021/bi00373a001;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=2822682; DOI=10.1093/oxfordjournals.jbchem.a122039;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2822726; DOI=10.1083/jcb.105.4.1855;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 157-162; 597-605; 630-647; 662-671 AND 744-773,
AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 489-533.
TISSUE=Brain;
PubMed=2994074; DOI=10.1073/pnas.82.18.6357;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
PubMed=2166579; DOI=10.1016/0167-4781(90)90099-N;
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).
[8]
PHOSPHORYLATION BY CAMP-DEPENDENT KINASE.
PubMed=7510709;
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).
[9]
PHOSPHORYLATION AT SER-23 AND SER-943.
PubMed=9435504;
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:C1981-C1986(1997).
[10]
PHOSPHORYLATION AT TYR-10.
PubMed=10473631; DOI=10.1091/mbc.10.9.2847;
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).
[11]
PROTEIN SEQUENCE OF N-TERMINUS, AND PHOSPHORYLATION AT SER-16 AND
SER-23 BY PROTEIN KINASE C.
PubMed=7775468; DOI=10.1074/jbc.270.23.14072;
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).
[12]
BINDING SITE FOR PHOSPHOINOSITIDE-3 KINASE, AND MUTAGENESIS.
PubMed=10823893; DOI=10.1073/pnas.100128297;
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).
[13]
INTERACTION WITH FXYD3.
PubMed=15743908; DOI=10.1091/mbc.E04-10-0878;
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).
[14]
INTERACTION WITH FXYD1.
PubMed=17283221; DOI=10.1096/fj.06-7269com;
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).
[15]
PHOSPHORYLATION, DEPHOSPHORYLATION, AND INTERACTION WITH SIK1.
PubMed=17939993; DOI=10.1073/pnas.0706838104;
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).
[16]
INTERACTION WITH FXYD1.
PubMed=19339511; DOI=10.1152/ajpcell.00523.2008;
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:C1346-C1355(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-47; SER-228;
SER-452 AND SER-484, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
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).
[18]
INTERACTION WITH FXYD1.
PubMed=23532852; DOI=10.1074/jbc.M113.460956;
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).
[19]
STRUCTURE BY NMR OF 383-595 ALONE AND IN COMPLEX WITH ATP, AND
ATP-BINDING SITE.
PubMed=12730684; DOI=10.1038/nsb924;
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).
-!- 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.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Na(+)(In) + K(+)(Out) = ADP +
phosphate + Na(+)(Out) + K(+)(In).
-!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
catalytic alpha subunit, an auxiliary non-catalytic beta subunit
and an additional regulatory subunit. Interacts with regulatory
subunit FXYD1 (PubMed:17283221, PubMed:19339511, PubMed:23532852).
Interacts with regulatory subunit FXYD3 (PubMed:15743908).
Interacts with SLC35G1 and STIM1 (By similarity). Interacts with
SIK1 (PubMed:17939993). {ECO:0000250|UniProtKB:P05023,
ECO:0000269|PubMed:15743908, ECO:0000269|PubMed:17283221,
ECO:0000269|PubMed:17939993, ECO:0000269|PubMed:19339511,
ECO:0000269|PubMed:23532852}.
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein
{ECO:0000255}.
-!- PTM: Phosphorylation on Tyr-10 modulates pumping activity.
Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1
to PKC. Dephosphorylation by protein phosphatase 2A (PP2A)
following increases in intracellular sodium, leading to increase
catalytic activity. {ECO:0000269|PubMed:10473631,
ECO:0000269|PubMed:17939993, ECO:0000269|PubMed:7510709,
ECO:0000269|PubMed:7775468, ECO:0000269|PubMed:9435504}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M14511; AAA40775.1; -; mRNA.
EMBL; X05882; CAA29306.1; -; mRNA.
EMBL; M28647; AAA41671.1; -; mRNA.
EMBL; BC061968; AAH61968.1; -; mRNA.
EMBL; M11733; AAA40783.1; -; mRNA.
EMBL; X53233; CAA37325.1; -; Genomic_DNA.
EMBL; X53234; CAA37326.1; -; Genomic_DNA.
PIR; A24639; A24639.
RefSeq; NP_036636.1; NM_012504.1.
UniGene; Rn.217534; -.
UniGene; Rn.2992; -.
PDB; 1MO7; NMR; -; A=386-595.
PDB; 1MO8; NMR; -; A=386-595.
PDBsum; 1MO7; -.
PDBsum; 1MO8; -.
ProteinModelPortal; P06685; -.
SMR; P06685; -.
BioGrid; 246399; 10.
ELM; P06685; -.
IntAct; P06685; 4.
MINT; P06685; -.
STRING; 10116.ENSRNOP00000045650; -.
BindingDB; P06685; -.
ChEMBL; CHEMBL3010; -.
iPTMnet; P06685; -.
PhosphoSitePlus; P06685; -.
PaxDb; P06685; -.
PRIDE; P06685; -.
Ensembl; ENSRNOT00000040430; ENSRNOP00000045650; ENSRNOG00000030019.
GeneID; 24211; -.
KEGG; rno:24211; -.
UCSC; RGD:2167; rat.
CTD; 476; -.
RGD; 2167; Atp1a1.
eggNOG; KOG0203; Eukaryota.
eggNOG; COG0474; LUCA.
GeneTree; ENSGT00890000139334; -.
HOVERGEN; HBG004298; -.
InParanoid; P06685; -.
KO; K01539; -.
OMA; ARIMPEQ; -.
OrthoDB; EOG091G01BB; -.
PhylomeDB; P06685; -.
Reactome; R-RNO-5578775; Ion homeostasis.
Reactome; R-RNO-936837; Ion transport by P-type ATPases.
SABIO-RK; P06685; -.
EvolutionaryTrace; P06685; -.
PRO; PR:P06685; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000030019; -.
Genevisible; P06685; RN.
GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
GO; GO:0005901; C:caveola; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0005768; C:endosome; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:1903561; C:extracellular vesicle; ISO:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043209; C:myelin sheath; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0014069; C:postsynaptic density; ISO:RGD.
GO; GO:0043234; C:protein complex; ISO:RGD.
GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:RGD.
GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
GO; GO:0043531; F:ADP binding; IDA:RGD.
GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IDA:BHF-UCL.
GO; GO:0016791; F:phosphatase activity; ISO:RGD.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:RGD.
GO; GO:0030955; F:potassium ion binding; IDA:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0031402; F:sodium ion binding; IDA:RGD.
GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; IDA:UniProtKB.
GO; GO:1990239; F:steroid hormone binding; ISO:RGD.
GO; GO:0090662; P:ATP hydrolysis coupled transmembrane transport; IDA:BHF-UCL.
GO; GO:0060048; P:cardiac muscle contraction; TAS:BHF-UCL.
GO; GO:0030007; P:cellular potassium ion homeostasis; ISO:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:RGD.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISO:RGD.
GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:RGD.
GO; GO:0015988; P:energy coupled proton transmembrane transport, against electrochemical gradient; TAS:RGD.
GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IC:BHF-UCL.
GO; GO:0060081; P:membrane hyperpolarization; IMP:RGD.
GO; GO:0086009; P:membrane repolarization; ISO:RGD.
GO; GO:0031947; P:negative regulation of glucocorticoid biosynthetic process; ISO:RGD.
GO; GO:0045822; P:negative regulation of heart contraction; ISO:RGD.
GO; GO:0045823; P:positive regulation of heart contraction; ISO:RGD.
GO; GO:0045989; P:positive regulation of striated muscle contraction; ISO:RGD.
GO; GO:0010107; P:potassium ion import; IDA:RGD.
GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL.
GO; GO:0006813; P:potassium ion transport; IDA:RGD.
GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:RGD.
GO; GO:0002028; P:regulation of sodium ion transport; IDA:UniProtKB.
GO; GO:0002026; P:regulation of the force of heart contraction; ISO:RGD.
GO; GO:0055119; P:relaxation of cardiac muscle; TAS:BHF-UCL.
GO; GO:0042493; P:response to drug; ISO:RGD.
GO; GO:1903416; P:response to glycoside; ISO:RGD.
GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:BHF-UCL.
GO; GO:0006814; P:sodium ion transport; IDA:RGD.
CDD; cd02608; P-type_ATPase_Na-K_like; 1.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 2.
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR005775; P-type_ATPase_IIC.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell membrane;
Complete proteome; Direct protein sequencing; Hydrolase;
Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Potassium; Potassium transport; Reference proteome;
Sodium; Sodium transport; Sodium/potassium transport; Transmembrane;
Transmembrane helix; Transport.
PROPEP 1 5 {ECO:0000269|PubMed:7775468}.
/FTId=PRO_0000002489.
CHAIN 6 1023 Sodium/potassium-transporting ATPase
subunit alpha-1.
/FTId=PRO_0000002490.
TOPO_DOM 6 87 Cytoplasmic. {ECO:0000255}.
TRANSMEM 88 108 Helical. {ECO:0000255}.
TOPO_DOM 109 131 Extracellular. {ECO:0000255}.
TRANSMEM 132 152 Helical. {ECO:0000255}.
TOPO_DOM 153 288 Cytoplasmic. {ECO:0000255}.
TRANSMEM 289 308 Helical. {ECO:0000255}.
TOPO_DOM 309 320 Extracellular. {ECO:0000255}.
TRANSMEM 321 338 Helical. {ECO:0000255}.
TOPO_DOM 339 772 Cytoplasmic. {ECO:0000255}.
TRANSMEM 773 792 Helical. {ECO:0000255}.
TOPO_DOM 793 802 Extracellular. {ECO:0000255}.
TRANSMEM 803 823 Helical. {ECO:0000255}.
TOPO_DOM 824 843 Cytoplasmic. {ECO:0000255}.
TRANSMEM 844 866 Helical. {ECO:0000255}.
TOPO_DOM 867 918 Extracellular. {ECO:0000255}.
TRANSMEM 919 938 Helical. {ECO:0000255}.
TOPO_DOM 939 951 Cytoplasmic. {ECO:0000255}.
TRANSMEM 952 970 Helical. {ECO:0000255}.
TOPO_DOM 971 985 Extracellular. {ECO:0000255}.
TRANSMEM 986 1006 Helical. {ECO:0000255}.
TOPO_DOM 1007 1023 Cytoplasmic. {ECO:0000255}.
REGION 82 84 Phosphoinositide-3 kinase binding.
ACT_SITE 376 376 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 717 717 Magnesium. {ECO:0000250}.
METAL 721 721 Magnesium. {ECO:0000250}.
BINDING 487 487 ATP. {ECO:0000269|PubMed:12730684}.
MOD_RES 9 9 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 10 10 Phosphotyrosine.
{ECO:0000269|PubMed:10473631}.
MOD_RES 16 16 Phosphoserine; by PKC.
{ECO:0000269|PubMed:7775468}.
MOD_RES 21 21 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 23 23 Phosphoserine; by PKC.
{ECO:0000269|PubMed:7775468,
ECO:0000269|PubMed:9435504}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 260 260 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 542 542 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05023}.
MOD_RES 661 661 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 668 668 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 943 943 Phosphoserine; by PKA.
{ECO:0000269|PubMed:9435504}.
MUTAGEN 16 16 S->A: Dopamine fails to increase
phosphoinositide-3 kinase activity and to
promote its interaction with Na(+)/K(+)
ATPase. {ECO:0000269|PubMed:10823893}.
MUTAGEN 83 83 P->R: Dopamine fails to increase
phosphoinositide-3 kinase activity and to
promote its interaction with Na(+)/K(+)
ATPase. {ECO:0000269|PubMed:10823893}.
CONFLICT 68 69 AA -> PV (in Ref. 3; AAA41671).
{ECO:0000305}.
CONFLICT 175 175 G -> E (in Ref. 3; AAA41671).
{ECO:0000305}.
CONFLICT 188 188 G -> V (in Ref. 3; AAA41671).
{ECO:0000305}.
CONFLICT 335 335 G -> V (in Ref. 3; AAA41671).
{ECO:0000305}.
STRAND 394 396 {ECO:0000244|PDB:1MO7}.
STRAND 403 405 {ECO:0000244|PDB:1MO7}.
HELIX 416 427 {ECO:0000244|PDB:1MO7}.
STRAND 431 435 {ECO:0000244|PDB:1MO7}.
STRAND 438 440 {ECO:0000244|PDB:1MO7}.
HELIX 442 444 {ECO:0000244|PDB:1MO8}.
STRAND 447 449 {ECO:0000244|PDB:1MO7}.
TURN 451 453 {ECO:0000244|PDB:1MO7}.
HELIX 454 461 {ECO:0000244|PDB:1MO7}.
TURN 462 464 {ECO:0000244|PDB:1MO7}.
HELIX 467 473 {ECO:0000244|PDB:1MO7}.
STRAND 478 480 {ECO:0000244|PDB:1MO7}.
TURN 483 485 {ECO:0000244|PDB:1MO8}.
STRAND 489 494 {ECO:0000244|PDB:1MO7}.
STRAND 496 500 {ECO:0000244|PDB:1MO7}.
STRAND 502 509 {ECO:0000244|PDB:1MO7}.
HELIX 511 515 {ECO:0000244|PDB:1MO7}.
STRAND 518 521 {ECO:0000244|PDB:1MO7}.
STRAND 526 529 {ECO:0000244|PDB:1MO8}.
HELIX 532 546 {ECO:0000244|PDB:1MO7}.
STRAND 556 558 {ECO:0000244|PDB:1MO8}.
TURN 562 564 {ECO:0000244|PDB:1MO7}.
TURN 572 574 {ECO:0000244|PDB:1MO7}.
SEQUENCE 1023 AA; 113054 MW; 85E98233EE6C18E9 CRC64;
MGKGVGRDKY EPAAVSEHGD KKSKKAKKER DMDELKKEVS MDDHKLSLDE LHRKYGTDLS
RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SMLLWIGAIL CFLAYGIRSA
TEEEPPNDDL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI
NAEDVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR
NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWFA
LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI EVCCGSVMEM REKYTKIVEI
PFNSTNKYQL SIHKNPNASE PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN
AYLELGGLGE RVLGFCHLLL PDEQFPEGFQ FDTDEVNFPV DNLCFVGLIS MIDPPRAAVP
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVNQVNPRDA
KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN
DSPALKKADI GVAMGIVGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL
TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK
TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRETW DDRWINDVED
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE
ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE
TYY


Related products :

Catalog number Product name Quantity
ER451 Sodium per potassium-transporting ATPase subunit alpha-3 Elisa Kit 96T
AT1A1_PIG Pig ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-1 96T
EIAAB45649 ATP6A1,ATP6V1A,ATP6V1A1,Homo sapiens,Human,Vacuolar ATPase isoform VA68,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,VPP2,V-type proton ATPase catalytic subunit A
EIAAB45652 Atp6a1,Atp6a2,Atp6v1a,Atp6v1a1,Mouse,Mus musculus,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45651 ATP6A1,ATP6V1A,ATP6V1A1,Bos taurus,Bovine,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
H1745 Sodium potassium-transporting ATPase subunit alpha-2 (ATP1A2), Rat, ELISA Kit 96T
AT1A2_BOVIN Bovine ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-2 96T
H1749 Sodium potassium-transporting ATPase subunit alpha-3 (ATP1A3), Rat, ELISA Kit 96T
H1744 Sodium potassium-transporting ATPase subunit alpha-2 (ATP1A2), Pig, ELISA Kit 96T
AT1A1_RABIT Rabbit ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-1 96T
AT1A2_MOUSE Mouse ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-2 96T
AT1A2_HUMAN Human ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-2 96T
E1431r Bovine ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-1 96T
H1732 Sodium potassium-transporting ATPase subunit alpha-1 (ATP1A1), Dog, ELISA Kit 96T
AT1A1_HUMAN Human ELISA Kit FOR Sodium per potassium-transporting ATPase subunit alpha-1 96T
CSB-EL002322RA Rat Sodium per potassium-transporting ATPase subunit alpha-1(ATP1A1) ELISA kit 96T
H1752 Sodium potassium-transporting ATPase subunit alpha-4 (ATP1A4), Rat, ELISA Kit 96T
H1736 Sodium potassium-transporting ATPase subunit alpha-1 (ATP1A1), Pig, ELISA Kit 96T
H1738 Sodium potassium-transporting ATPase subunit alpha-1 (ATP1A1), Rat, ELISA Kit 96T
EIAAB45650 ATP6A1,ATP6V1A,ATP6V1A1,Pig,Sus scrofa,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
H1747 Sodium potassium-transporting ATPase subunit alpha-3 (ATP1A3), Human, ELISA Kit 96T
H1746 Sodium potassium-transporting ATPase subunit alpha-3 (ATP1A3), Chicken, ELISA Kit 96T
H1748 Sodium potassium-transporting ATPase subunit alpha-3 (ATP1A3), Mouse, ELISA Kit 96T
H1737 Sodium potassium-transporting ATPase subunit alpha-1 (ATP1A1), Rabbit, ELISA Kit 96T
H1734 Sodium potassium-transporting ATPase subunit alpha-1 (ATP1A1), Human, ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur