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

 AT1A1_RABIT             Reviewed;        1023 AA.
Q9N0Z6;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
28-FEB-2018, entry version 104.
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;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11738066; DOI=10.1016/S0008-6363(01)00412-6;
Fransen P., Hendrickx J., Brutsaert D.L., Sys S.U.;
"Distribution and role of Na(+)/K(+) ATPase in endocardial
endothelium.";
Cardiovasc. Res. 52:487-499(2001).
-!- 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 (By
similarity). May contribute to blood-heart barrier properties of
endocardial endothelium and may control cardiac performance via
endothelial Na(+)/H(+) exchange. {ECO:0000250,
ECO:0000269|PubMed:11738066}.
-!- 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. Interacts with regulatory subunit FXYD3. Interacts
with SIK1. Interacts with SLC35G1 and STIM1.
{ECO:0000250|UniProtKB:P05023, ECO:0000250|UniProtKB:P06685}.
-!- INTERACTION:
Q9TT37:ATP1B1; NbExp=2; IntAct=EBI-9685690, EBI-9685670;
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Expressed in endocardial endothelial cells.
{ECO:0000269|PubMed:11738066}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIC subfamily. {ECO:0000305}.
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EMBL; AF235024; AAF60310.2; -; mRNA.
RefSeq; NP_001156546.1; NM_001163074.1.
UniGene; Ocu.2457; -.
ProteinModelPortal; Q9N0Z6; -.
SMR; Q9N0Z6; -.
IntAct; Q9N0Z6; 2.
STRING; 9986.ENSOCUP00000024821; -.
PRIDE; Q9N0Z6; -.
GeneID; 100302415; -.
KEGG; ocu:100302415; -.
CTD; 476; -.
eggNOG; KOG0203; Eukaryota.
eggNOG; COG0474; LUCA.
HOGENOM; HOG000265622; -.
HOVERGEN; HBG004298; -.
InParanoid; Q9N0Z6; -.
KO; K01539; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL.
GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; IEA:UniProtKB-EC.
GO; GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB.
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; 3.
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;
Acetylation; ATP-binding; Cell membrane; Complete proteome; 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:0000250}.
/FTId=PRO_0000305979.
CHAIN 6 1023 Sodium/potassium-transporting ATPase
subunit alpha-1. {ECO:0000250}.
/FTId=PRO_0000305980.
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.
{ECO:0000250}.
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:0000250}.
MOD_RES 9 9 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 10 10 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06685}.
MOD_RES 16 16 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P06685}.
MOD_RES 21 21 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000250|UniProtKB:P06685}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000250|UniProtKB:P06685}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 260 260 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8VDN2}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000250|UniProtKB:P06685}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000250|UniProtKB:P06685}.
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:0000250|UniProtKB:P06685}.
SEQUENCE 1023 AA; 112994 MW; F6BA59C8979F574D CRC64;
MGKGVGRDKY EPAAVSEHGD KKGKKAKKER DMDELKKEVS MDDHKLSLDE LHRKYGTDLS
RGLTTARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SMLLWIGAIL CFLAYGILAA
TEEDFDNDNL YLGVVLAAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI
NAEDVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR
NIAFFSTNCV EGTARGIVIY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWLA
LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI ELCCGSVKEM RERYTKIVEI
PFNSTNKYQL SIHKNLNANE PRHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN
AYLELGGLGE RVLGFCHLLL PDEQFPEGFQ FDTDEVNFPV DNLCFIGLIS MIDPPRAAVP
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA
KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN
DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL
TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK
TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRVDW DDRWINDVED
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE
ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV YDEIRKLIIR RRPGGWVEKE
TYY


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