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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_RHIMB             Reviewed;        1023 AA.
P30714;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
16-MAY-2003, sequence version 2.
12-SEP-2018, entry version 122.
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;
Rhinella marina (Cane toad) (Bufo marinus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae;
Rhinella.
NCBI_TaxID=8386;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Urinary bladder urothelium;
PubMed=1380956;
Jaisser F., Canessa C.M., Horisberger J.-D., Rossier B.C.;
"Primary sequence and functional expression of a novel ouabain-
resistant Na,K-ATPase. The beta subunit modulates potassium activation
of the Na,K-pump.";
J. Biol. Chem. 267:16895-16903(1992).
[2]
SEQUENCE REVISION TO 835-836.
Jaisser F.;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[3]
PHOSPHORYLATION AT THR-15 AND SER-16 BY PROTEIN KINASE C, AND
PHOSPHORYLATION AT SER-943 BY CAMP-DEPENDENT KINASE.
PubMed=7929106;
Beguin P., Beggah A.T., Chibalin A.V., Burgener-Kairuz P., Jaisser F.,
Mathews P.M., Rossier B.C., Cotecchia S., Geering K.;
"Phosphorylation of the Na,K-ATPase alpha-subunit by protein kinase A
and C in vitro and in intact cells. Identification of a novel motif
for PKC-mediated phosphorylation.";
J. Biol. Chem. 269:24437-24445(1994).
-!- 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).
-!- ACTIVITY REGULATION: This alpha subunit is resistant to ouabain.
-!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
catalytic alpha subunit, an auxiliary non-catalytic beta subunit
and an additional regulatory subunit. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Mainly expressed in kidney. Found in bladder,
colon, eye, and testis. Found in low levels in brain, heart,
spleen and liver.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIC subfamily. {ECO:0000305}.
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EMBL; Z11798; CAA77842.2; -; mRNA.
PIR; A43451; S24650.
ProteinModelPortal; P30714; -.
SMR; P30714; -.
iPTMnet; P30714; -.
PRIDE; P30714; -.
HOVERGEN; HBG004298; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; IEA:UniProtKB-EC.
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;
ATP-binding; Cell membrane; Hydrolase; Ion transport; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Potassium; Potassium transport; Sodium; Sodium transport;
Sodium/potassium transport; Transmembrane; Transmembrane helix;
Transport.
PROPEP 1 5 {ECO:0000250}.
/FTId=PRO_0000002501.
CHAIN 6 1023 Sodium/potassium-transporting ATPase
subunit alpha-1.
/FTId=PRO_0000002502.
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 Interaction with phosphoinositide-3
kinase. {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 15 15 Phosphothreonine; by PKC.
{ECO:0000269|PubMed:7929106}.
MOD_RES 16 16 Phosphoserine; by PKC.
{ECO:0000269|PubMed:7929106}.
MOD_RES 943 943 Phosphoserine; by PKA.
{ECO:0000269|PubMed:7929106}.
SEQUENCE 1023 AA; 112617 MW; D66E8C4028F41BF1 CRC64;
MGYGAGRDKY EPAATSEHGG KKGKGKGKDR DMEELKKEVT MEDHKMTLEE LHRKYGTDLT
RGLTTARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SMLLWIGAIL CFLAYGIRKA
SDLEPDNDNL YLGVVLSAVV IITGCFSYYQ EAKSSRIMES FKNMVPQQAL VIRNGEKLSI
NAENVVQGDL VEVKGGDRIP ADLRIISAHG CKVDNSSLTG ESEPQTRSPD FTNENPLETR
NIAFFSTNCV EGTARGIVIN TGDRTVMGRI ATLASGLEGG QTPIAVEIGH FIHIITGVAV
FLGVSFFILS LILHYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGAS FDKSSPTWTA
LARIAGLCNR AVFPAGQENT PILKRDVVGD ASESALLKCI ELCCGSVKDM REKNQKVAEI
PFNSTNKYQL SVHKNANPSE SRYLLVMKGA PERILDRCSS ILLQGKEQPL DEELKDAFQN
AYLELGGLGE RVLGFCHLLL DDEQFPDGFS FDTEDVNFPT EGLCFVGLIS MIDPPRAAVP
DRVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVNQVNPRDA
KACVIHGTDL KDMNADQIDD ILRHHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN
DSPALKKADI GIAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL
TSNIPEITPF LIFIIADIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK
KDKLVNERLI SMAYGQIGMI QALGGFFAYF VILAENGFLP STLLGIRVAW EDRYVNDVED
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE
ETALAAFLSY CPGMDVALRM YPLKPTWWFC AFPYSLLIFI YDEVRKLILR RSPGGWVEKE
TYY


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