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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_CHICK             Reviewed;        1021 AA.
P09572;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
28-FEB-2018, entry version 144.
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;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=2831227;
Takeyasu K., Tamkun M.M., Renaud K.J., Fambrough D.M.;
"Ouabain-sensitive (Na+ + K+)-ATPase activity expressed in mouse L
cells by transfection with DNA encoding the alpha-subunit of an avian
sodium pump.";
J. Biol. Chem. 263:4347-4354(1988).
-!- 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. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein
{ECO:0000255}.
-!- PTM: Phosphorylation on Tyr-10 modulates pumping activity.
{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; J03230; AAA48607.1; -; mRNA.
PIR; A28199; A28199.
RefSeq; NP_990852.1; NM_205521.1.
UniGene; Gga.2155; -.
ProteinModelPortal; P09572; -.
SMR; P09572; -.
BioGrid; 676774; 1.
DIP; DIP-27N; -.
IntAct; P09572; 1.
STRING; 9031.ENSGALP00000036172; -.
PaxDb; P09572; -.
PRIDE; P09572; -.
GeneID; 396530; -.
KEGG; gga:396530; -.
CTD; 476; -.
eggNOG; KOG0203; Eukaryota.
eggNOG; COG0474; LUCA.
HOGENOM; HOG000265622; -.
HOVERGEN; HBG004298; -.
InParanoid; P09572; -.
KO; K01539; -.
PhylomeDB; P09572; -.
PRO; PR:P09572; -.
Proteomes; UP000000539; Unplaced.
GO; GO:1990794; C:basolateral part of cell; IDA:AgBase.
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; 2.
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.
2: Evidence at transcript level;
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
/FTId=PRO_0000002493.
CHAIN 6 1021 Sodium/potassium-transporting ATPase
subunit alpha-1.
/FTId=PRO_0000002494.
TOPO_DOM 6 85 Cytoplasmic. {ECO:0000255}.
TRANSMEM 86 106 Helical. {ECO:0000255}.
TOPO_DOM 107 129 Extracellular. {ECO:0000255}.
TRANSMEM 130 150 Helical. {ECO:0000255}.
TOPO_DOM 151 286 Cytoplasmic. {ECO:0000255}.
TRANSMEM 287 306 Helical. {ECO:0000255}.
TOPO_DOM 307 318 Extracellular. {ECO:0000255}.
TRANSMEM 319 336 Helical. {ECO:0000255}.
TOPO_DOM 337 770 Cytoplasmic. {ECO:0000255}.
TRANSMEM 771 790 Helical. {ECO:0000255}.
TOPO_DOM 791 800 Extracellular. {ECO:0000255}.
TRANSMEM 801 821 Helical. {ECO:0000255}.
TOPO_DOM 822 841 Cytoplasmic. {ECO:0000255}.
TRANSMEM 842 864 Helical. {ECO:0000255}.
TOPO_DOM 865 916 Extracellular. {ECO:0000255}.
TRANSMEM 917 936 Helical. {ECO:0000255}.
TOPO_DOM 937 949 Cytoplasmic. {ECO:0000255}.
TRANSMEM 950 968 Helical. {ECO:0000255}.
TOPO_DOM 969 983 Extracellular. {ECO:0000255}.
TRANSMEM 984 1004 Helical. {ECO:0000255}.
TOPO_DOM 1005 1021 Cytoplasmic. {ECO:0000255}.
REGION 80 82 Phosphoinositide-3 kinase binding.
{ECO:0000250}.
ACT_SITE 374 374 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 715 715 Magnesium. {ECO:0000250}.
METAL 719 719 Magnesium. {ECO:0000250}.
BINDING 485 485 ATP. {ECO:0000250}.
MOD_RES 10 10 Phosphotyrosine. {ECO:0000250}.
MOD_RES 16 16 Phosphoserine; by PKC. {ECO:0000250}.
MOD_RES 941 941 Phosphoserine; by PKA. {ECO:0000250}.
SEQUENCE 1021 AA; 112231 MW; 921E86B6FD843EEB CRC64;
MGKGAGRDKY EPTATSEHGT KKKKAKERDM DELKKEISMD DHKLSLDELH RKYGTDLSRG
LTTARAAEIL ARDGPNTLTP PPTTPEWVKF CRQLFGGFSL LLWIGSLLCF LAYGITSVME
GEPNSDNLYL GVVLAAVVII TGCFSYYQEA KSSKIMESFK NMVPQQALVV RNGEKMSINA
EGVVVGDLVE VKGGDRIPAD LRIISAHGCK VDNSSLTGES EPQTRSPDFS NENPLETRNI
AFFSTNCVEG TAVGIVISTG DRTVMGRIAS LASGLEGGKT PIAMEIEHFI HLITGVAVFL
GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE
AVGTLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TENQSGASFD KSSATWLALS
RIAGLCNRAV FQANQENVPI LKRAVAGDAS ESALLKCIEL CCGSVKEMRE RYPKVVEIPF
NSTNKYQLSI HKNANAGESR HLLVMKGAPE RILDRCDSIL IHGKVQPLDE EIKDAFQNAY
LELGGLGERV LGFCHLALPD DQFPEGFQFD TDEVNFPVEK LCFVGLMSMI DPPRAAVPDA
VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISDGNETVE DIAARLNIPV SQVNPRDAKA
CVVHGSDLKD MTSEQLDDIL LHHTEIVFAR TSPQQKLIIV EGCQRQGAIV AVTGDGVNDS
PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS
NIPEITPFLI FIIANIPLPL GTCTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD
KLVNERLISM AYGQIGMIQA LGGFFTYFVI MAENGFLPSG LVGIRLQWDD RWINDVEDSY
GQQWTFEQRK IVEFTCHTAF FVSIVVVQWA DLIICKTRRN SVFQQGMKNK ILIFGLFEET
ALAAFLSYCP GMDVALRMYP LKPTWWFCAF PYSLLIFLYD EIRKLIIRRN PGGWVERETY
Y


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