ID   AT1A1_CHICK             Reviewed;        1021 AA.
AC   P09572;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-1;
DE            Short=Na(+)/K(+) ATPase alpha-1 subunit;
DE            EC=7.2.2.13;
DE   AltName: Full=Sodium pump subunit alpha-1;
DE   Flags: Precursor;
GN   Name=ATP1A1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=2831227; DOI=10.1016/s0021-9258(18)68932-x;
RA   Takeyasu K., Tamkun M.M., Renaud K.J., Fambrough D.M.;
RT   "Ouabain-sensitive (Na+ + K+)-ATPase activity expressed in mouse L cells by
RT   transfection with DNA encoding the alpha-subunit of an avian sodium pump.";
RL   J. Biol. Chem. 263:4347-4354(1988).
CC   -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC       catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC       potassium ions across the plasma membrane. This action creates the
CC       electrochemical gradient of sodium and potassium ions, providing the
CC       energy for active transport of various nutrients.
CC       {ECO:0000250|UniProtKB:P05023}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
CC         Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         EC=7.2.2.13;
CC   -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC       catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC       additional regulatory subunit. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC       {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: Phosphorylation on Tyr-10 modulates pumping activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIC subfamily. {ECO:0000305}.
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DR   EMBL; J03230; AAA48607.1; -; mRNA.
DR   PIR; A28199; A28199.
DR   RefSeq; NP_990852.1; NM_205521.1.
DR   AlphaFoldDB; P09572; -.
DR   BMRB; P09572; -.
DR   SMR; P09572; -.
DR   BioGRID; 676774; 1.
DR   DIP; DIP-27N; -.
DR   IntAct; P09572; 1.
DR   STRING; 9031.ENSGALP00000056482; -.
DR   PaxDb; 9031-ENSGALP00000024150; -.
DR   GeneID; 396530; -.
DR   KEGG; gga:396530; -.
DR   CTD; 476; -.
DR   VEuPathDB; HostDB:geneid_396530; -.
DR   eggNOG; KOG0203; Eukaryota.
DR   InParanoid; P09572; -.
DR   PhylomeDB; P09572; -.
DR   PRO; PR:P09572; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:1990794; C:basolateral part of cell; IDA:AgBase.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IBA:GO_Central.
DR   GO; GO:0030007; P:intracellular potassium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006883; P:intracellular sodium ion homeostasis; IBA:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR   CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR005775; P-type_ATPase_IIC.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01106; ATPase-IIC_X-K; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43294:SF9; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA-1; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW   Potassium transport; Reference proteome; Sodium; Sodium transport;
KW   Sodium/potassium transport; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   PROPEP          1..5
FT                   /id="PRO_0000002493"
FT   CHAIN           6..1021
FT                   /note="Sodium/potassium-transporting ATPase subunit alpha-
FT                   1"
FT                   /id="PRO_0000002494"
FT   TOPO_DOM        6..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..129
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..286
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..318
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..770
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        771..790
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        791..800
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        801..821
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        822..841
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        842..864
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        865..916
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        917..936
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        937..949
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        950..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        969..983
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        984..1004
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1005..1021
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..82
FT                   /note="Phosphoinositide-3 kinase binding"
FT                   /evidence="ECO:0000250"
FT   REGION          214..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        374
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         485
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         715
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         719
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         16
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         941
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
SQ   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
//