ID   AT1A_TETCF              Reviewed;        1022 AA.
AC   P05025;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha;
DE            Short=Na(+)/K(+) ATPase alpha subunit;
DE            EC=7.2.2.13;
DE   AltName: Full=Sodium pump subunit alpha;
DE   Flags: Precursor;
OS   Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX   NCBI_TaxID=7787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2993905; DOI=10.1038/316733a0;
RA   Kawakami K., Noguchi S., Noda M., Takahashi H., Ohta T., Kawamura M.,
RA   Nojima H., Nagano K., Hirose T., Inayama S., Hayashida H., Miyata T.,
RA   Numa S.;
RT   "Primary structure of the alpha-subunit of Torpedo californica (Na+ +
RT   K+)ATPase deduced from cDNA sequence.";
RL   Nature 316:733-736(1985).
RN   [2]
RP   PROTEIN SEQUENCE OF 386-402; 502-512; 671-689 AND 887-906.
RX   PubMed=3008150; DOI=10.1073/pnas.83.7.2071;
RA   Ohta T., Nagano K., Yoshida M.;
RT   "The active site structure of Na+/K+-transporting ATPase: location of the
RT   5'-(p-fluorosulfonyl)benzoyladenosine binding site and soluble peptides
RT   released by trypsin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:2071-2075(1986).
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   -!- 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 {ECO:0000305}; Multi-pass membrane
CC       protein.
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; X02810; CAA26578.1; -; mRNA.
DR   PIR; S00503; S00503.
DR   AlphaFoldDB; P05025; -.
DR   SMR; P05025; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Direct protein sequencing; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Potassium; Potassium transport; Sodium; Sodium transport;
KW   Sodium/potassium transport; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   PROPEP          1..5
FT                   /id="PRO_0000002509"
FT   CHAIN           6..1022
FT                   /note="Sodium/potassium-transporting ATPase subunit alpha"
FT                   /id="PRO_0000002510"
FT   TOPO_DOM        6..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..131
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..288
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..320
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        339..771
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        772..791
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        792..801
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        802..822
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        823..842
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        843..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        866..917
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        918..937
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        938..950
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        951..969
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        970..984
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        985..1005
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1006..1022
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..84
FT                   /note="Interaction with phosphoinositide-3 kinase"
FT                   /evidence="ECO:0000250"
FT   REGION          215..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        376
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         716
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         720
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         16
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         942
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1022 AA;  112430 MW;  D92FE737847D73C2 CRC64;
     MGKGAASEKY QPAATSENAK NSKKSKSKTT DLDELKKEVS LDDHKLNLDE LHQKYGTDLT
     QGLTPARAKE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF SILLWTGAIL CFLAYGIQVA
     TVDNPANDNL YLGVVLSTVV IITGCFSYYQ EAKSSKIMDS FKNMVPQQAL VIRDGEKSSI
     NAEQVVVGDL VEVKGGDRIP ADLRIISACS CKVDNSSLTG ESEPQSRSPE YSSENPLETK
     NIAFFSTNCV EGTARGIVIN IGDHTVMGRI ATLASGLEVG QTPIAAEIEH FIHIITGVAV
     FLGVSFFILS LILGYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
     LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGIS FDKTSLSWNA
     LSRIAALCNR AVFQAGQDSV PILKRSVAGD ASESALLKCI ELCCGSVSQM RDRNPKIVEI
     PFNSTNKYQL SIHENDKADS RYLLVMKGAP ERILDRCSTI LLNGEDKPLN EEMKEAFQNA
     YLELGGLGER VLGFCHLKLS TSKFPEGYPF DVEEPNFPIT DLCFVGLMSM IDPPRAAVPD
     AVGKCRSAGI KVIMVTGDHP ITAKAIAKGV GIISEGNETV EDIAARLNIP VNQVNPRDAK
     ACVVHGTDLK DLSHENLDDI LHYHTEIVFA RTSPQQKLII VEGCQRQGAI VAVTGDGVND
     SPALKKADIG VAMGIAGSDV SKQAADMILL DDNFASIVTG VEEGRLIFDN LKKSIAYTLT
     SNIPEITPFL VFIIANVPLP LGTVTILCID LGTDMVPAIS LAYERAESDI MKRQPRNPKT
     DKLVNERLIS MAYGQIGMIQ ALGGFFSYFV ILAENGFLPI DLIGIREKWD ELWTQDLEDS
     YGQQWTYEQR KIVEYTCHTS FFVSIVIVQW ADLIICKTRR NSIFQQGMKN KILIFGLFEE
     TALAAFLSYT PGTDIALRMY PLKPSWWFCA FPYSLIIFLY DEARRFILRR NPGGWVEQET
     YY
//