ID   AT1A_ARTSF              Reviewed;         996 AA.
AC   P17326;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-A;
DE            Short=Na(+)/K(+) ATPase alpha-A subunit;
DE            EC=7.2.2.13;
DE   AltName: Full=Sodium pump subunit alpha-A;
OS   Artemia franciscana (Brine shrimp) (Artemia sanfranciscana).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Anostraca; Artemiidae; Artemia.
OX   NCBI_TaxID=6661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2553490; DOI=10.1016/0014-5793(89)81816-2;
RA   Baxter-Lowe L.A., Guo J.Z., Bergstroem E.E., Hokin L.E.;
RT   "Molecular cloning of the Na,K-ATPase alpha-subunit in developing brine
RT   shrimp and sequence comparison with higher organisms.";
RL   FEBS Lett. 257:181-187(1989).
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; Y07513; CAA68811.1; -; mRNA.
DR   PIR; S06635; S06635.
DR   AlphaFoldDB; P17326; -.
DR   SMR; P17326; -.
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:SF13; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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; 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; Sodium; Sodium transport; Sodium/potassium transport;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..996
FT                   /note="Sodium/potassium-transporting ATPase subunit alpha-
FT                   A"
FT                   /id="PRO_0000046306"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        107..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        268..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        297..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        762..785
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        820..847
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        889..909
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        926..951
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   REGION          191..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        353
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000305"
FT   BINDING         483
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         692
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         696
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   996 AA;  111022 MW;  92A4D129F327A42C CRC64;
     MGKKQGKQLS DLKKELELDQ HKIPLEELCR RLGTNTETGL TSSQAKSHLE KYGPNALTPP
     RTTPEWIKFC KQLFGGFQML LWIGSILCFI AYTMEKYKNP DVLGDNLYLG LALLFVVIMT
     GCFAYYQDHN ASKIMDSFKN LMPQFAFVIR DGKKIQLKAE EVTVGDLVEV KFGDRIPADI
     RITSCQSMKV DNSSLTGESE PQSRSTECTN DNPLETKNLA FFFTNTLEGT GRGIVINVGD
     DSVMGRIACL ASSLDSGKTP IAREIEHFIH IITAMAVSLA AVFAVISFLY GYTWLEAAIF
     MIGIIVAKVP EGLLATVTVC LTLTAKRMAK KNCLVRNLEA VETLGSTSTI CSDKTGTLTQ
     NRMTVAHMWF DQKIVTADTT ENQSGNQLYR GSKGFPELIR VASLCSRAEF KTEHAHLPVL
     KRDVNGDASE AAILKFAEMS TGSVMNIRSK QKKVSEIPFN SANKYQVSVH EREDKSGYFL
     VMKGAPERIL ERCSTILIDG TEIPLDNHMK ECFNNAYMEL GGMGERVLGF CDFELPSDQY
     PRGYVFDADE PNFPISGLRF VGLMSMIDPP RAAVPDAVSK CRSAGIKVIM VTGDHPITAK
     AIARQVGIIS EGHETVDDIA ARLNIPVSEV NPRSAQAAVI HGNDLKDMNS DQLDDILRHY
     REIVFARTSP QQKLIIVEGV QRQGEFVAVT GDGVNDSPAL KKADIGVAMG IAGSDVSKQA
     ADMILLDDNF ASIVTGVEEG RLIFDNIKKS IAYTLTSKIP ELSPFLMYIL FDLPLAIGTV
     TILCIDLGTD VVPAISMAYE GPEADPRKPR DPVKEKLVNE RLISMAYGQI GVMQAFGGFF
     TYFVIMGECG FLPNRLFGLR KWWESKAYND LTDSYGQEWT WDARKQLEYT CHTAFFISIV
     IVQWTDLIIC KTRRLSLFQQ GMKNGTLNFA LVFETCVAAF LSYTPGMDKG LRMYPLKIWW
     WFPPMPFSLL ILVYDECRKF LMRRNPGGFL ERETYY
//