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 02-SEP-2026, entry version 138. 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; Altocrustacea; Allotriocarida; OC Branchiopoda; 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=2 K(+)(out) + 3 Na(+)(in) + ATP + H2O = 2 K(+)(in) + 3 CC Na(+)(out) + ADP + phosphate + H(+); Xref=Rhea:RHEA:18353, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:456216; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y07513; CAA68811.1; -; mRNA. DR PIR; S06635; S06635. DR PDB; 8K1L; EM; 3.44 A; A=1-996. DR AlphaFoldDB; P17326; -. DR SMR; P17326; -. DR GO; GO:0090533; C:cation-transporting ATPase complex; IEA:UniProtKB-ARBA. DR GO; GO:0098797; C:plasma membrane protein complex; IEA:UniProtKB-ARBA. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IEA:UniProtKB-EC. DR GO; GO:0030007; P:intracellular potassium ion homeostasis; IEA:TreeGrafter. DR GO; GO:0006883; P:intracellular sodium ion homeostasis; IEA:TreeGrafter. DR GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:TreeGrafter. DR GO; GO:1902600; P:proton transmembrane transport; IEA:TreeGrafter. DR GO; GO:0036376; P:sodium ion export across plasma membrane; IEA:TreeGrafter. DR CDD; cd02608; P-type_ATPase_Na-K_like; 1. DR FunFam; 1.20.1110.10:FF:000038; Sodium/potassium-transporting ATPase subunit alpha; 1. DR FunFam; 2.70.150.10:FF:000003; Sodium/potassium-transporting ATPase subunit alpha; 1. DR FunFam; 3.40.1110.10:FF:000001; Sodium/potassium-transporting ATPase subunit alpha; 1. DR FunFam; 3.40.50.1000:FF:000004; Sodium/potassium-transporting ATPase subunit alpha; 1. DR FunFam; 1.20.1110.10:FF:000095; Sodium/potassium-transporting ATPase subunit alpha-1; 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; IPR059000; ATPase_P-type_domA. DR InterPro; IPR050510; Cation_transp_ATPase_P-type. 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 PRINTS; PR00119; CATATPASE. DR PRINTS; PR00121; NAKATPASE. DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1. 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. DR PDBsum; 8K1L; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell membrane; Ion transport; Magnesium; KW Membrane; 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" FT TURN 20..22 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 25..32 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 36..38 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 42..51 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 57..61 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 65..72 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 79..98 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 106..127 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 134..137 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 178..184 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 193..195 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 232..237 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 239..242 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 243..252 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 260..283 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 285..288 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 289..291 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 294..304 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 311..313 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 314..329 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 330..332 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 333..337 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 349..352 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 356..358 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 367..370 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 373..376 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 394..404 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 413..416 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 419..421 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 424..426 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 428..441 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 445..450 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 453..456 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 466..471 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 475..484 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 486..490 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 493..498 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 501..504 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 507..522 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 526..535 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 537..539 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 548..550 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 556..567 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 574..583 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 587..591 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 596..606 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 616..623 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 627..629 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 632..634 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 642..646 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 650..659 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 661..667 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 670..681 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 682..684 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 687..690 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 697..702 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 703..713 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 715..719 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 722..725 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 732..754 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 758..769 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 773..775 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 779..786 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 789..791 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 792..796 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 797..799 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 800..802 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 806..808 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 809..812 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 820..823 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 824..829 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 830..849 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 853..856 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 860..864 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 881..911 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 913..915 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 917..920 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 925..941 FT /evidence="ECO:0007829|PDB:8K1L" FT TURN 945..948 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 949..951 FT /evidence="ECO:0007829|PDB:8K1L" FT STRAND 960..962 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 965..983 FT /evidence="ECO:0007829|PDB:8K1L" FT HELIX 989..992 FT /evidence="ECO:0007829|PDB:8K1L" 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 //