AT1A_ARTSF
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 03-AUG-2022, entry version 125.
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 PRIDE; P17326; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
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
