ID   AT1B_ARTSF              Reviewed;        1004 AA.
AC   P28774;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-B;
DE            Short=Na(+)/K(+) ATPase alpha-B subunit;
DE            EC=7.2.2.13;
DE   AltName: Full=Sodium pump subunit alpha-B;
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=1657719; DOI=10.1016/0378-1119(91)90151-z;
RA   Macias M.T., Martinez J.L., Palmero I., Sastre L.;
RT   "Cloning of a cDNA encoding an Artemia franciscana Na/K ATPase alpha-
RT   subunit.";
RL   Gene 105:197-204(1991).
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; X56650; CAA39972.1; -; mRNA.
DR   PIR; JH0470; JH0470.
DR   AlphaFoldDB; P28774; -.
DR   SMR; P28774; -.
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   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..1004
FT                   /note="Sodium/potassium-transporting ATPase subunit alpha-
FT                   B"
FT                   /id="PRO_0000046307"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        110..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        272..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        301..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        768..791
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        828..855
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        897..918
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        934..959
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   REGION          197..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        357
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000305"
FT   BINDING         489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         698
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         702
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1004 AA;  110699 MW;  CE4E6BECE19A78C7 CRC64;
     MAKGKQKKGK DLNELKKELD IDFHKIPIEE CYQRLGSNPE TGLTNAQARS NIERDGPNCL
     TPPKTTPEWI KFCKNLFGGF ALLLWTGAIL CFLAYGIEAS SGNEDMLKDN LYLGIVLATV
     VIVTGIFSYY QENKSSRIMD SFKNLVPQYA LALREGQRVT LKAEELTMGD IVEVKFGDRV
     PADLRVLEAR SFKVDNSSLT GESEPQARSP EFTNDNPLET KNLAFFSTNA VEGTMRGIVI
     GIGDNTVMGR IAGLASGLDT GETPIAKEIA HFIHIITGVA VFLGVTFFII AFVLGYHWLD
     AVVFLIGIIV ANVPEGLLAT VTVCLTLTAK RMASKNCLVK NLEAVETLGS TSTICSDKTG
     TLTQNRMTVA HMWFDGTITE ADTTEDQSGA QFDKSSAGWK ALVKIAALCS RAEFKPNQST
     TPILKREVTG DASEAAILKC VELTTGETEA IRKRNKKICE IPFNSANKFQ VSIHENEDKS
     DGRYLLVMKG APERILERCS TIFMNGKEID MTEELKEAFN NAYMELGGLG ERVLGFCDYL
     LPLDKYPHGF AFNADDANFP LTGLRFAGLM SMIDPPRAAV PDAVAKCRSA GIKVIMVTGD
     HPITAKAIAK SVGIISEGNE TVEDIAARLN IPVSEVNPRD AKAAVVHGGE LRDITPDALD
     EILRHHPEIV FARTSPQQKL IIVEGCQRQG AIVAVTGDGV NDSPALKKAD IGVAMGIAGS
     DVSKQAADMI LLDDNFASIV TGVEEGRLIF DNLKKSIVYT LTSNIPEISP FLLFILFDIP
     LPLGTVTILC IDLGTDMVPA ISLAYEEAES DIMKRRPRNP VTDKLVNERL ISLAYGQIGM
     IQASAGFFVY FVIMAECGFL PWDLFGLRKH WDSRAVNDLT DSYGQEWTYD ARKQLESSCH
     TAYFVSIVIV QWADLIISKT RRNSVFQQGM RNNILNFALV FETCLAAFLS YTPGMDKGLR
     MYPLKINWWF PALPFSFLIF VYDEARKFIL RRNPGGWVEQ ETYY
//