ID   AT1A2_CHICK             Reviewed;        1017 AA.
AC   P24797;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-2;
DE            Short=Na(+)/K(+) ATPase alpha-2 subunit;
DE            EC=7.2.2.13;
DE   AltName: Full=Sodium pump subunit alpha-2;
GN   Name=ATP1A2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2171348; DOI=10.1152/ajpcell.1990.259.4.c619;
RA   Takeyasu K., Lemas V., Fambrough D.M.;
RT   "Stability of Na(+)-K(+)-ATPase alpha-subunit isoforms in evolution.";
RL   Am. J. Physiol. 259:C619-C630(1990).
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: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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; M59959; AAA48981.1; -; mRNA.
DR   PIR; I50394; A37227.
DR   RefSeq; NP_990807.1; NM_205476.1.
DR   AlphaFoldDB; P24797; -.
DR   SMR; P24797; -.
DR   GeneID; 396468; -.
DR   CTD; 477; -.
DR   VEuPathDB; HostDB:geneid_396530; -.
DR   InParanoid; P24797; -.
DR   PhylomeDB; P24797; -.
DR   PRO; PR:P24797; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IBA:GO_Central.
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; ISS:UniProtKB.
DR   GO; GO:0030007; P:intracellular potassium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006883; P:intracellular sodium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0001504; P:neurotransmitter uptake; ISS:AgBase.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006942; P:regulation of striated muscle contraction; ISS:AgBase.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
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:SF6; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA-2; 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; Reference proteome; Sodium; Sodium transport;
KW   Sodium/potassium transport; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1017
FT                   /note="Sodium/potassium-transporting ATPase subunit alpha-
FT                   2"
FT                   /id="PRO_0000046297"
FT   TOPO_DOM        1..82
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..126
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        148..283
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..315
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..766
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        767..786
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        787..796
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        797..817
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        818..837
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        838..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        861..912
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        913..932
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        933..945
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        946..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        965..979
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        980..1000
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1001..1017
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..79
FT                   /note="Interaction with phosphoinositide-3 kinase"
FT                   /evidence="ECO:0000250"
FT   REGION          207..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        371
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         502
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         711
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         715
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         937
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1017 AA;  112051 MW;  38E87C1BDE93B8C5 CRC64;
     MDGREYSPAA TTSENGGGRR KQKEKELDEL KKEVNLDDHK LSLDELGRKY QVDLSRGLSN
     ARAAEVLAQD GPNALTPPPT TPEWVKFCRQ LFGGFSILLW IGAILCFLAY GIQAAMEDEP
     SNDNLYLGVV LAAVVIVTGC FSYYQEAKSS KIMDSFKNMV PQQALVIREG EKIQINAENV
     VVGDLVEVKG GDRVPADMRI ISSHGCKVDN SSLTGESEPQ TRSPEFTHEN PLETRNICFF
     STNCVEGTAR GIVISTGDRT VMGRIASLAS GLEVGRTPIA MEIEHFIRLI TGVAVFLGLS
     FFILSLILGY TWLEAVIFLI GIIVANVPEG LLATVTVCLT LTAKRMARKN CLVKNLEAVE
     TLGSTSTICS DKTGTLTQNR MTVAHMWFDN QIHEADTTED QSGATFDKRS PTWAALSRIA
     GLCNRAVFKP GQENISISKR DTAGDASESA LLKCIQLSCG SVKKMRDKNP KVTEIPFNST
     NKYQLSIHER EEDPQGHILV MKGAPERILE RCSRILLQGQ EVPLDEEMKE AFQNAYLELG
     GLGERVLGFC HLYLPPDKFP RGFRFDADEV NFPTSDLCFV GLMSMIDPPR AAVPDAVGKC
     RSAGIKVIMV TGDHPITAKA IAKGVGIISE GNETVEDIAA RLNIPVSQVN PREAKACVVH
     GSDLKDMTAE QLDEILRNHT EIVFARTSPQ QKLIIVEGCQ RQGAIVAVTG DGVNDSPALK
     KADIGIAMGI AGSDVSKQAA DMILLDDNFA SIVTGVEEGR LIFDNLKKSI AYTLTSNIPE
     ITPFLLFIIA NIPLPLGTVT ILCIDLGTDM VPAISLAYEA AESDIMKRQP RNPRTDKLVN
     ERLISMAYGQ IGMIQALGGF FTYFVILAEN GFLPARLLGV RLAWDDRSTN DLEDSYGQEW
     TYEQRKVVEF TCHTAFFASI VVVQWADLII CKTRRNSVFQ QGMKNKILIF GLLEETALAA
     FLSYCPGMGV ALRMYPLKVT WWFCAFPYSL LIFAYDEVRK LILRRYPGGW VEKETYY
//