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Database: UniProt
Entry: A0A452RC36_URSAM
LinkDB: A0A452RC36_URSAM
Original site: A0A452RC36_URSAM 
ID   A0A452RC36_URSAM        Unreviewed;      1127 AA.
AC   A0A452RC36;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-2 {ECO:0000256|ARBA:ARBA00039738};
DE            EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
DE   AltName: Full=Sodium pump subunit alpha-2 {ECO:0000256|ARBA:ARBA00041492};
GN   Name=ATP1A2 {ECO:0000313|Ensembl:ENSUAMP00000016257.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000016257.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000016257.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00035887};
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. Interacts with regulatory subunit FXYD1.
CC       {ECO:0000256|ARBA:ARBA00038783}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIC subfamily. {ECO:0000256|ARBA:ARBA00006934}.
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DR   AlphaFoldDB; A0A452RC36; -.
DR   STRING; 9643.ENSUAMP00000016257; -.
DR   Ensembl; ENSUAMT00000018211.1; ENSUAMP00000016257.1; ENSUAMG00000012224.1.
DR   GeneTree; ENSGT00940000159936; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0031090; C:organelle membrane; IEA:Ensembl.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:Ensembl.
DR   GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IEA:Ensembl.
DR   GO; GO:0030955; F:potassium ion binding; IEA:Ensembl.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR   GO; GO:0031402; F:sodium ion binding; IEA:Ensembl.
DR   GO; GO:1990239; F:steroid hormone binding; IEA:Ensembl.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
DR   GO; GO:0071383; P:cellular response to steroid hormone stimulus; IEA:Ensembl.
DR   GO; GO:0030007; P:intracellular potassium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0006883; P:intracellular sodium ion homeostasis; IEA:Ensembl.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; IEA:Ensembl.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023201}.
FT   TRANSMEM        76..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        301..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        832..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        932..949
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        964..980
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..96
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1029..1049
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1127 AA;  122992 MW;  A81348A5E094BD7B CRC64;
     SPAATTAENG GGKKKQKEKE LDELKKEVAM TRSHSSPRLS QGLTNQRAQD ILARDGPNAL
     TPPPTTPEWV KFCRQLFGGF SILLWIGAIL CFLAYGIQAA MEDEPSNDNL YLGVVLAAVV
     IVTGCFSYYQ EAKSSKIMDS FKNMVPQQAL VVREGEKMQI NAEEVVVGDL VEVKGGDRVP
     ADLRIISSHG CKVDNSSLTG ESEPQTRSPE FTHENPLETR NICFFSTNCV EGTARGIVIA
     TGDRTVMGRI ATLASGLEVG RTPIAMEIEH FIQLITGVAV FLGVSFFVLS LILGYSWLEA
     VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN LEAVETLGST STICSDKTGT
     LTQNRMTVAH MWFDNQIHEA DTTEDQSGAT FDKRSPTWTA LSRIAGLCNR AVFKAGQENI
     SVSKRDTAGD ASESALLKCI ELSCGSVRKM RDRNPKVAEI PFNSTNKYQL SIHEREDSPQ
     SHVLVMKGAP ERILDRCSTI LVQGKEIPLD KEMQDAFQNA YMELGGLGER VLGFCQLNLP
     SGKFPRGFRF DTDELNFPTE KLCFVGLMSM IDPPRAAVPD AVGKCRSAGI KVIMVTGDHP
     ITAKAIAKGV GIISEGNETV EDIAARLNIP VSQVNPREAK ACVVHGSDLK DMTSEQLDEI
     LKNHTEIVFA RTSPQQKLII VEGCQRQGAI VAVTGDGVND SPALKKADIG IAMGISGSDV
     SKQAADMILL DDNFASIVTG VEEGRLIFDN LKKSIAYTLT SNIPEITPFL LFIIANIPLP
     LGTVTILCID LGTDMVPAIS LAYEAAESDI MKRQPRNPQT DKLVNERLIS MAYGQIGMIQ
     ALGGFFTYFV ILAENGFLPS RLLGIRLDWD DRSMNDLEDS YGQEWTYEQR KVVEFTCHTA
     FFASIVVVQW ADLIICKTRR NSVFQQGMKN KILIFGLLEE TALAAFLSYC PGMGVALRMY
     PLKVTWWFCA FPYSLLIFIY DEVRKLILRR YPGGEHPAPP TPRQCAPLLA APRGSTPKPF
     LLRLLTLSPR APRSGAPGPR TTAGDPLSPV LVPLTRGPSS LTASPPSHPD FALLGTSLGP
     HTGPVLLTWP QAPSLRGRIS VPPPRPVSSQ LCPPISPTGW VEKETYY
//
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