AT1A1_HORSE
ID AT1A1_HORSE Reviewed; 1021 AA.
AC P18907;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-1;
DE Short=Sodium pump subunit alpha-1;
DE EC=7.2.2.13;
DE AltName: Full=Na(+)/K(+) ATPase alpha-1 subunit;
DE Flags: Precursor;
GN Name=ATP1A1;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2544461; DOI=10.1016/0014-5793(89)80691-x;
RA Kano I., Nagai F., Satoh K., Ushiyama K., Nakao T., Kano K.;
RT "Structure of the alpha 1 subunit of horse Na,K-ATPase gene.";
RL FEBS Lett. 250:91-98(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 {ECO:0000250|UniProtKB:P05023}.
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. Interacts with regulatory subunit FXYD1.
CC Interacts with regulatory subunit FXYD3. Interacts with SIK1. Interacts
CC with SLC35G1 and STIM1. Interacts with CLN3; this interaction regulates
CC the sodium/potassium-transporting ATPase complex localization at the
CC plasma membrane (By similarity). {ECO:0000250|UniProtKB:P05023,
CC ECO:0000250|UniProtKB:P06685}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P06685}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:P06685}.
CC Melanosome {ECO:0000250|UniProtKB:P05023}.
CC -!- PTM: Phosphorylation on Tyr-10 modulates pumping activity.
CC Phosphorylation of Ser-941 by PKA modulates the response of ATP1A1 to
CC PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following
CC increases in intracellular sodium, leading to increase catalytic
CC activity (By similarity). {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; X16773; CAA34716.1; -; Genomic_DNA.
DR EMBL; X16774; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16775; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16776; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16777; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16778; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16779; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16780; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16781; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16782; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16783; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16784; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16785; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16786; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16787; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16788; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16789; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16790; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16791; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16792; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16793; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16794; CAA34716.1; JOINED; Genomic_DNA.
DR EMBL; X16795; CAA34716.1; JOINED; Genomic_DNA.
DR PIR; S04630; S04630.
DR AlphaFoldDB; P18907; -.
DR SMR; P18907; -.
DR STRING; 9796.ENSECAP00000022397; -.
DR PaxDb; P18907; -.
DR PRIDE; P18907; -.
DR Ensembl; ENSECAT00000026804; ENSECAP00000022397; ENSECAG00000024623.
DR VGNC; VGNC:49506; ATP1A1.
DR GeneTree; ENSGT00940000154840; -.
DR InParanoid; P18907; -.
DR OrthoDB; 100699at2759; -.
DR Proteomes; UP000002281; Chromosome 5.
DR Bgee; ENSECAG00000024623; Expressed in adult mammalian kidney and 23 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031090; C:organelle membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IBA:GO_Central.
DR GO; GO:0036126; C:sperm flagellum; 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:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
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:0016791; F:phosphatase activity; IEA:Ensembl.
DR GO; GO:1990239; F:steroid hormone binding; IEA:Ensembl.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR GO; GO:0086009; P:membrane repolarization; IEA:Ensembl.
DR GO; GO:0031947; P:negative regulation of glucocorticoid biosynthetic process; IEA:Ensembl.
DR GO; GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl.
DR GO; GO:0045823; P:positive regulation of heart contraction; IEA:Ensembl.
DR GO; GO:0045989; P:positive regulation of striated muscle contraction; IEA:Ensembl.
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:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB.
DR GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
DR GO; GO:1903416; P:response to glycoside; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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; -; 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 3: Inferred from homology;
KW Acetylation; ATP-binding; Cell membrane; Cell projection; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Potassium; Potassium transport; Reference proteome; Sodium;
KW Sodium transport; Sodium/potassium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT PROPEP 1..5
FT /evidence="ECO:0000250"
FT /id="PRO_0000002481"
FT CHAIN 6..1021
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 1"
FT /id="PRO_0000002482"
FT TOPO_DOM 6..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..318
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..770
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..790
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 791..800
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 822..841
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 865..916
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 917..936
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 937..949
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 950..968
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 969..983
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 984..1004
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1005..1021
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..82
FT /note="Phosphoinositide-3 kinase binding"
FT /evidence="ECO:0000250"
FT REGION 214..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 374
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 715
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 10
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 16
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 258
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 540
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05023"
FT MOD_RES 659
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 941
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P06685"
SQ SEQUENCE 1021 AA; 112697 MW; 4FEB03FFB04E0216 CRC64;
MGKGGGRDKY EPAAISEHGN KKKAKKERDM DELKKEVSMD DHKLSLDELQ RKYGTDLSRG
LTTARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM LLWIGAILCF LAYGIQAATE
EEPQNDNLYL GVVLSAVVII TGCFSYYQEA KSSKIMESFK NMVPQQALVV RNGEKMSINA
EEVVVGDLVE VKGGDRIPAD LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI
AFFSTNCVEG TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL
GVTFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE
AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TENQSGVSFD KTSATWLSLS
RIAGLCNRAV FQANQENIPI LKRAVAGDAS ESALLKCIEL CCGSVKEMRD RYPKIVEIPF
NSTNKYQLSI HKNPNTSEPQ HLLVMKGAPE RILDRCSSIL LNGKEQPLDE ELKDAFQNAY
LELGGLGERV LGFCHLFLPD EQFPEGFQFD TDDVNFPLEN LCFVGLISMI DPPRAAVPDA
VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISEGNETVE DIAARLNIPV SQVNPRDAKA
CVVHGSDLKD MTPEQLDDIL RHHTEIVFAR TSPQQKLIIV EGCQRQGAIV AVTGDGVNDS
PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS
NIPEITPFLI FIIANIPLPL GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPQTD
KLVNERLISM AYGQIGMIQA LGGFFTYFVI LAENGFLPIH LLGLRVDWDD RWVNDVEDSY
GQQWTYEQRK IVEFTCHTAF FVSIVVVQWA DLVICKTRRN SVFQQGMKNK ILIFGLFEET
ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD EVRKLIIRRR PGGWVEKETY
Y
