AT1A1_CANLF
ID AT1A1_CANLF Reviewed; 1021 AA.
AC P50997;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-1;
DE Short=Na(+)/K(+) ATPase alpha-1 subunit;
DE EC=7.2.2.13;
DE AltName: Full=Sodium pump subunit alpha-1;
DE Flags: Precursor;
GN Name=ATP1A1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xie Z., Li H., Liu G., Wang Y., Askari A., Mercer R.W.;
RT "Cloning of the dog Na/K-ATPase alpha 1 subunit.";
RL (In) Bamberg E., Schoner W. (eds.);
RL The sodium pump, pp.49-52, Springer-Verlag, New York (1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 92-311.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=1316269; DOI=10.1002/j.1460-2075.1992.tb05218.x;
RA Canessa C.M., Horisberger J.-D., Louvard D., Rossier B.C.;
RT "Mutation of a cysteine in the first transmembrane segment of Na,K-ATPase
RT alpha subunit confers ouabain resistance.";
RL EMBO J. 11:1681-1687(1992).
RN [3]
RP INTERACTION WITH FXYD1.
RX PubMed=16943195; DOI=10.1074/jbc.m606254200;
RA Bossuyt J., Despa S., Martin J.L., Bers D.M.;
RT "Phospholemman phosphorylation alters its fluorescence resonance energy
RT transfer with the Na/K-ATPase pump.";
RL J. Biol. Chem. 281:32765-32773(2006).
RN [4]
RP INTERACTION WITH FXYD1.
RX PubMed=21454534; DOI=10.1074/jbc.m110.184101;
RA Bibert S., Liu C.C., Figtree G.A., Garcia A., Hamilton E.J., Marassi F.M.,
RA Sweadner K.J., Cornelius F., Geering K., Rasmussen H.H.;
RT "FXYD proteins reverse inhibition of the Na+-K+ pump mediated by
RT glutathionylation of its beta1 subunit.";
RL J. Biol. Chem. 286:18562-18572(2011).
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 (PubMed:16943195, PubMed:21454534). Interacts with regulatory subunit
CC FXYD3 (By similarity). Interacts with SIK1 (By similarity). Interacts
CC with SLC35G1 and STIM1 (By similarity). Interacts with CLN3; this
CC interaction regulates the sodium/potassium-transporting ATPase complex
CC localization at the plasma membrane (By similarity).
CC {ECO:0000250|UniProtKB:P05023, ECO:0000250|UniProtKB:P06685,
CC ECO:0000269|PubMed:16943195, ECO:0000269|PubMed:21454534}.
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; L42173; AAA67372.1; -; mRNA.
DR EMBL; X66174; CAA46950.1; -; mRNA.
DR RefSeq; NP_001003306.1; NM_001003306.2.
DR AlphaFoldDB; P50997; -.
DR SMR; P50997; -.
DR STRING; 9612.ENSCAFP00000038629; -.
DR BindingDB; P50997; -.
DR ChEMBL; CHEMBL4838; -.
DR DrugCentral; P50997; -.
DR PaxDb; P50997; -.
DR PRIDE; P50997; -.
DR GeneID; 403992; -.
DR CTD; 476; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; P50997; -.
DR OrthoDB; 100699at2759; -.
DR PRO; PR:P50997; -.
DR Proteomes; UP000002254; Unplaced.
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:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; 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; ISS:UniProtKB.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB.
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 1: Evidence at protein level;
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_0000002479"
FT CHAIN 6..1021
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 1"
FT /id="PRO_0000002480"
FT TOPO_DOM 4..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..36
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 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 941
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT CONFLICT 109
FT /note="C -> Y (in Ref. 2; CAA46950)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="I -> V (in Ref. 2; CAA46950)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="K -> E (in Ref. 2; CAA46950)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="L -> F (in Ref. 2; CAA46950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1021 AA; 112667 MW; 938A19AA487CBEAA CRC64;
MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH RKYGTDLSRG
LTTARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM LLWIGAILCF LAYGIQAATE
EEPQNDNLYL GVVLSAVVII TGCFSYYQEA KSSKIMESFK NMVPQQALVI RNGEKMSINA
EEVVIGDLVE VKGGDRIPAD LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI
AFFSTNCVKG TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL
GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE
AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TENQSGVSFD KSSATWLALS
RIAGLCNRAV FQANQENLPI LKRAVAGDAS ESALLKCIEL CCGSVKEMRD RYAKIVEIPF
NSTNKYQLSI HKNPNTSEPR HLLVMKGAPE RILDRCSSIL LHGKEQPLDE ELKDALQNAY
LELGGLGERV LGFRHLFLPD EQFPEGFQFD TDDVNFPVEN LCFVGFISMI GPPRAAVPDA
VGKCRGAGIK VIMVTGDHPI TAKAIAKGAG IISEGNETVE DIAARLNIPV RQVNPRDAKA
CVVHGSDLKD MTSEQLDGIL KYHTEIVFAR TSPQQKLIIV EGCQRQGAIV AVTGDGVNDS
PALKKADIGV AMGIVGSDAS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS
NIPEITPFLI FIIANIPLPL GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD
KLVNERLISM AYGQIGMIQA LGGFFTYFVI LAENGFLPTH LLGLRVDWDD RWINDVEDSY
GQQWTYEQRK IVEFTCHTAF FVSIVVVQWA DLVICKTRRN SVFQQGMKNK ILIFGLFEET
ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD EVRKLIIRRR PGGWVEKETY
Y
