AT1A1_XENLA
ID AT1A1_XENLA Reviewed; 1025 AA.
AC Q92123; Q91683; Q92127;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
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;
GN Name=atp1a1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney epithelium;
RX PubMed=2544104; DOI=10.1152/ajprenal.1989.256.6.f1034;
RA Verrey F., Kairouz P., Schaerer E., Fuentes P., Geering K., Rossier B.C.,
RA Kraehenbuhl J.-P.;
RT "Primary sequence of Xenopus laevis Na+-K+-ATPase and its localization in
RT A6 kidney cells.";
RL Am. J. Physiol. 256:F1034-F1043(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Neural plate;
RX PubMed=8631513; DOI=10.1006/dbio.1996.0086;
RA Davies C.S., Messenger N.J., Craig R., Warner A.E.;
RT "Primary sequence and developmental expression pattern of mRNAs and protein
RT for an alpha1 subunit of the sodium pump cloned from the neural plate of
RT Xenopus laevis.";
RL Dev. Biol. 174:431-447(1996).
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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein
CC {ECO:0000255}.
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; U10108; AAA19022.1; -; mRNA.
DR EMBL; U49238; AAC59759.1; -; mRNA.
DR EMBL; U49239; AAC59760.1; -; mRNA.
DR PIR; A60444; A60444.
DR RefSeq; NP_001084064.1; NM_001090595.1.
DR AlphaFoldDB; Q92123; -.
DR SMR; Q92123; -.
DR PRIDE; Q92123; -.
DR DNASU; 399285; -.
DR GeneID; 399285; -.
DR KEGG; xla:399285; -.
DR CTD; 399285; -.
DR Xenbase; XB-GENE-6254180; atp1a1.L.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 399285; Expressed in kidney and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
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; IDA:BHF-UCL.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:BHF-UCL.
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 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..1025
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 1"
FT /id="PRO_0000046296"
FT TOPO_DOM 1..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..133
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..774
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 775..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..804
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 805..825
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 826..845
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 846..868
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 869..920
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..940
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..953
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 954..972
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 973..987
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 988..1008
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1009..1025
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..86
FT /note="Interaction with phosphoinositide-3 kinase"
FT /evidence="ECO:0000250"
FT REGION 216..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 378
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 723
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 16
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 945
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT CONFLICT 9
FT /note="K -> Q (in Ref. 2; AAC59760)"
FT /evidence="ECO:0000305"
FT CONFLICT 29..30
FT /note="Missing (in Ref. 2; AAC59759/AAC59760)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="E -> D (in Ref. 2; AAC59760)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..63
FT /note="MQR -> LQK (in Ref. 2; AAC59760)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="T -> S (in Ref. 2; AAC59760)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="A -> S (in Ref. 2; AAC59760)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="V -> G (in Ref. 2; AAC59760)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="F -> L (in Ref. 2; AAC59760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1025 AA; 113084 MW; B5F9B4EB6D86EEA0 CRC64;
MGYGAGRDKY EPAATSEQGG KKKKGKGKGK EKDMDELKKE VTMEDHKLSL DELHRKFGTD
MQRGLTTARA AEILARDGPN ALTPPPTTPE WVKFCRQLFG GFSMLLWIGA ILCFLAYGIQ
AAMEEEPQND NLYLGVVLSA VVIITGCFSY YQEAKSSKIM ESFKNMVPQQ ALVIRSGEKL
SINAEEVVLG DLVEVKGGDR IPADLRVISS HGCKVDNSSL TGESEPQTRS PDFTNENPLE
TRNIAFFSTN CVEGTARGIV VNTGDRTVMG RIATLASGLD GGRTPIAIEI EHFIHIITGV
AVFLGVSFFI LSLILQYTWL EAVIFLIGII VANVPEGLLA TVTVCLTLTA KRMARKNCLV
KNLEAVETLG STSTICSDKT GTLTQNRMTV AHMWFDNQIH EADTTENQSG ASFDKSSPTW
TALSRVAGLC NRAVFQAGQE NTPILKRDVA GDASESALLK CIELCCGSVR DMREKNHKVA
EIPFNSTNKY QLSVHKNANP SESRYILVMK GAPERILDRC TSIILQGKEQ PLDEELKDAF
QNAYLELGGL GERVLGFCHL ALPDDQFPDG FQFDTEEVNF PTENLCFVGL ISMIDPPRAA
VPDAVGKCRS AGIKVIMVTG DHPITAKAIA KGVGIISEGN ETVEDIAARL NIPVNQVNPR
DAKACVIHGT DLKDMTEEQI DDILRHHTEI VFARTSPQQK LIIVEGCQRQ GAIVAVTGDG
VNDSPALKKA DIGIAMGIAG SDVSKQAADM ILLDDNFASI VTGVEEGRLI FDNLKKSIAY
TLTSNIPEIT PFLIFIIANI PLPLGTVTIL CIDLGTDMVP AISLAYEQAE SDIMKRQPRN
PKTDKLVNER LISMAYGQIG MIQALGGFFT YFVILAENGF LPWTLLGIRV NWDDRWTNDV
EDSYGQQWTY EQRKIVEFTC HTSFFISIVV VQWADLIICK TRRNSVFQQG MKNKILIFGL
FEETALAAFL SYCPGMDVAL RMYPLKPTWW FCAFPYSLII FIYDEVRKLI IRRSPGGWVE
KESYY
