AT1A3_RAT
ID AT1A3_RAT Reviewed; 1013 AA.
AC P06687; Q16732; Q9Z1G6;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-3;
DE Short=Na(+)/K(+) ATPase alpha-3 subunit;
DE EC=7.2.2.13;
DE AltName: Full=Na(+)/K(+) ATPase alpha(III) subunit;
DE AltName: Full=Sodium pump subunit alpha-3;
GN Name=Atp1a3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3028470; DOI=10.1021/bi00373a001;
RA Shull G.E., Greeb J., Lingrel J.B.;
RT "Molecular cloning of three distinct forms of the Na+,K+-ATPase alpha-
RT subunit from rat brain.";
RL Biochemistry 25:8125-8132(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2822682; DOI=10.1093/oxfordjournals.jbchem.a122039;
RA Hara Y., Urayama O., Kawakami K., Nojima H., Nagamune H., Kojima T.,
RA Ohta T., Nagano K., Nakao M.;
RT "Primary structures of two types of alpha-subunit of rat brain Na+,K+,-
RT ATPase deduced from cDNA sequences.";
RL J. Biochem. 102:43-58(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-930.
RC TISSUE=Brain, and Liver;
RX PubMed=2822726; DOI=10.1083/jcb.105.4.1855;
RA Herrera V.L.M., Emanuel J.R., Ruiz-Opazo N., Levenson R., Nadal-Ginard B.;
RT "Three differentially expressed Na,K-ATPase alpha subunit isoforms:
RT structural and functional implications.";
RL J. Cell Biol. 105:1855-1865(1987).
RN [4]
RP PROTEIN SEQUENCE OF 58-64; 147-152; 246-254; 260-271; 425-434; 436-448;
RP 517-525; 587-595; 620-648; 734-763 AND 878-883, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-218 AND SER-442, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP INTERACTION WITH FXYD1.
RX PubMed=23532852; DOI=10.1074/jbc.m113.460956;
RA Wypijewski K.J., Howie J., Reilly L., Tulloch L.B., Aughton K.L.,
RA McLatchie L.M., Shattock M.J., Calaghan S.C., Fuller W.;
RT "A separate pool of cardiac phospholemman that does not regulate or
RT associate with the sodium pump: multimers of phospholemman in ventricular
RT muscle.";
RL J. Biol. Chem. 288:13808-13820(2013).
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. Interacts with regulatory subunit FXYD1.
CC {ECO:0000269|PubMed:23532852}.
CC -!- SUBCELLULAR LOCATION: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M14513; AAA40777.1; -; mRNA.
DR EMBL; X05883; CAA29307.1; -; mRNA.
DR EMBL; M28648; AAA41672.1; -; mRNA.
DR PIR; C24639; C24639.
DR RefSeq; NP_036638.1; NM_012506.1.
DR AlphaFoldDB; P06687; -.
DR SMR; P06687; -.
DR BioGRID; 246401; 9.
DR IntAct; P06687; 4.
DR MINT; P06687; -.
DR STRING; 10116.ENSRNOP00000027497; -.
DR BindingDB; P06687; -.
DR ChEMBL; CHEMBL3885640; -.
DR ChEMBL; CHEMBL4106149; -.
DR CarbonylDB; P06687; -.
DR iPTMnet; P06687; -.
DR PhosphoSitePlus; P06687; -.
DR jPOST; P06687; -.
DR PaxDb; P06687; -.
DR PRIDE; P06687; -.
DR GeneID; 24213; -.
DR KEGG; rno:24213; -.
DR UCSC; RGD:2169; rat.
DR CTD; 478; -.
DR RGD; 2169; Atp1a3.
DR VEuPathDB; HostDB:ENSRNOG00000020263; -.
DR eggNOG; KOG0203; Eukaryota.
DR HOGENOM; CLU_002360_4_3_1; -.
DR InParanoid; P06687; -.
DR OMA; RRFLTYH; -.
DR OrthoDB; 388324at2759; -.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR SABIO-RK; P06687; -.
DR PRO; PR:P06687; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020263; Expressed in cerebellum and 18 other tissues.
DR Genevisible; P06687; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0044327; C:dendritic spine head; IDA:RGD.
DR GO; GO:0044326; C:dendritic spine neck; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR GO; GO:0098984; C:neuron to neuron synapse; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0031090; C:organelle membrane; ISO:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:ARUK-UCL.
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; ISO:RGD.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISO:RGD.
DR GO; GO:0099520; F:ion antiporter activity involved in regulation of presynaptic membrane potential; ISO:RGD.
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:0086037; F:P-type sodium:potassium-exchanging transporter activity involved in regulation of cardiac muscle cell membrane potential; ISO:RGD.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IDA:ARUK-UCL.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:RGD.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISO:RGD.
DR GO; GO:0007613; P:memory; ISO:RGD.
DR GO; GO:1990535; P:neuron projection maintenance; ISO:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:RGD.
DR GO; GO:0006813; P:potassium ion transport; IDA:RGD.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; ISO:RGD.
DR GO; GO:0006814; P:sodium ion transport; IDA:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
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 ATP-binding; Cell membrane; Direct protein sequencing; 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 CHAIN 1..1013
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 3"
FT /id="PRO_0000046300"
FT TOPO_DOM 1..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..762
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 763..782
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 783..792
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 793..813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 814..833
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 834..856
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 857..908
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 909..928
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 929..941
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 942..960
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 961..975
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 997..1013
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..74
FT /note="Interaction with phosphoinositide-3 kinase"
FT /evidence="ECO:0000250"
FT ACT_SITE 366
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 707
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 711
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIC6"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIC6"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 548
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIC6"
FT MOD_RES 933
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT CONFLICT 1..3
FT /note="MGD -> MNL (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="A -> R (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="D -> E (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="A -> G (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="E -> Q (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="K -> T (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="E -> D (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..194
FT /note="DLR -> ELG (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="G -> R (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="Missing (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="V -> K (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 807..809
FT /note="VPA -> DPT (in Ref. 3; AAA41672)"
FT /evidence="ECO:0000305"
FT CONFLICT 908
FT /note="C -> F (in Ref. 1; AAA40777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1013 AA; 111692 MW; 72F051406284EA8A CRC64;
MGDKKDDKSS PKKSKAKERR DLDDLKKEVA MTEHKMSVEE VCRKYNTDCV QGLTHSKAQE
ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SILLWIGAIL CFLAYGIQAG TEDDPSGDNL
YLGIVLAAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIREGEKMQV NAEEVVVGDL
VEIKGGDRVP ADLRIISAHG CKVDNSSLTG ESEPQTRSPD CTHDNPLETR NITFFSTNCV
EGTARGVVVA TGDRTVMGRI ATLASGLEVG KTPIAIEIEH FIQLITGVAV FLGVSFFILS
LILGYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN LEAVETLGST
STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTEDQSGTS FDKSSHTWVA LSHIAGLCNR
AVFKGGQDNI PVLKRDVAGD ASESALLKCI ELSSGSVKLM RERNKKVAEI PFNSTNKYQL
SIHETEDPND NRYLLVMKGA PERILDRCAT ILLQGKEQPL DEEMKEAFQN AYLELGGLGE
RVLGFCHYYL PEEQFPKGFA FDCDDVNFTT DNLCFVGLMS MIDPPRAAVP DAVGKCRSAG
IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA KACVIHGTDL
KDFTSEQIDE ILQNHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN DSPALKKADI
GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF
LLFIMANIPL PLGTITILCI DLGTDMVPAI SLAYEAAESD IMKRQPRNPR TDKLVNERLI
SMAYGQIGMI QALGGFFSYF VILAENGFLP GNLVGIRLNW DDRTVNDLED SYGQQWTYEQ
RKVVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE ETALAAFLSY
CPGMDVALRM YPLKPSWWFC AFPYSFLIFV YDEIRKLILR RNPGGWVEKE TYY
