AT1A3_MOUSE
ID AT1A3_MOUSE Reviewed; 1013 AA.
AC Q6PIC6;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 157.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 21-27; 36-81; 153-163; 168-184; 203-254; 260-271;
RP 350-367; 404-420; 425-434; 436-458; 466-492; 517-557; 587-595; 603-615;
RP 620-648; 652-682; 689-764; 878-901; 931-940; 943-969 AND 1001-1009.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15648052; DOI=10.1002/pmic.200401066;
RA Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA Hart G.W., Burlingame A.L.;
RT "Quantitative analysis of both protein expression and serine / threonine
RT post-translational modifications through stable isotope labeling with
RT dithiothreitol.";
RL Proteomics 5:388-398(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-548, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-218, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC {ECO:0000250}.
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:0000250|UniProtKB:P06687}.
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; BC034645; AAH34645.1; -; mRNA.
DR EMBL; BC037206; AAH37206.1; -; mRNA.
DR EMBL; BC042894; AAH42894.1; -; mRNA.
DR CCDS; CCDS20969.2; -.
DR RefSeq; NP_001277398.1; NM_001290469.1.
DR AlphaFoldDB; Q6PIC6; -.
DR SMR; Q6PIC6; -.
DR BioGRID; 231339; 17.
DR IntAct; Q6PIC6; 10.
DR MINT; Q6PIC6; -.
DR STRING; 10090.ENSMUSP00000099922; -.
DR GlyConnect; 2725; 1 N-Linked glycan (1 site).
DR GlyGen; Q6PIC6; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q6PIC6; -.
DR PhosphoSitePlus; Q6PIC6; -.
DR SwissPalm; Q6PIC6; -.
DR jPOST; Q6PIC6; -.
DR MaxQB; Q6PIC6; -.
DR PaxDb; Q6PIC6; -.
DR PeptideAtlas; Q6PIC6; -.
DR PRIDE; Q6PIC6; -.
DR ProteomicsDB; 277263; -.
DR DNASU; 232975; -.
DR Ensembl; ENSMUST00000080882; ENSMUSP00000079691; ENSMUSG00000040907.
DR GeneID; 232975; -.
DR KEGG; mmu:232975; -.
DR UCSC; uc009frf.2; mouse.
DR CTD; 478; -.
DR MGI; MGI:88107; Atp1a3.
DR VEuPathDB; HostDB:ENSMUSG00000040907; -.
DR eggNOG; KOG0203; Eukaryota.
DR GeneTree; ENSGT00940000160476; -.
DR HOGENOM; CLU_002360_4_3_1; -.
DR InParanoid; Q6PIC6; -.
DR OMA; RRFLTYH; -.
DR OrthoDB; 388324at2759; -.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 232975; 3 hits in 60 CRISPR screens.
DR ChiTaRS; Atp1a3; mouse.
DR PRO; PR:Q6PIC6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6PIC6; protein.
DR Bgee; ENSMUSG00000040907; Expressed in primary visual cortex and 130 other tissues.
DR ExpressionAtlas; Q6PIC6; baseline and differential.
DR Genevisible; Q6PIC6; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0044305; C:calyx of Held; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0044327; C:dendritic spine head; ISO:MGI.
DR GO; GO:0044326; C:dendritic spine neck; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0098984; C:neuron to neuron synapse; IDA:ARUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0031090; C:organelle membrane; ISO:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
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:MGI.
DR GO; GO:0031748; F:D1 dopamine receptor binding; ISO:MGI.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IPI:BHF-UCL.
DR GO; GO:0099520; F:ion antiporter activity involved in regulation of presynaptic membrane potential; ISO:MGI.
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; IGI:BHF-UCL.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; IDA:BHF-UCL.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; ISO:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:1990535; P:neuron projection maintenance; ISO:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; IGI:BHF-UCL.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0006814; P:sodium ion transport; ISO:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
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_0000046299"
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:0000250|UniProtKB:P06687"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15648052"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06687"
FT MOD_RES 548
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 933
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
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
