Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00390
Entry Name
UniProt Accession
Theoretical PI
5.3
Molecular Weight
112982.17
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Sodium/potassium-transporting ATPase subunit alpha-1
Protein Synonyms/Alias
Na(+)/K(+) ATPase alpha-1 subunit; 3.6.3.9; Sodium pump subunit alpha-1;
Gene Name
Atp1a1
Gene Synonyms/Alias
Created Date
05-JUL-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
606
Canonical
VPDAVGKCRSAGIKV
[1]
S-Palmitoylation
937
Canonical
QWADLVICKTRRNSV
[1]
S-Palmitoylation
990
Canonical
LKPTWWFCAFPYSLL
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (By similarity).
Sequence Annotation
Topological domain: 6 96 Cytoplasmic.
Transmembrane: 97 117 Helical.
Topological domain: 118 129 Extracellular.
Transmembrane: 130 150 Helical.
Topological domain: 151 291 Cytoplasmic.
Transmembrane: 292 312 Helical.
Topological domain: 313 319 Extracellular.
Transmembrane: 320 340 Helical.
Topological domain: 341 789 Cytoplasmic.
Transmembrane: 790 810 Helical.
Topological domain: 811 865 Extracellular.
Transmembrane: 866 886 Helical.
Topological domain: 887 915 Cytoplasmic.
Transmembrane: 916 936 Helical.
Topological domain: 937 952 Extracellular.
Transmembrane: 953 973 Helical.
Topological domain: 974 979 Cytoplasmic.
Transmembrane: 980 1000 Helical.
Topological domain: 1001 1023 Extracellular.
Region: 82 84 Phosphoinositide-3 kinase binding.
Active site: 376 376 4-aspartylphosphate intermediate.
Metal binding site: 717 717 Magnesium.
Metal binding site: 721 721 Magnesium.
Binding site: 487 487 ATP.
Modified residue: 9 9 N6-acetyllysine.
Modified residue: 10 10 Phosphotyrosine.
Modified residue: 16 16 Phosphoserine.
Modified residue: 21 21 N6-acetyllysine.
Modified residue: 260 260 Phosphotyrosine.
Modified residue: 542 542 Phosphotyrosine.
Modified residue: 661 661 N6-succinyllysine.
Modified residue: 943 943 Phosphoserine; by PKA.
Protein Length
1023 AA.
Protein Sequence
(Canonical)
MGKGVGRDKY EPAAVSEHGD KKGKKAKKER DMDELKKEVS MDDHKLSLDE LHRKYGTDLS  60
RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SMLLWIGAIL CFLAYGIRSA  120
TEEEPPNDDL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI  180
NAEDVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR  240
NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV  300
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN  360
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWFA  420
LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI EVCCGSVMEM REKYSKIVEI  480
PFNSTNKYQL SIHKNPNASE PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN  540
AYLELGGLGE RVLGFCHLLL PDEQFPEGFQ FDTDDVNFPV DNLCFVGLIS MIDPPRAAVP  600
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVNQVNPRDA  660
KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN  720
DSPALKKADI GVAMGIVGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL  780
TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK  840
TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRETW DDRWVNDVED  900
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE  960
ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE  1020
TYY                                                                1023
FASTA
(Canonical)
>LipidDB-10090-00390|Q8VDN2
MGKGVGRDKYEPAAVSEHGDKKGKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLS
RGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRSA
TEEEPPNDDLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSI
NAEDVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETR
NIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAEEIEHFIHLITGVAV
FLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKN
LEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWFA
LSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIEVCCGSVMEMREKYSKIVEI
PFNSTNKYQLSIHKNPNASEPKHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQN
AYLELGGLGERVLGFCHLLLPDEQFPEGFQFDTDDVNFPVDNLCFVGLISMIDPPRAAVP
DAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNQVNPRDA
KACVVHGSDLKDMTSEELDDILRYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVN
DSPALKKADIGVAMGIVGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTL
TSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPK
TDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPFHLLGIRETWDDRWVNDVED
SYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFE
ETALAAFLSYCPGMGAALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKE
TYY
Gene Ontology
GO:0016324; C:apical plasma membrane; IDA:MGI
GO:0016323; C:basolateral plasma membrane; IDA:MGI
GO:0005901; C:caveola; IEA:Ensembl
GO:0005783; C:endoplasmic reticulum; IEA:Ensembl
GO:0005768; C:endosome; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005794; C:Golgi apparatus; IEA:Ensembl
GO:0016021; C:integral component of membrane; ISS:UniProtKB
GO:0005886; C:plasma membrane; IDA:MGI
GO:0043234; C:protein complex; ISO:MGI
GO:0042383; C:sarcolemma; IDA:BHF-UCL
GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:Ensembl
GO:0030315; C:T-tubule; IDA:BHF-UCL
GO:0043531; F:ADP binding; IEA:Ensembl
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0016791; F:phosphatase activity; IMP:MGI
GO:0030955; F:potassium ion binding; IEA:Ensembl
GO:0031402; F:sodium ion binding; IEA:Ensembl
GO:0005391; F:sodium:potassium-exchanging ATPase activity; IDA:MGI
GO:0006754; P:ATP biosynthetic process; IEA:InterPro
GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl
GO:0016311; P:dephosphorylation; IMP:GOC
GO:0060081; P:membrane hyperpolarization; IEA:Ensembl
GO:0031947; P:negative regulation of glucocorticoid biosynthetic process; IMP:MGI
GO:0045822; P:negative regulation of heart contraction; IMP:MGI
GO:0045823; P:positive regulation of heart contraction; IMP:MGI
GO:0045989; P:positive regulation of striated muscle contraction; IMP:MGI
GO:0010107; P:potassium ion import; IEA:Ensembl
GO:0008217; P:regulation of blood pressure; IGI:MGI
GO:0086004; P:regulation of cardiac muscle cell contraction; IEA:Ensembl
GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB
GO:0002026; P:regulation of the force of heart contraction; IMP:MGI
GO:0042493; P:response to drug; IMP:MGI
GO:0035725; P:sodium ion transmembrane transport; IDA:GOC
Interpro
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N
InterPro; IPR023299; ATPase_P-typ_cyto_domN
InterPro; IPR005775; ATPase_P-typ_Na/K_IIC
InterPro; IPR018303; ATPase_P-typ_P_site
InterPro; IPR023298; ATPase_P-typ_TM_dom
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A
InterPro; IPR001757; Cation_transp_P_typ_ATPase
InterPro; IPR023214; HAD-like_dom
Pfam
Pfam; PF00689; Cation_ATPase_C;
Pfam; PF00690; Cation_ATPase_N;
Pfam; PF00122; E1-E2_ATPase;
Pfam; PF00702; Hydrolase;
SMART
SMART; SM00831; Cation_ATPase_N;
PROSITE
PROSITE; PS00154; ATPASE_E1_E2;
PRINTS
PRINTS; PR00119; CATATPASE;