NiceProt View of Swiss-Prot: P18907
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1 Hosted by NCSC US ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot Mirror sites: Australia Bolivia Canada China Korea Switzerland Taiwan Search Swiss-Prot/TrEMBL for horse alpha Go Clear NiceProt View of Swiss-Prot: P18907 Printer-friendly view Submit update Quick BlastP se [Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools] Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents. Entry information Entry name A1A1_HORSE Primary accession number P18907 Secondary accession numbers None Entered in Swiss-Prot in Release 16, November 1990 Sequence was last modified in Release 16, November 1990 Annotations were last modified in Release 43, March 2004 Name and origin of the protein Protein name Sodium/potassium-transporting ATPase alpha-1 chain [Precursor] Synonyms EC Sodium pump 1 Na+/K+ ATPase 1 Gene name ATP1A1 From Equus caballus (Horse) [TaxID: 9796] Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Perissodactyla; Equidae; Equus. References 1 of 7 2/9/04 4:28 PM
2 [1] SEQUENCE FROM NUCLEIC ACID. MEDLINE= ; PubMed= ; [NCBI, ExPASy, EBI, Israel, Japan] Kano I., Nagai F., Satoh K., Ushiyama K., Nakao T., Kano K.; "Structure of the alpha 1 subunit of horse Na,K-ATPase gene."; FEBS Lett. 250:91-98(1989). Comments FUNCTION: 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. CATALYTIC ACTIVITY: ATP + H 2 O + Na + (In) + K + (Out) = ADP + phosphate + Na + (Out) + K + (In). SUBUNIT: Composed of three subunits: alpha (catalytic), beta and gamma. SUBCELLULAR LOCATION: Integral membrane protein. PTM: Phosphorylation on Tyr-10 modulates pumping activity (By similarity). SIMILARITY: Belongs to the cation transport ATPases family (P-type ATPases). Subfamily IIC. Copyright This Swiss-Prot entry is copyright. It is produced through a collaboration between the Swiss Institute of Bioinformatics and the EMBL outstation - the European Bioinformatics Institute. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See or send an to license@isb-sib.ch) Cross-references X16773; CAA ; -. [EMBL / GenBank / DDBJ] X16774; CAA ; [EMBL / GenBank / DDBJ] X16775; CAA ; [EMBL / GenBank / DDBJ] X16776; CAA ; [EMBL / GenBank / DDBJ] X16777; CAA ; [EMBL / GenBank / DDBJ] EMBL X16778; CAA ; [EMBL / GenBank / DDBJ] X16779; CAA ; [EMBL / GenBank / DDBJ] X16780; CAA ; [EMBL / GenBank / DDBJ] X16781; CAA ; [EMBL / GenBank / DDBJ] X16782; CAA ; [EMBL / GenBank / DDBJ] 2 of 7 2/9/04 4:28 PM
3 X16783; CAA ; [EMBL / GenBank / DDBJ] X16784; CAA ; [EMBL / GenBank / DDBJ] X16785; CAA ; [EMBL / GenBank / DDBJ] X16786; CAA ; [EMBL / GenBank / DDBJ] X16787; CAA ; [EMBL / GenBank / DDBJ] X16788; CAA ; [EMBL / GenBank / DDBJ] X16789; CAA ; [EMBL / GenBank / DDBJ] X16790; CAA ; [EMBL / GenBank / DDBJ] X16791; CAA ; [EMBL / GenBank / DDBJ] X16792; CAA ; [EMBL / GenBank / DDBJ] X16793; CAA ; [EMBL / GenBank / DDBJ] X16794; CAA ; [EMBL / GenBank / DDBJ] X16795; CAA ; [EMBL / GenBank / DDBJ] PIR S04630; S HSSP P04191; 1EUL. [HSSP ENTRY / PDB] GO: ; Cellular component: sodium/potassium-exchanging ATPase complex (inferred from sequence or structural similarity). GO: ; Molecular function: sodium/potassium-exchanging ATPase activity (inferred from sequence or structural similarity). GO: ; Biological process: ATP hydrolysis coupled proton transport (inferred from sequence or structural similarity). GO GO: ; Biological process: hydrogen ion homeostasis (inferred from sequence or structural similarity). GO: ; Biological process: potassium ion transport (inferred from sequence or structural similarity). GO: ; Biological process: sodium ion transport (inferred from sequence or structural similarity). GO: ; Biological process: sperm motility (inferred from sequence or structural similarity). IPR001757; ATPase_E1-E2. InterPro IPR006069; Cation_ATPase. IPR006068; Cation_ATPase_C. 3 of 7 2/9/04 4:28 PM
4 IPR004014; Cation_ATPase_N. IPR008250; E1-E2_ATPase_reg. IPR005834; Hydrolase. IPR005775; Na/K_ATPase_alph. Graphical view of domain structure. PF00689; Cation_ATPase_C; 1. PF00690; Cation_ATPase_N; 1. Pfam PF00122; E1-E2_ATPase; 1. PF00702; Hydrolase; 1. Pfam graphical view of domain structure. PR00119; CATATPASE. PRINTS PR00121; NAKATPASE. TIGR01106; ATPase-IIC_X-K; 1. TIGRFAMs TIGR01494; ATPase_P-type; 5. PROSITE PS00154; ATPASE_E1_E2; 1. ProDom [Domain structure / List of seq. sharing at least 1 domain] HOVERGEN [Family / Alignment / Tree] BLOCKS P ProtoNet P ProtoMap P PRESAGE P DIP P ModBase P SMR P18907; 4FEB03FFB04E0216. SWISS-2DPAGE Get region on 2D PAGE. Keywords Hydrolase; Sodium/potassium transport; Transmembrane; Phosphorylation; Magnesium; Metal-binding; ATP-binding; Multigene family. Features Feature table viewer Feature aligner Key From To Length Description PROPEP By similarity. CHAIN Sodium/potassium-transporting ATPase alpha-1 chain. DOMAIN Cytoplasmic (Potential). TRANSMEM Potential. DOMAIN Lumenal (Potential). TRANSMEM Potential. DOMAIN Cytoplasmic (Potential). TRANSMEM Potential. DOMAIN Lumenal (Potential). 4 of 7 2/9/04 4:28 PM
5 TRANSMEM Potential. DOMAIN Cytoplasmic (Potential). TRANSMEM Potential. DOMAIN Lumenal (Potential). TRANSMEM Potential. DOMAIN Cytoplasmic (Potential). TRANSMEM Potential. DOMAIN Lumenal (Potential). TRANSMEM Potential. DOMAIN Cytoplasmic (Potential). TRANSMEM Potential. DOMAIN Lumenal (Potential). TRANSMEM Potential. DOMAIN Cytoplasmic (Potential). MOD_RES PHOSPHORYLATION (BY SIMILARITY). MOD_RES PHOSPHORYLATION (BY PKC) (BY SIMILARITY). MOD_RES PHOSPHORYLATION (BY SIMILARITY). MOD_RES PHOSPHORYLATION (BY PKA) (BY SIMILARITY). BINDING BINDING OF PHOSPHOINOSITIDE-3 KINASE (BY SIMILARITY). METAL Magnesium (By similarity). METAL Magnesium (By similarity). Sequence information Length: 1021 AA [This is the length of the unprocessed precursor] Molecular weight: Da [This is the MW of the unprocessed precursor] CRC64: 4FEB03FFB04E0216 [This is a checksum on the sequence] MGKGGGRDKY EPAAISEHGN KKKAKKERDM DELKKEVSMD DHKLSLDELQ RKYGTDLSRG LTTARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM LLWIGAILCF LAYGIQAATE EEPQNDNLYL GVVLSAVVII TGCFSYYQEA KSSKIMESFK NMVPQQALVV RNGEKMSINA EEVVVGDLVE VKGGDRIPAD LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI AFFSTNCVEG TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL P18907 in FASTA format 5 of 7 2/9/04 4:28 PM
6 GVTFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TENQSGVSFD KTSATWLSLS RIAGLCNRAV FQANQENIPI LKRAVAGDAS ESALLKCIEL CCGSVKEMRD RYPKIVEIPF NSTNKYQLSI HKNPNTSEPQ HLLVMKGAPE RILDRCSSIL LNGKEQPLDE ELKDAFQNAY LELGGLGERV LGFCHLFLPD EQFPEGFQFD TDDVNFPLEN LCFVGLISMI DPPRAAVPDA VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISEGNETVE DIAARLNIPV SQVNPRDAKA CVVHGSDLKD MTPEQLDDIL RHHTEIVFAR TSPQQKLIIV EGCQRQGAIV AVTGDGVNDS PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS NIPEITPFLI FIIANIPLPL GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPQTD KLVNERLISM AYGQIGMIQA LGGFFTYFVI LAENGFLPIH LLGLRVDWDD RWVNDVEDSY GQQWTYEQRK IVEFTCHTAF FVSIVVVQWA DLVICKTRRN SVFQQGMKNK ILIFGLFEET ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD EVRKLIIRRR PGGWVEKETY Y View entry in original Swiss-Prot format 6 of 7 2/9/04 4:28 PM
7 View entry in raw text format (no links) Report form for errors/updates in this Swiss-Prot entry BLAST submission on ExPASy/SIB or at NCBI (USA) Sequence analysis tools: ProtParam, ProtScale, Compute pi/mw, PeptideMass, PeptideCutter, Dotlet (Java) ScanProsite, MotifScan Search the SWISS-MODEL Repository Hosted by NCSC US ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot Mirror sites: Australia Bolivia Canada China Korea Switzerland Taiwan 7 of 7 2/9/04 4:28 PM
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