View source for Potassium-transporting ATPase alpha chain 1 (Sus scrofa)

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{{#invoke:InfoboxforTarget|run|ATP4A|[https://www.uniprot.org/uniprot/P19156 P19156]|Sus scrofa|Cys814, Cys823|[http://pfam.xfam.org/family/PF00689 Cation transporting ATPase, C-terminus],<br/>Cation transport ATPase (P-type) family,<br/>Type IIC subfamily|[[:Category:Potassium-transporting ATPase alpha chain 1 (Sus scrofa)|Ligand list]]|Ion channel}}

==Summary==

===Protein Function ===
The gastric hydrogen potassium ATPase or H<sup>+</sup>/K<sup>+</sup> ATPase is the proton pump of the stomach. It exchanges potassium from the intestinal lumen with cytoplasmic hydronium and is the enzyme primarily responsible for the acidification of the stomach contents and the activation of the digestive enzyme pepsin. <br/>
H<sup>+</sup>/K<sup>+</sup> ATPase is a P2-type ATPase, a member of the eukaryotic class of P-type ATPases. Like the Ca2<sup>+</sup> and the Na<sup>+</sup>/K<sup>+</sup> ATPases, the H<sup>+</sup>/K<sup>+</sup> ATPase functions as an α, β protomer. Unlike other eukaryotic ATPases, the H<sup>+</sup>/K<sup>+</sup> ATPase is electroneutral, transporting one proton into the stomach lumen per potassium retrieved from the gastric lumen. As an ion pump the H+/K+ ATPase is able to transport ions against a concentration gradient using energy derived from the hydrolysis of ATP. Like all P-type ATPases, a phosphate group is transferred from adenosine triphosphate (ATP) to the H<sup>+</sup>/K<sup>+</sup> ATPase during the transport cycle. This phosphate transfer powers a conformational change in the enzyme that helps drive ion transport. (From Wikipedia)<br/>
[[File:584-586-function.jpg|center|450px]]
<div align="center">Proton pump function</div>

===Cys Function & Property===
* Hydrophobic property:
:[[File:584-hydro.png||600px]]
* SASA：
:Cys814: 24.44 A^2 <br/>
:Cys823: 27.265 A^2 <br/>

==Protein Sequence==
<font face="Courier">
MGKAENYELY QVELGPGPSG DMAAKMSKKK AGRGGGKRKE KLENMKKEME <br/>
INDHQLSVAE LEQKYQTSAT KGLSASLAAE LLLRDGPNAL RPPRGTPEYV <br/>
KFARQLAGGL QCLMWVAAAI CLIAFAIQAS EGDLTTDDNL YLALALIAVV <br/>
VVTGCFGYYQ EFKSTNIIAS FKNLVPQQAT VIRDGDKFQI NADQLVVGDL <br/>
VEMKGGDRVP ADIRILQAQG RKVDNSSLTG ESEPQTRSPE CTHESPLETR <br/>
NIAFFSTMCL EGTAQGLVVN TGDRTIIGRI ASLASGVENE KTPIAIEIEH <br/>
FVDIIAGLAI LFGATFFIVA MCIGYTFLRA MVFFMAIVVA YVPEGLLATV <br/>
TVCLSLTAKR LASKNCVVKN LEAVETLGST SVICSDKTGT LTQNRMTVSH <br/>
LWFDNHIHSA DTTEDQSGQT FDQSSETWRA LCRVLTLCNR AAFKSGQDAV <br/>
PVPKRIVIGD ASETALLKFS ELTLGNAMGY RERFPKVCEI PFNSTNKFQL <br/>
SIHTLEDPRD PRHVLVMKGA PERVLERCSS ILIKGQELPL DEQWREAFQT <br/>
AYLSLGGLGE RVLGFCQLYL SEKDYPPGYA FDVEAMNFPT SGLSFAGLVS <br/>
MIDPPRATVP DAVLKCRTAG IRVIMVTGDH PITAKAIAAS VGIISEGSET <br/>
VEDIAARLRV PVDQVNRKDA RACVINGMQL KDMDPSELVE ALRTHPEMVF <br/>
ARTSPQQKLV IVESCQRLGA IVAVTGDGVN DSPALKKADI GVAMGIAGSD <br/>
AAKNAADMIL LDDNFASIVT GVEQGRLIFD NLKKSIAYTL TKNIPELTPY <br/>
LIYITVSVPL PLG<span style="background:#ffff00">'''C'''</span>ITILFI EL<span style="background:#ffff00">'''C'''</span>TDIFPSV SLAYEKAESD IMHLRPRNPK <br/>
RDRLVNEPLA AYSYFQIGAI QSFAGFTDYF TAMAQEGWFP LLCVGLRPQW <br/>
ENHHLQDLQD SYGQEWTFGQ RLYQQYTCYT VFFISIEMCQ IADVLIRKTR <br/>
RLSAFQQGFF RNRILVIAIV FQVCIGCFLC YCPGMPNIFN FMPIRFQWWL <br/>
VPMPFGLLIF VYDEIRKLGV RCCPGSWWDQ ELYY                   <br/> 
</font>

==Structural Information==
*Known structures with covalent ligands: <br/>
:Unknown<br/> 

*Protein structure:
[[File:584.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko00190 Oxidative phosphorylation] <br/>
*[https://www.genome.jp/kegg-bin/show_pathway?ko01100 Metabolic pathways] <br/>
*[https://www.genome.jp/kegg-bin/show_pathway?ko04966 Collecting duct acid secretion] <br/>
*[https://www.genome.jp/kegg-bin/show_pathway?ko04971 Gastric acid secretion] <br/>

==Experimental Evidence==
:Tryptic Digest, Isotope Labeling, Tricine-SDS-PAGE, Homologous Analysis of Sequence

==Reference==
# Shin J M, Besancon M, Simon A, et al. '''The site of action of pantoprazole in the gastric H+/K+-ATPase[J].''' Biochimica et Biophysica Acta (BBA)-Biomembranes, 1993, 1148(2): 223-233. [https://www.ncbi.nlm.nih.gov/pubmed/?term=8389196 8389196]<br/> 
# Morii M, Takata H, Fujisaki H, et al. '''The potency of substituted benzimidazoles such as E3810, omeprazole, Ro 18-5364 to inhibit gastric H+, K+-ATPase is correlated with the rate of acid-activation of the inhibitor[J].''' Biochemical pharmacology, 1990, 39(4): 661-667. [https://www.ncbi.nlm.nih.gov/pubmed/?term=2154989 2154989]<br/>

[[Category:Targets]]
[[Category:Sus scrofa]]
[[Category:Ion channel]]
[[Category:Cation transport ATPase (P-type) family]]
[[Category:Type IIC subfamily]]
[[Category:Oxidative phosphorylation]]
[[Category:Metabolic pathways]]
[[Category:Collecting duct acid secretion]]
[[Category:Gastric acid secretion]]