View source for Potassium-transporting ATPase alpha chain 1

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{{#invoke:InfoboxforTarget|run|ATP4A, Proton pump|[https://www.uniprot.org/uniprot/P20648 P20648]|Homo sapiens|Cys323, Cys815,<br/>Cys894, Cys824|[http://pfam.xfam.org/family/PF00689 Cation transporting ATPase, C-terminus],<br/>[http://pfam.xfam.org/family/PF00690 Cation transporting ATPase, N-terminus],<br/>Cation transport ATPase (P-type) family, Type IIC subfamily|[[:Category:Potassium-transporting ATPase alpha chain 1|Ligand list]]|Ion channel}}
==Summary==

===Protein Function ===
The H,K-ATPase (ATP4A), also known as Gastric H(+)/K(+) ATPase subunit alpha, the enzyme responsible for generating gastric acid by pumping hydronium ions out of the parietal cell of the stomach in exchange for potassium, belongs to the family of P2-type ATPases and has homology with other members of this family such as the Na,K-ATPases (65%) and Ca-ATPases (23%). ATP4A Catalyzes the hydrolysis of ATP coupled with the exchange of H<sup>+</sup> and K<sup>+</sup> ions across the plasma membrane. (From Uniprot, PMID: 10660561)
<br/>

===Cys Function & Property===
From microsequence analysis, lansoprazole labels the enzyme at three positions, Cys321 in the TM3/4 domain, Cys813/822 in the TM5/6 domain, and Cys892 in the TM7/8 domain. Omeprazole labels the enzyme at two positions, again Cys813/822 in the TM5/6 domain and Cys892 in the TM718 domain. (PMID: 9405786)<br/>

* Hydrophobic property:
:[[File:496-hydro.png||600px]]
* SASA：
:Unknown

==Protein Sequence==
<font face="Courier">
MGKAENYELY SVELGPGPGG DMAAKMSKKK KAGGGGGKRK EKLENMKKEM <br/>
EINDHQLSVA ELEQKYQTSA TKGLSASLAA ELLLRDGPNA LRPPRGTPEY <br/>
VKFARQLAGG LQCLMWVAAA ICLIAFAIQA SEGDLTTDDN LYLAIALIAV <br/>
VVVTGCFGYY QEFKSTNIIA SFKNLVPQQA TVIRDGDKFQ INADQLVVGD <br/>
LVEMKGGDRV PADIRILAAQ GCKVDNSSLT GESEPQTRSP ECTHESPLET <br/>
RNIAFFSTMC LEGTVQGLVV NTGDRTIIGR IASLASGVEN EKTPIAIEIE <br/>
HFVDIIAGLA ILFGATFFIV AM<span style="background:#ffff00">'''C'''</span>IGYTFLR AMVFFMAIVV AYVPEGLLAT <br/>
VTVCLSLTAK RLASKNCVVK NLEAVETLGS TSVICSDKTG TLTQNRMTVS <br/>
HLWFDNHIHT ADTTEDQSGQ TFDQSSETWR ALCRVLTLCN RAAFKSGQDA <br/>
VPVPKRIVIG DASETALLKF SELTLGNAMG YRDRFPKVCE IPFNSTNKFQ <br/>
LSIHTLEDPR DPRHLLVMKG APERVLERCS SILIKGQELP LDEQWREAFQ <br/>
TAYLSLGGLG ERVLGFCQLY LNEKDYPPGY AFDVEAMNFP SSGLCFAGLV <br/>
SMIDPPRATV PDAVLKCRTA GIRVIMVTGD HPITAKAIAA SVGIISEGSE <br/>
TVEDIAARLR VPVDQVNRKD ARACVINGMQ LKDMDPSELV EALRTHPEMV <br/>
FARTSPQQKL VIVESCQRLG AIVAVTGDGV NDSPALKKAD IGVAMGIAGS <br/>
DAAKNAADMI LLDDNFASIV TGVEQGRLIF DNLKKSIAYT LTKNIPELTP <br/>
YLIYITVSVP LPLG<span style="background:#ffff00">'''C'''</span>ITILF IEL<span style="background:#ffff00">'''C'''</span>TDIFPS VSLAYEKAES DIMHLRPRNP <br/>
KRDRLVNEPL AAYSYFQIGA IQSFAGFTDY FTAMAQEGWF PLL<span style="background:#ffff00">'''C'''</span>VGLRAQ <br/>
WEDHHLQDLQ DSYGQEWTFG QRLYQQYTCY TVFFISIEVC QIADVLIRKT <br/>
RRLSAFQQGF FRNKILVIAI VFQVCIGCFL CYCPGMPNIF NFMPIRFQWW <br/>
LVPLPYGILI FVYDEIRKLG VRCCPGSWWD QELYY <br/> 
</font>

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

*Protein structure:
:Unknown <br/>

==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/>
*[https://www.genome.jp/kegg-bin/show_pathway?ko04510 Focal adhesion] <br/>

==Experimental Evidence==
:Cys-directed mutation, Tricine-SDS-PAGE, Microsequence analysis

==Reference==
# Lambrecht N, Munson K, Vagin O, et al. '''Comparison of covalent with reversible inhibitor binding sites of the gastric H, K-ATPase by site-directed mutagenesis[J].''' Journal of Biological Chemistry, 2000, 275(6): 4041-4048. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10660561 10660561]<br/> 
# Shin J M, Besancon M, Bamberg K, et al. '''Structural aspects of the gastric H, K ATPase[J].''' Annals of the New York Academy of Sciences, 1997, 834: 65-76. [https://www.ncbi.nlm.nih.gov/pubmed/?term=9405786 9405786]<br/> 

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