Difference between revisions of "Potassium-transporting ATPase alpha chain 1"

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===Cys Function & Property===
 
===Cys Function & Property===
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From microsequence analysis, lansoprazole labels the enzyme at three positions, cysteine 321 in the TM3/4 domain, cys 813/822 in the TM5/6 domain, and cys 892 in the TM7/8 domain. Omeprazole labels the enzyme at two positions, again cys 813/822 in the TM5/6 domain and cys 892 in the TM718 domain. (PMID: 9405786)<br/>
  
 
* Hydrophobic property:
 
* Hydrophobic property:

Revision as of 04:16, 29 July 2019

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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+ and K+ ions across the plasma membrane. (From Uniprot, PMID: 10660561)

Cys Function & Property

From microsequence analysis, lansoprazole labels the enzyme at three positions, cysteine 321 in the TM3/4 domain, cys 813/822 in the TM5/6 domain, and cys 892 in the TM7/8 domain. Omeprazole labels the enzyme at two positions, again cys 813/822 in the TM5/6 domain and cys 892 in the TM718 domain. (PMID: 9405786)

  • Hydrophobic property:
496-hydro.png
  • SASA：
Unknown

Protein Sequence

MGKAENYELY SVELGPGPGG DMAAKMSKKK KAGGGGGKRK EKLENMKKEM
EINDHQLSVA ELEQKYQTSA TKGLSASLAA ELLLRDGPNA LRPPRGTPEY
VKFARQLAGG LQCLMWVAAA ICLIAFAIQA SEGDLTTDDN LYLAIALIAV
VVVTGCFGYY QEFKSTNIIA SFKNLVPQQA TVIRDGDKFQ INADQLVVGD
LVEMKGGDRV PADIRILAAQ GCKVDNSSLT GESEPQTRSP ECTHESPLET
RNIAFFSTMC LEGTVQGLVV NTGDRTIIGR IASLASGVEN EKTPIAIEIE
HFVDIIAGLA ILFGATFFIV AMCIGYTFLR AMVFFMAIVV AYVPEGLLAT
VTVCLSLTAK RLASKNCVVK NLEAVETLGS TSVICSDKTG TLTQNRMTVS
HLWFDNHIHT ADTTEDQSGQ TFDQSSETWR ALCRVLTLCN RAAFKSGQDA
VPVPKRIVIG DASETALLKF SELTLGNAMG YRDRFPKVCE IPFNSTNKFQ
LSIHTLEDPR DPRHLLVMKG APERVLERCS SILIKGQELP LDEQWREAFQ
TAYLSLGGLG ERVLGFCQLY LNEKDYPPGY AFDVEAMNFP SSGLCFAGLV
SMIDPPRATV PDAVLKCRTA GIRVIMVTGD HPITAKAIAA SVGIISEGSE
TVEDIAARLR VPVDQVNRKD ARACVINGMQ LKDMDPSELV EALRTHPEMV
FARTSPQQKL VIVESCQRLG AIVAVTGDGV NDSPALKKAD IGVAMGIAGS
DAAKNAADMI LLDDNFASIV TGVEQGRLIF DNLKKSIAYT LTKNIPELTP
YLIYITVSVP LPLGCITILF IELCTDIFPS VSLAYEKAES DIMHLRPRNP
KRDRLVNEPL AAYSYFQIGA IQSFAGFTDY FTAMAQEGWF PLLCVGLRAQ
WEDHHLQDLQ DSYGQEWTFG QRLYQQYTCY TVFFISIEVC QIADVLIRKT
RRLSAFQQGF FRNKILVIAI VFQVCIGCFL CYCPGMPNIF NFMPIRFQWW
LVPLPYGILI FVYDEIRKLG VRCCPGSWWD QELYY

Structural Information

  • Known structures with covalent ligands:
Unknown
  • Protein structure:
Unknown

Related Pathway

Experimental Evidence

Cys-directed mutation, Tricine-SDS-PAGE

Reference

  1. 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. 10660561
  2. 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. 9405786
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