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

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(Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|ATP4A, Proton pump|[https://www.uniprot.org/uniprot/P20648 P20648]|Homo sapiens|Cys323, Cys815,<br/>Cys894, Cys...")
 
 
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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) (TC 3.A.3) family,<br/>Type IIC subfamily|[[:Category:Potassium-transporting ATPase alpha chain 1|Ligand list]]}}
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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==
 
==Summary==
  
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===Cys Function & Property===
 
===Cys Function & Property===
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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:
 
* Hydrophobic property:
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==Experimental Evidence==
 
==Experimental Evidence==
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:Cys-directed mutation, Tricine-SDS-PAGE  
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:Cys-directed mutation, Tricine-SDS-PAGE, Microsequence analysis
  
 
==Reference==
 
==Reference==
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# 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/>  
 
# 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/>  
  
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[[Category:Targets|Targets]]
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[[Category:Targets]]
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[[Category:Homo sapiens|Homo sapiens]]
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[[Category:Homo sapiens]]
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[[Category:Cation transport ATPase (P-type) (TC 3.A.3) family|Cation transport ATPase (P-type) (TC 3.A.3) family]]
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[[Category:Ion channel]]
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[[Category:Type IIC subfamily|Type IIC subfamily]]
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[[Category:Cation transport ATPase (P-type) family]]
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[[Category:Oxidative phosphorylation|Oxidative phosphorylation]]
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[[Category:Type IIC subfamily]]
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[[Category:Metabolic pathways|Metabolic pathways]]
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[[Category:Oxidative phosphorylation]]
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[[Category:Gastric acid secretion|Gastric acid secretion]]
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[[Category:Metabolic pathways]]
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[[Category:Collecting duct acid secretion|Collecting duct acid secretion]]
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[[Category:Gastric acid secretion]]
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[[Category:Collecting duct acid secretion]]
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[[Category:Focal adhesion]]

Latest revision as of 04:18, 25 August 2019

Basic Information
Short Name ATP4A, Proton pump
UNP ID P20648
Organism Homo sapiens
Cys Site Cys323, Cys815,
Cys894, Cys824
Family/Domain Cation transporting ATPase, C-terminus,
Cation transporting ATPase, N-terminus,
Cation transport ATPase (P-type) family, Type IIC subfamily
Known Ligand Ligand list
Function Type 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+ and K+ ions across the plasma membrane. (From Uniprot, PMID: 10660561)

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)

  • 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, Microsequence analysis

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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