Function for haloacid dehalogenase-like hydrolase domain containing 2: Difference between revisions
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Revision as of 12:40, 9 June 2007
Haloacid dehalogenase-like hydrolase domain containing 2 (2HO4:A,B)
Where's does the name come from?
Hydolase indicates this protein's main molecular function, hydrolase activity. /Link
Definition of hydrolase activity:
Catalysis of the hydrolysis of various bonds
e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
Hydolysis is a breakdown process of compounds in the body,
by replace the covalent bond with water molecule and making the product more water soluble.
Domain containing 2
Domain containing 2 are illustrating it has 2 domains.
Sequence and Secondary Structure /Link
From the above diagram, two domains are showed separately and color in blue and purple.
Type: polypeptide(L)
Length: 259 residues
Secondary Structure: 44% helical (14 helices; 123 residues) 17% beta sheet (12 strands; 48 residues)
2HO4Aa: pdp domain 2HO4Aa (in purple)
2HO4Ab: pdp domain 2HO4Ab (in blue)
What does it mean when protein with 2 domains?
It could either be 2 binding site?
Or, more than one type of molecular function?
Mouse Genome Informatics(MGI)
We found 5 Category of Function or Process with evidence in this protein.
GO Annotations in Tabular Form/Link
Category | Classification | Term Evidence | Inferred From | Ref(s) |
---|---|---|---|---|
Molecular Function | catalytic activity | IEA | InterPro:IPR005834 | J:72247 |
Molecular Function | hydrolase activity | IEA | InterPro:IPR006357 | J:72247 |
Molecular Function | hydrolase activity | IEA | SP_KW:KW-0378 | J:60000 |
Molecular Function | magnesium ion binding | IEA | SP_KW:KW-0460 | J:60000 |
Biological Process | metabolic process | IEA | InterPro:IPR005834,InterPro:IPR006357 | J:72247 |
Gene Ontology Evidence Code Abbreviations: IC Inferred by curator IDA Inferred from direct assay IEA Inferred from electronic annotation IGI Inferred from genetic interaction IMP Inferred from mutant phenotype IPI Inferred from physical interaction ISS Inferred from sequence or structural similarity NAS Non-traceable author statement ND No biological data available RCA Reviewed computational analysis TAS Traceable author statement
So where's the evidence from?
The evidence was done by Mammalian Orthology Load, which the information was derived from Homologene National Center for Biotechnology Information. This protein was reviewed in 2004 and record with J Number: J:90500.
The Mammalian Orthology Query Result proven, the evidence was from using both Amino acid sequence comparison and Nucleotide sequence comparison on different species. And the results shown human, mouse, rat, chimpanzee and dog all has the sequence of this protein.
Protein Data Bank (PDB)
Ligands and Prosthetic Groups
ID | Name Chemical | Formula | Weight Ligand | Link |
---|---|---|---|---|
PO4 | Phosphate Ion | O4 P 3- | 94.971 | /View |
MG | Magnesium Ion | Mg 2+ | 24.305 | /View |
MSE | Selenomethionine | C5 H11 N O2 Se | 196.107 | /View |
PBD Biology and Chemistry Report /Link
Where does the protein mainly locate?
Genomics Institute of the Novartis Research Foundation /Link
The diagram illustrate the expression of protein or gene in different organisms
What are the conlcusion we can withdraw from the diagram above?
The sequence expression of the protein appears more in amygdala, cortex, hypothalamus, spinal cord, dentritic cells, T cells, B cells and lymphatic system. Which means this protein expression mainly functioning in the central nerve system and immune system.
May be
How does the protein function?
What are basis of Haloacid dehalogenase family?
Identification on Haloacid dehalogenase family on the basis of the structural similarities has been described. The HAD superfamily has similar reaction mechanism base on its structure. The basis of structural of HAD family are hydrolases contains enzymes (such as L-2-haloacid dehalogenase, epoxide hydrolase), variety of phosphatases (e.g. phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase and sucrose-phosphate synthase), and the catalytic subunits (such as the P-type ATPases). The ATPases are essential for the transport of cations across biological membranes, because it contains the binding sites for ATP and Mg2, and a phosphorylation site.
What are the functions?
A research was done in 1979, by administrating chlorpromazine at the rate of 15 milligram per kilogram to rats. By determining mitochondria of the sensomotor cortex and localize Mg-activated ATPase in the cortex, the result shown hydrolase activity increased in the brain after three hours administration. The disscussion suggest the increase of ATP-hydrolase activity in the cortex will induce depression of glycolytic and respiratory activity of the cells. And this is cause by increase of permeability of the mitochndrial membranes. (Kleshchinov et al., 1979)
Literature to read
http://www.springerlink.com/content/mmt8t16q20131540/
What about it's functional partners
From /STRING uses orthology information from the excellent COG database, we predicted it's functional partners.
From the result of occurrence we discover KIAA0423 annotation, which is still not available (1723 aa) is it best suit predicted Functional Partners. /Link
The above result shows using protein sequence to compare difference species and their .
e.g. Pan troglodytes and Homo sapiens are two species highly conservatity