Summary: Protein-arginine deiminase (PAD)
Protein-arginine deiminase (PAD) Provide feedback
Members of this family are found in mammals. In the presence of calcium ions, PAD enzymes EC:220.127.116.11 catalyse the post-translational modification reaction responsible for the formation of citrulline residues: Protein L-arginine + H2O <=> Protein L-citrulline + NH3. Several types are recognised (and included in the family) on the basis of molecular mass, substrate specificity, and tissue localisation. The expression of type I PAD is known to be under the control of oestrogen .
Rogers G, Winter B, McLaughlan C, Powell B, Nesci T; , J Invest Dermatol 1997;108:700-707.: Peptidylarginine deiminase of the hair follicle: characterization, localization, and function in keratinizing tissues. PUBMED:9129218 EPMC:9129218
Asaga H, Ishigami A; , Neurosci Lett 2001;299:5-8.: Protein deimination in the rat brain after kainate administration: citrulline-containing proteins as a novel marker of neurodegeneration. PUBMED:11166924 EPMC:11166924
Rus'd AA, Ikejiri Y, Ono H, Yonekawa T, Shiraiwa M, Kawada A, Takahara H; , Eur J Biochem 1999;259:660-669.: Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse. PUBMED:10092850 EPMC:10092850
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013530
In the presence of calcium ions, Protein-arginine deiminase (PAD) enzymes EC catalyse the post-translational modification reaction responsible for the formation of citrulline residues from protein-bound arginine residues [PUBMED:10092850]. Four PAD isotypes of PAD have been identified in mammals, a fifth may also exist. Non-mammalian vertebrates appear to have only a single PAD enzyme. All known natural substrates of PAD are proteins known to have an important structural function, such as keratin (PAD1), intermediate filaments or proteins associated with intermediate filaments. Citrulination may have consequences for the structural integrity and interactions of these proteins. Physiological levels of calcium appear to be too low to activate these enzymes suggesting a role between PAD activation and loss of calcium homeostasis during terminal differentiation and cell death (apoptosis).
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||cytoplasm (GO:0005737)|
|Molecular function||calcium ion binding (GO:0005509)|
|protein-arginine deiminase activity (GO:0004668)|
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This superfamily contains a number of related enzymes such as AstB, peptidyl-arginine deiminase, arginine deiminase and amidinotransferase [1,2].
The clan contains the following 4 members:Amidinotransf AstB PAD PAD_porph
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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Curation and family details
|Seed source:||Pfam-B_2195 (release 6.4)|
|Number in seed:||7|
|Number in full:||323|
|Average length of the domain:||310.40 aa|
|Average identity of full alignment:||44 %|
|Average coverage of the sequence by the domain:||60.02 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||10|
|Download:||download the raw HMM for this family|
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There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PAD domain has been found. There are 12 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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