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{{Infobox_gene}}
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'''Peptidyl arginine deiminase, type III''', also known as '''PADI3''', is a [[protein]] which in humans is encoded by the ''PADI3'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PADI3 peptidyl arginine deiminase, type III| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51702| accessdate = }}</ref><ref name="pmid11069618">{{cite journal | vauthors = Kanno T, Kawada A, Yamanouchi J, Yosida-Noro C, Yoshiki A, Shiraiwa M, Kusakabe M, Manabe M, Tezuka T, Takahara H | title = Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin | journal = The Journal of Investigative Dermatology | volume = 115 | issue = 5 | pages = 813–23 |date=November 2000 | pmid = 11069618 | doi = 10.1046/j.1523-1747.2000.00131.x | url = }}</ref>
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This gene encodes a member of the [[Protein-arginine deiminase|peptidyl arginine deiminase]] family of enzymes, which catalyze the post-translational [[citrullination|deimination]] of proteins by converting [[arginine]] residues into [[citrulline]]s in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type III enzyme modulates hair structural proteins, such as [[filaggrin]] in the [[hair follicle]] and [[TCHH|trichohyalin]] in the inner root sheath, during hair follicle formation. Together with the type I enzyme, this enzyme may also play a role in terminal differentiation of the [[Epidermis (zoology)|epidermis]]. This gene exists in a cluster with four other [[Homology (biology)#Paralogy|paralogous]] genes.<ref name="entrez" />
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Peptidyl arginine deiminase, type III
| HGNCid = 18337
| Symbol = PADI3
| AltSymbols =; MGC126307; MGC126308; PAD3; PDI3
| OMIM = 606755
| ECnumber = 
| Homologene = 7882
| MGIid = 1338891
| GeneAtlas_image1 = PBB_GE_PADI3_220779_at_tn.png
| Function = {{GNF_GO|id=GO:0004668 |text = protein-arginine deiminase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 51702
    | Hs_Ensembl = ENSG00000142619
    | Hs_RefseqProtein = NP_057317
    | Hs_RefseqmRNA = NM_016233
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 17448180
    | Hs_GenLoc_end = 17483315
    | Hs_Uniprot = Q9ULW8
    | Mm_EntrezGene = 18601
    | Mm_Ensembl = ENSMUSG00000025328
    | Mm_RefseqmRNA = NM_011060
    | Mm_RefseqProtein = NP_035190
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 140057445
    | Mm_GenLoc_end = 140082724
    | Mm_Uniprot = Q5DTJ8
  }}
}}
'''Peptidyl arginine deiminase, type III''', also known as '''PADI3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PADI3 peptidyl arginine deiminase, type III| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51702| accessdate = }}</ref>


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==See also==
{{PBB_Summary
*[[Protein-arginine deiminase]]
| section_title =  
| summary_text = This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type III enzyme modulates hair structural proteins, such as filaggrin in the hair follicle and trichohyalin in the inner root sheath, during hair follicle formation. Together with the type I enzyme, this enzyme may also play a role in terminal differentiation of the epidermis. This gene exists in a cluster with four other paralogous genes.<ref name="entrez">{{cite web | title = Entrez Gene: PADI3 peptidyl arginine deiminase, type III| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51702| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Vossenaar ER, Zendman AJ, van Venrooij WJ, Pruijn GJ |title=PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. |journal=Bioessays |volume=25 |issue= 11 |pages= 1106-18 |year= 2004 |pmid= 14579251 |doi= 10.1002/bies.10357 }}
*{{cite journal  | vauthors=Vossenaar ER, Zendman AJ, van Venrooij WJ, Pruijn GJ |title=PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. |journal=BioEssays |volume=25 |issue= 11 |pages= 1106–18 |year= 2004 |pmid= 14579251 |doi= 10.1002/bies.10357 }}
*{{cite journal | author=Chavanas S, Méchin MC, Nachat R, ''et al.'' |title=Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis. |journal=J. Dermatol. Sci. |volume=44 |issue= 2 |pages= 63-72 |year= 2006 |pmid= 16973334 |doi= 10.1016/j.jdermsci.2006.07.004 }}
*{{cite journal   |vauthors=Chavanas S, Méchin MC, Nachat R, etal |title=Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis. |journal=J. Dermatol. Sci. |volume=44 |issue= 2 |pages= 63–72 |year= 2006 |pmid= 16973334 |doi= 10.1016/j.jdermsci.2006.07.004 }}
*{{cite journal | author=Rus'd AA, Ikejiri Y, Ono H, ''et al.'' |title=Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse. |journal=Eur. J. Biochem. |volume=259 |issue= 3 |pages= 660-9 |year= 1999 |pmid= 10092850 |doi=  }}
*{{cite journal   |vauthors=Rus'd AA, Ikejiri Y, Ono H, etal |title=Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse. |journal=Eur. J. Biochem. |volume=259 |issue= 3 |pages= 660–9 |year= 1999 |pmid= 10092850 |doi=10.1046/j.1432-1327.1999.00083.x }}
*{{cite journal | author=Kanno T, Kawada A, Yamanouchi J, ''et al.'' |title=Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin. |journal=J. Invest. Dermatol. |volume=115 |issue= 5 |pages= 813-23 |year= 2000 |pmid= 11069618 |doi= 10.1046/j.1523-1747.2000.00131.x }}
*{{cite journal   |vauthors=Kanno T, Kawada A, Yamanouchi J, etal |title=Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin. |journal=J. Invest. Dermatol. |volume=115 |issue= 5 |pages= 813–23 |year= 2000 |pmid= 11069618 |doi= 10.1046/j.1523-1747.2000.00131.x }}
*{{cite journal | author=Venter JC, Adams MD, Myers EW, ''et al.'' |title=The sequence of the human genome. |journal=Science |volume=291 |issue= 5507 |pages= 1304-51 |year= 2001 |pmid= 11181995 |doi= 10.1126/science.1058040 }}
*{{cite journal   |vauthors=Venter JC, Adams MD, Myers EW, etal |title=The sequence of the human genome. |journal=Science |volume=291 |issue= 5507 |pages= 1304–51 |year= 2001 |pmid= 11181995 |doi= 10.1126/science.1058040 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Chavanas S, Méchin MC, Takahara H, ''et al.'' |title=Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. |journal=Gene |volume=330 |issue=  |pages= 19-27 |year= 2004 |pmid= 15087120 |doi= 10.1016/j.gene.2003.12.038 }}
*{{cite journal   |vauthors=Chavanas S, Méchin MC, Takahara H, etal |title=Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. |journal=Gene |volume=330 |issue=  |pages= 19–27 |year= 2004 |pmid= 15087120 |doi= 10.1016/j.gene.2003.12.038 }}
*{{cite journal  | author=Iida A, Nakamura Y |title=Identification of 45 novel SNPs in the 83-kb region containing peptidylarginine deiminase types 1 and 3 loci on chromosomal band 1p36.13. |journal=J. Hum. Genet. |volume=49 |issue= 7 |pages= 387-90 |year= 2004 |pmid= 15150696 |doi= 10.1007/s10038-004-0156-1 }}
*{{cite journal  | vauthors=Iida A, Nakamura Y |title=Identification of 45 novel SNPs in the 83-kb region containing peptidylarginine deiminase types 1 and 3 loci on chromosomal band 1p36.13. |journal=J. Hum. Genet. |volume=49 |issue= 7 |pages= 387–90 |year= 2004 |pmid= 15150696 |doi= 10.1007/s10038-004-0156-1 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Nachat R, Méchin MC, Takahara H, ''et al.'' |title=Peptidylarginine deiminase isoforms 1-3 are expressed in the epidermis and involved in the deimination of K1 and filaggrin. |journal=J. Invest. Dermatol. |volume=124 |issue= 2 |pages= 384-93 |year= 2005 |pmid= 15675958 |doi= 10.1111/j.0022-202X.2004.23568.x }}
*{{cite journal   |vauthors=Nachat R, Méchin MC, Takahara H, etal |title=Peptidylarginine deiminase isoforms 1-3 are expressed in the epidermis and involved in the deimination of K1 and filaggrin. |journal=J. Invest. Dermatol. |volume=124 |issue= 2 |pages= 384–93 |year= 2005 |pmid= 15675958 |doi= 10.1111/j.0022-202X.2004.23568.x }}
*{{cite journal | author=Méchin MC, Enji M, Nachat R, ''et al.'' |title=The peptidylarginine deiminases expressed in human epidermis differ in their substrate specificities and subcellular locations. |journal=Cell. Mol. Life Sci. |volume=62 |issue= 17 |pages= 1984-95 |year= 2005 |pmid= 16091842 |doi= 10.1007/s00018-005-5196-y }}
*{{cite journal   |vauthors=Méchin MC, Enji M, Nachat R, etal |title=The peptidylarginine deiminases expressed in human epidermis differ in their substrate specificities and subcellular locations. |journal=Cell. Mol. Life Sci. |volume=62 |issue= 17 |pages= 1984–95 |year= 2005 |pmid= 16091842 |doi= 10.1007/s00018-005-5196-y }}
*{{cite journal | author=Dong S, Kanno T, Yamaki A, ''et al.'' |title=NF-Y and Sp1/Sp3 are involved in the transcriptional regulation of the peptidylarginine deiminase type III gene (PADI3) in human keratinocytes. |journal=Biochem. J. |volume=397 |issue= 3 |pages= 449-59 |year= 2006 |pmid= 16671893 |doi= 10.1042/BJ20051939 }}
*{{cite journal   |vauthors=Dong S, Kanno T, Yamaki A, etal |title=NF-Y and Sp1/Sp3 are involved in the transcriptional regulation of the peptidylarginine deiminase type III gene (PADI3) in human keratinocytes. |journal=Biochem. J. |volume=397 |issue= 3 |pages= 449–59 |year= 2006 |pmid= 16671893 |doi= 10.1042/BJ20051939 | pmc=1533312 }}
*{{cite journal | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
*{{cite journal   |vauthors=Gregory SG, Barlow KF, McLay KE, etal |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
}}
}}
{{refend}}
{{refend}}


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{{Carbon-nitrogen non-peptide hydrolases}}
 
 
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Latest revision as of 17:29, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Peptidyl arginine deiminase, type III, also known as PADI3, is a protein which in humans is encoded by the PADI3 gene.[1][2]

This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type III enzyme modulates hair structural proteins, such as filaggrin in the hair follicle and trichohyalin in the inner root sheath, during hair follicle formation. Together with the type I enzyme, this enzyme may also play a role in terminal differentiation of the epidermis. This gene exists in a cluster with four other paralogous genes.[1]

See also

References

  1. ↑ 1.0 1.1 "Entrez Gene: PADI3 peptidyl arginine deiminase, type III".
  2. ↑ Kanno T, Kawada A, Yamanouchi J, Yosida-Noro C, Yoshiki A, Shiraiwa M, Kusakabe M, Manabe M, Tezuka T, Takahara H (November 2000). "Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin". The Journal of Investigative Dermatology. 115 (5): 813–23. doi:10.1046/j.1523-1747.2000.00131.x. PMID 11069618.

Further reading



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