PADI1: Difference between revisions

Jump to navigation Jump to search
WikiBot (talk | contribs)
m Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}})
 
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Peptidyl arginine deiminase, type I''', also known as '''PADI1''', is a [[protein]] which in humans is encoded by the ''PADI1'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PADI1 peptidyl arginine deiminase, type I| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29943| accessdate = }}</ref><ref name="pmid12416996">{{cite journal | vauthors = Guerrin M, Ishigami A, Méchin MC, Nachat R, Valmary S, Sebbag M, Simon M, Senshu T, Serre G | title = cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I | journal = The Biochemical Journal | volume = 370 | issue = Pt 1 | pages = 167–74 |date=February 2003 | pmid = 12416996 | pmc = 1223146 | doi = 10.1042/BJ20020870 | url = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a member of the [[peptidylarginine deiminases|peptidyl arginine deiminase]] family of enzymes, which catalyze the post-translational [[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 I enzyme is involved in the late stages of [[Epidermis (skin)|epidermal]] differentiation, where it deiminates [[filaggrin]] and [[keratin 1|keratin K1]], which maintains hydration of the [[stratum corneum]], and hence the cutaneous barrier function. This enzyme may also play a role in [[hair follicle]] formation. 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 I
| HGNCid = 18367
| Symbol = PADI1
| AltSymbols =; PDI; PAD1; HPAD10; PDI1
| OMIM = 607934
| ECnumber = 
| Homologene = 7881
| MGIid = 1338893
| GeneAtlas_image1 = PBB_GE_PADI1_220962_s_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 = 29943
    | Hs_Ensembl = ENSG00000142623
    | Hs_RefseqProtein = NP_037490
    | Hs_RefseqmRNA = NM_013358
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 17404208
    | Hs_GenLoc_end = 17445087
    | Hs_Uniprot = Q9ULC6
    | Mm_EntrezGene = 18599
    | Mm_Ensembl = ENSMUSG00000025329
    | Mm_RefseqmRNA = NM_011059
    | Mm_RefseqProtein = NP_035189
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 140085057
    | Mm_GenLoc_end = 140117854
    | Mm_Uniprot = Q544I4
  }}
}}
'''Peptidyl arginine deiminase, type I''', also known as '''PADI1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PADI1 peptidyl arginine deiminase, type I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29943| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==References==
{{PBB_Summary
{{reflist}}
| 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 I enzyme is involved in the late stages of epidermal differentiation, where it deiminates filaggrin and keratin K1, which maintains hydration of the stratum corneum, and hence the cutaneous barrier function. This enzyme may also play a role in hair follicle formation. This gene exists in a cluster with four other paralogous genes.<ref name="entrez">{{cite web | title = Entrez Gene: PADI1 peptidyl arginine deiminase, type I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29943| accessdate = }}</ref>
}}


==References==
{{reflist|2}}
==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=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Guerrin M, Ishigami A, Méchin MC, ''et al.'' |title=cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I. |journal=Biochem. J. |volume=370 |issue= Pt 1 |pages= 167-74 |year= 2003 |pmid= 12416996 |doi= 10.1042/BJ20020870 }}
*{{cite journal   |vauthors=Guerrin M, Ishigami A, Méchin MC, etal |title=cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I |journal=Biochem. J. |volume=370 |issue= Pt 1 |pages= 167–74 |year= 2003 |pmid= 12416996 |doi= 10.1042/BJ20020870 | pmc=1223146 }}
*{{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=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{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=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=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}}


{{protein-stub}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{WikiDoc Sources}}
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = no
| update_citations = yes
}}
 
 
{{gene-1-stub}}

Latest revision as of 17:29, 7 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

Peptidyl arginine deiminase, type I, also known as PADI1, is a protein which in humans is encoded by the PADI1 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 I enzyme is involved in the late stages of epidermal differentiation, where it deiminates filaggrin and keratin K1, which maintains hydration of the stratum corneum, and hence the cutaneous barrier function. This enzyme may also play a role in hair follicle formation. This gene exists in a cluster with four other paralogous genes.[1]

References

  1. 1.0 1.1 "Entrez Gene: PADI1 peptidyl arginine deiminase, type I".
  2. Guerrin M, Ishigami A, Méchin MC, Nachat R, Valmary S, Sebbag M, Simon M, Senshu T, Serre G (February 2003). "cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I". The Biochemical Journal. 370 (Pt 1): 167–74. doi:10.1042/BJ20020870. PMC 1223146. PMID 12416996.

Further reading