Protein-arginine deiminase type-1

From Cysteinome
Jump to: navigation, search
Basic Information
Short Name PADI1, PDI1
UNP ID Q9ULC6
Organism Homo sapiens
Cys Site Cys645
Family/Domain Protein arginine deiminase family
Known Ligand Ligand list
Function Type Metabolic enzyme

Summary

Protein Function

Peptidyl arginine deiminase, type I, also known as PADI1, is a protein which in humans is encoded by the PADI1 gene. 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. (From Wikipedia)

Cys Function & Property

Cys645 is the active site of PADI1.

554 556-function.png
Alignment of PADIs' sequences

  • Hydrophobic property:
554-hydro.png
  • SASA:
Cys645: Unknown

Protein Sequence

MAPKRVVQLS LKMPTHAVCV VGVEAHVDIH SDVPKGANSF RVSGSSGVEV
FMVYNRTRVK EPIGKARWPL DTDADMVVSV GTASKELKDF KVRVSYFGEQ
EDQALGRSVL YLTGVDISLE VDTGRTGKVK RSQGDKKTWR WGPEGYGAIL
LVNCDRDNHR SAEPDLTHSW LMSLADLQDM SPMLLSCNGP DKLFDSHKLV
LNVPFSDSKR VRVFCARGGN SLSDYKQVLG PQCLSYEVER QPGEQEIKFY
VEGLTFPDAD FLGLVSLSVS LVDPGTLPEV TLFTDTVGFR MAPWIMTPNT
QPPEELYVCR VMDTHGSNEK FLEDMSYLTL KANCKLTICP QVENRNDRWI
QDEMEFGYIE APHKSFPVVF DSPRNRGLKD FPYKRILGPD FGYVTREIPL
PGPSSLDSFG NLDVSPPVTV GGTEYPLGRI LIGSSFPKSG GRQMARAVRN
FLKAQQVQAP VELYSDWLSV GHVDEFLTFV PTSDQKGFRL LLASPSACLK
LFQEKKEEGY GEAAQFDGLK HQAKRSINEM LADRHLQRDN LHAQKCIDWN
RNVLKRELGL AESDIVDIPQ LFFLKNFYAE AFFPDMVNMV VLGKYLGIPK
PYGPIINGRC CLEEKVQSLL EPLGLHCIFI DDYLSYHELQ GEIHCGTNVR
RKPFPFKWWN MVP

Structural Information

  • Known structure with covalent ligand:
Unknown
  • Protein structure:
Unknown

Related Pathway

Unknown

Experimental Evidence

Homologous Analysis Of Sequence, Molecular Docking, Cys-directed Mutation, MS

Reference

  1. Bello A M, Wasilewski E, Wei L, et al. Interrogation of the active sites of protein arginine deiminases (PAD1,-2, and-4) using designer probes[J]. ACS medicinal chemistry letters, 2013, 4(2): 249-253. 24900657
  2. Jones J E, Slack J L, Fang P, et al. Synthesis and screening of a haloacetamidine containing library to identify PAD4 selective inhibitors[J]. ACS chemical biology, 2011, 7(1): 160-165. 22004374