Protein-arginine deiminase type-2 (Mus musculus)

Basic Information
Short Name	PADI2, PDI2
UNP ID	Q9ULC6
Organism	Mus musculus
Cys Site	Cys655
Family/Domain	Protein arginine deiminase family
Known Ligand	Ligand list
Function Type	Metabolic enzyme

Summary

Protein Function

Protein-arginine deiminase type-2 is 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 II enzyme is the most widely expressed family member. Known substrates for this enzyme include myelin basic protein in the central nervous system and vimentin in skeletal muscle and macrophages. This enzyme is thought to play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis. This gene exists in a cluster with four other paralogous genes. (From Wikipedia)

Cys Function & Property

Cys655 is the active site of mouse PADI2. And this site is quite conserved in PADIs.

Alignment of PADIs' sequences

• Hydrophobic property:

• SASA：

Cys655: Unknown

Protein Sequence

MQPPIRENML RERTVRLQYG SRVEAVYVLG TQLWTDVYSA APAGAKTFSL
KHSEGVKVEV VRDGEAEEVV TNGKQRWALS PSSTLRLSMA QASTEASSDK
VTVNYYEEEG SAPIDQAGLF LTAIEISLDV DADRDGEVEK NNPKKASWTW
GPEGQGAILL VNCDRDTPWL PKEDCSDEKV YSKQDLQDMS QMILRTKGPD
RLPAGYEIVL YISMSDSDKV GVFYVENPFF GQRYIHILGR QKLYHVVKYT
GGSAELLFFV EGLCFPDESF SGLVSIHVSL LEYMAEGIPL TPIFTDTVMF
RIAPWIMTPN ILPPVSVFVC CMKDNYLFLK EVKNLVEKTN CELKVCFQYM
NRGDRWIQDE IEFGYIEAPH KGFPVVLDSP RDGNLKDFPI KQLLGPDFGY
VTREPLFETV TSLDSFGNLE VSPPVTVNGK EYPLGRILIG SSFPLSGGRR
MTKVVRDFLQ AQQVQAPVEL YSDWLTVGHV DEFMTFIPIP GKKEFRLLMA
STSACYQLFR EKQKAGHGEA VMFKGLGGMS SKRITINKIL SNESLTQENQ
YFQRCLDWNR DILKRELALT EKDIIDLPAL FKMDENHQAR AFFPNMVNMI
VLDKDLGIPK PFGPQVEEEC CLETHVRGLL EPLGLACTFI DDISAYHKFL
GEVHCGTNVR RKPFTFKWWH MVP

Structural Information

• Known structure with covalent ligand:
  

Unknown

• Protein structure:

Homology structure from hPADI2

Related Pathway

Unknown

Experimental Evidence

Homologous Analysis Of Sequence, Molecular Docking

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