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Q08642 (PADI2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-arginine deiminase type-2

EC=3.5.3.15
Alternative name(s):
Peptidylarginine deiminase II
Protein-arginine deiminase type II
Gene names
Name:Padi2
Synonyms:Pdi, Pdi2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the deimination of arginine residues of proteins.

Catalytic activity

Protein L-arginine + H2O = protein L-citrulline + NH3.

Cofactor

Calcium.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed in various tissues including muscle, uterus, spinal cord, salivary gland and pancreas. Ref.5

Developmental stage

Expressed during the estrus cycle. Expressed during diestrus and proestrus with an eight fold decline when estrus cycle is reached.

Sequence similarities

Belongs to the protein arginine deiminase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCalcium
   Molecular functionHydrolase
   PTMAcetylation
Citrullination
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processprotein citrullination

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

protein-arginine deiminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 673673Protein-arginine deiminase type-2
PRO_0000220027

Amino acid modifications

Modified residue11N-acetylmethionine Ref.1
Modified residue3521Citrulline Ref.1

Experimental info

Sequence conflict6651T → A in BAA04012. Ref.1
Sequence conflict6651T → A in AAH40350. Ref.4
Sequence conflict6651T → A in AAH49947. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q08642 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: F72A36079DA914E0

FASTA67376,250
        10         20         30         40         50         60 
MQPPIRENML RERTVRLQYG SRVEAVYVLG TQLWTDVYSA APAGAKTFSL KHSEGVKVEV 

        70         80         90        100        110        120 
VRDGEAEEVV TNGKQRWALS PSSTLRLSMA QASTEASSDK VTVNYYEEEG SAPIDQAGLF 

       130        140        150        160        170        180 
LTAIEISLDV DADRDGEVEK NNPKKASWTW GPEGQGAILL VNCDRDTPWL PKEDCSDEKV 

       190        200        210        220        230        240 
YSKQDLQDMS QMILRTKGPD RLPAGYEIVL YISMSDSDKV GVFYVENPFF GQRYIHILGR 

       250        260        270        280        290        300 
QKLYHVVKYT GGSAELLFFV EGLCFPDESF SGLVSIHVSL LEYMAEGIPL TPIFTDTVMF 

       310        320        330        340        350        360 
RIAPWIMTPN ILPPVSVFVC CMKDNYLFLK EVKNLVEKTN CELKVCFQYM NRGDRWIQDE 

       370        380        390        400        410        420 
IEFGYIEAPH KGFPVVLDSP RDGNLKDFPI KQLLGPDFGY VTREPLFETV TSLDSFGNLE 

       430        440        450        460        470        480 
VSPPVTVNGK EYPLGRILIG SSFPLSGGRR MTKVVRDFLQ AQQVQAPVEL YSDWLTVGHV 

       490        500        510        520        530        540 
DEFMTFIPIP GKKEFRLLMA STSACYQLFR EKQKAGHGEA VMFKGLGGMS SKRITINKIL 

       550        560        570        580        590        600 
SNESLTQENQ YFQRCLDWNR DILKRELALT EKDIIDLPAL FKMDENHQAR AFFPNMVNMI 

       610        620        630        640        650        660 
VLDKDLGIPK PFGPQVEEEC CLETHVRGLL EPLGLACTFI DDISAYHKFL GEVHCGTNVR 

       670 
RKPFTFKWWH MVP 

« Hide

References

« Hide 'large scale' references
[1]"cDNA nucleotide sequence and primary structure of mouse uterine peptidylarginine deiminase. Detection of a 3'-untranslated nucleotide sequence common to the mRNA of transiently expressed genes and rapid turnover of this enzyme's mRNA in the estrous cycle."
Tsuchida M., Takahara H., Minami N., Arai T., Kobayashi Y., Tsujimoto H., Fukazawa C., Sugawara K.
Eur. J. Biochem. 215:677-685(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT MET-1, CITRULLINATION AT ARG-352, PARTIAL PROTEIN SEQUENCE.
[2]"Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6."
Chavanas S., Mechin M.-C., Takahara H., Kawada A., Nachat R., Serre G., Simon M.
Gene 330:19-27(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland and Salivary gland.
[5]"Three types of mouse peptidylarginine deiminase: characterization and tissue distribution."
Terakawa H., Takahara H., Sugawara K.
J. Biochem. 110:661-666(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D16580 mRNA. Translation: BAA04012.1.
AB121692 Genomic DNA. Translation: BAD16624.1.
AL645625, AL807805 Genomic DNA. Translation: CAM16760.1.
AL807805, AL645625 Genomic DNA. Translation: CAM25735.1.
BC040350 mRNA. Translation: AAH40350.1.
BC049947 mRNA. Translation: AAH49947.1.
CCDSCCDS18857.1.
PIRDIMSR1. S35038.
RefSeqNP_032838.2. NM_008812.2.
UniGeneMm.2296.

3D structure databases

ProteinModelPortalQ08642.
SMRQ08642. Positions 15-673.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202093. 1 interaction.
IntActQ08642. 1 interaction.
MINTMINT-4106481.

Chemistry

ChEMBLCHEMBL2321611.

PTM databases

PhosphoSiteQ08642.

Proteomic databases

MaxQBQ08642.
PaxDbQ08642.
PRIDEQ08642.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030765; ENSMUSP00000030765; ENSMUSG00000028927.
GeneID18600.
KEGGmmu:18600.
UCSCuc008vni.2. mouse.

Organism-specific databases

CTD11240.
MGIMGI:1338892. Padi2.

Phylogenomic databases

eggNOGNOG42085.
GeneTreeENSGT00390000008680.
HOGENOMHOG000220908.
HOVERGENHBG053016.
InParanoidQ75WD0.
KOK01481.
OMACLETHVR.
OrthoDBEOG7P5T09.
TreeFamTF331952.

Enzyme and pathway databases

BRENDA3.5.3.15. 3474.

Gene expression databases

BgeeQ08642.
CleanExMM_PADI2.
GenevestigatorQ08642.

Family and domain databases

InterProIPR008972. Cupredoxin.
IPR004303. PAD.
IPR013530. PAD_C.
IPR013732. PAD_N.
IPR013733. Prot_Arg_deaminase_cen_dom.
IPR016296. Protein-arginine_deiminase_sub.
[Graphical view]
PANTHERPTHR10837. PTHR10837. 1 hit.
PfamPF03068. PAD. 1 hit.
PF08527. PAD_M. 1 hit.
PF08526. PAD_N. 1 hit.
[Graphical view]
PIRSFPIRSF001247. Protein-arginine_deiminase. 1 hit.
SUPFAMSSF110083. SSF110083. 1 hit.
SSF49503. SSF49503. 1 hit.
ProtoNetSearch...

Other

NextBio294502.
PROQ08642.
SOURCESearch...

Entry information

Entry namePADI2_MOUSE
AccessionPrimary (citable) accession number: Q08642
Secondary accession number(s): Q75WD0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot