ID   PADI3_RAT               Reviewed;         664 AA.
AC   P70708;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Protein-arginine deiminase type-3;
DE            EC=3.5.3.15 {ECO:0000250|UniProtKB:Q9ULW8};
DE   AltName: Full=Peptidylarginine deiminase III;
DE   AltName: Full=Protein-arginine deiminase type III;
GN   Name=Padi3; Synonyms=Pad3, Pdi3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Epidermis;
RX   PubMed=9192727; DOI=10.1093/oxfordjournals.jbchem.a021667;
RA   Nishijyo T., Kawada A., Kanno T., Shiraiwa M., Takahara H.;
RT   "Isolation and molecular cloning of epidermal- and hair follicle-specific
RT   peptidylarginine deiminase (type III) from rat.";
RL   J. Biochem. 121:868-875(1997).
CC   -!- FUNCTION: Catalyzes the deimination of arginine residues of proteins.
CC       {ECO:0000250|UniProtKB:Q9ULW8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4(+);
CC         Xref=Rhea:RHEA:18089, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:10588,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29965,
CC         ChEBI:CHEBI:83397; EC=3.5.3.15;
CC         Evidence={ECO:0000250|UniProtKB:Q9ULW8};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ULW8}.
CC   -!- TISSUE SPECIFICITY: Epidermis and hair follicles.
CC   -!- SIMILARITY: Belongs to the protein arginine deiminase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D88034; BAA13532.1; -; mRNA.
DR   PIR; JC5440; JC5440.
DR   RefSeq; NP_058926.1; NM_017230.2.
DR   AlphaFoldDB; P70708; -.
DR   SMR; P70708; -.
DR   STRING; 10116.ENSRNOP00000009230; -.
DR   iPTMnet; P70708; -.
DR   PhosphoSitePlus; P70708; -.
DR   PaxDb; P70708; -.
DR   PRIDE; P70708; -.
DR   GeneID; 29520; -.
DR   KEGG; rno:29520; -.
DR   UCSC; RGD:3289; rat.
DR   CTD; 51702; -.
DR   RGD; 3289; Padi3.
DR   eggNOG; ENOG502QVJA; Eukaryota.
DR   InParanoid; P70708; -.
DR   OrthoDB; 787070at2759; -.
DR   PhylomeDB; P70708; -.
DR   BRENDA; 3.5.3.15; 5301.
DR   Reactome; R-RNO-3247509; Chromatin modifying enzymes.
DR   PRO; PR:P70708; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0004668; F:protein-arginine deiminase activity; IDA:UniProtKB.
DR   GO; GO:0019546; P:arginine deiminase pathway; NAS:RGD.
DR   GO; GO:0036414; P:histone citrullination; IBA:GO_Central.
DR   GO; GO:0018101; P:protein citrullination; ISO:RGD.
DR   Gene3D; 2.60.40.1700; -; 1.
DR   Gene3D; 2.60.40.1860; -; 1.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR004303; PAD.
DR   InterPro; IPR013530; PAD_C.
DR   InterPro; IPR036556; PAD_central_sf.
DR   InterPro; IPR013732; PAD_N.
DR   InterPro; IPR038685; PAD_N_sf.
DR   InterPro; IPR013733; Prot_Arg_deaminase_cen_dom.
DR   PANTHER; PTHR10837; PTHR10837; 1.
DR   Pfam; PF03068; PAD; 1.
DR   Pfam; PF08527; PAD_M; 1.
DR   Pfam; PF08526; PAD_N; 1.
DR   PIRSF; PIRSF001247; Protein-arginine_deiminase; 1.
DR   SUPFAM; SSF110083; SSF110083; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..664
FT                   /note="Protein-arginine deiminase type-3"
FT                   /id="PRO_0000220031"
SQ   SEQUENCE   664 AA;  75038 MW;  E5E6DDBCFADC66F3 CRC64;
     MSLQRTVRVS LEHPTSAVCV AGVETIVDIY GSVPEGTDMF EVYGTPGVDI YVSPSMERNR
     ERADTRRWCF NKGLEIIVVM NSPSNDLNDS HVQIAYHSSH EHLPLAYAVL YLTCVDITLD
     CDMNCADRQD RSFVDKRQWM WGPDGYGAIL LVNCDRDEVS SDAQDNCDQC VRCLQDLEDM
     SVMVLRTQGP ESLFDDHRLI LHTSSCDAER ARVFHVCGPE DSCEAYRCVL GPDRMSYEVP
     RLKGYEERFY VEGLSFPDAG FPGILSFHIT LLDDSNEDYS ETPIFTDTVV FRVAPWIMTP
     STLPPLEVYV CQVRNNTCFV EAVEELARKA GCKLTICPQA ENRNDRWIQD EMELGYTQAP
     HKTLPVVFDS PRNGELQGFP YKRILGLDFG YVTREPPDSS VSGLDSFGNL EVSPPVVANG
     KEYPLGRILI GGNLPGSRGR RVTQVVRDFL HAQKVQPLVE LFVDWLAVGH VDEFLSFVPA
     PDGKGFRLLL ASPGACFRLF QEKQKWGHGR SLLFEGVIGD RRVQTISINQ VLSNQSLINF
     NKFAQSCIDW NREVLKRELG LGESDIIDIP QLFKSEKRKA VAFFPDLVNM LVLGKHLGIP
     KPFGPIINGR CCLEEKVRSL LEPLGLHCTF IDDFTPYHML HGEVHCGTNV RREPFAFKWW
     HMVP