ID   PADI3_SHEEP             Reviewed;         664 AA.
AC   O02849;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=PAD, PAD3, PDI3;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 198-221 AND 616-639.
RC   TISSUE=Wool follicle;
RX   PubMed=9129218; DOI=10.1111/1523-1747.ep12292083;
RA   Rogers G., Winter B., McLaughlan C., Powell B., Nesci T.;
RT   "Peptidylarginine deiminase of the hair follicle: characterization,
RT   localisation, and function in keratinising tissues.";
RL   J. Invest. Dermatol. 108:700-707(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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ULW8}.
CC   -!- TISSUE SPECIFICITY: Found in wool follicles, keratinizing epithelia of
CC       the ruminal mucosa, embryonic hoof and tongue filiform papillae.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the protein arginine deiminase family.
CC       {ECO:0000305}.
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DR   EMBL; U85264; AAB53205.1; -; mRNA.
DR   RefSeq; NP_001009791.1; NM_001009791.1.
DR   AlphaFoldDB; O02849; -.
DR   SMR; O02849; -.
DR   STRING; 9940.ENSOARP00000011833; -.
DR   PRIDE; O02849; -.
DR   GeneID; 443369; -.
DR   KEGG; oas:443369; -.
DR   CTD; 51702; -.
DR   eggNOG; ENOG502QVJA; Eukaryota.
DR   OrthoDB; 787070at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004668; F:protein-arginine deiminase activity; ISS:UniProtKB.
DR   GO; GO:0018101; P:protein citrullination; IEA:InterPro.
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   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..664
FT                   /note="Protein-arginine deiminase type-3"
FT                   /id="PRO_0000220032"
SQ   SEQUENCE   664 AA;  74747 MW;  8FB88CE04AD0E5C1 CRC64;
     MSLQRIVRVS LEHPTSAVCV AGVETLVDVY GSVPEGTEMF EVYGTPGVDV YICPSVERDR
     ERAVARRWHF DMGSQIVVVM NSPSNVNDTV TFKFPTIPAE TPRPLAYAVL YLTCVDITLD
     CDLNCEGRQD RDFVDKLQWV WGPSGHGAVL LVNCDRDSMS SNDQEHCDHH VRCLQDLEDM
     SVMILRTQGP DALFDDHKLV LHTSRADAER ARVFHACGPE DSCEAYRHVL GQNKVSYEVP
     RFHGEEERFF VEGLSFPDAG FSGLVTFHVT LLDDSNEDFS ESPIFTDTVV FRVAPWIMTP
     STQPPLEVYV CRVRNNTCFV DAVAELARRA GCKLTVCPQA ENRNDRWIQD EMELGYIQAP
     HKTFPVVFDS PRNGELQNFP YKRILGPDFG YATREPRDNS VSGLDSFGNL EVSPPVVANG
     KEYPLGRILF GGNLPGSRGR RVTQVVRDFL HAQKVQPPVE LFVDWLAVGH VDECLSFVPA
     TDGKGFRMPL ASPSACFKLF QEKQKWGHGG ALLFQGVIGN QQVNTVSISQ VLSNGSLIGY
     NKFVQSCIDW NREVLKRELG LAERDIVDIP QLFKMERRKA VAFFPDLVNM LVLGKHLGIP
     KPFGPVINGR CCLEEKVRSL LEPLGLRCTF IDDFTPYHML HGEVHCGTNV RRQPFSFKWW
     CMEP