ID   PADI3_MOUSE             Reviewed;         664 AA.
AC   Q9Z184; A2AMU4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 140.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Epidermis;
RX   PubMed=10092850; DOI=10.1046/j.1432-1327.1999.00083.x;
RA   Rusd A.A., Ikejiri Y., Ono H., Yonekawa T., Shiraiwa M., Kawada A.,
RA   Takahara H.;
RT   "Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I,
RT   type III and type IV, and the expression pattern of type I in mouse.";
RL   Eur. J. Biochem. 259:660-669(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   CHARACTERIZATION, AND TISSUE SPECIFICITY.
RX   PubMed=1778991; DOI=10.1093/oxfordjournals.jbchem.a123636;
RA   Terakawa H., Takahara H., Sugawara K.;
RT   "Three types of mouse peptidylarginine deiminase: characterization and
RT   tissue distribution.";
RL   J. Biochem. 110:661-666(1991).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=27866708; DOI=10.1016/j.ajhg.2016.10.004;
RA   Ue Basmanav F.B., Cau L., Tafazzoli A., Mechin M.C., Wolf S., Romano M.T.,
RA   Valentin F., Wiegmann H., Huchenq A., Kandil R., Garcia Bartels N.,
RA   Kilic A., George S., Ralser D.J., Bergner S., Ferguson D.J.,
RA   Oprisoreanu A.M., Wehner M., Thiele H., Altmueller J., Nuernberg P.,
RA   Swan D., Houniet D., Buechner A., Weibel L., Wagner N., Grimalt R.,
RA   Bygum A., Serre G., Blume-Peytavi U., Sprecher E., Schoch S., Oji V.,
RA   Hamm H., Farrant P., Simon M., Betz R.C.;
RT   "Mutations in three genes encoding proteins involved in hair shaft
RT   formation cause uncombable hair syndrome.";
RL   Am. J. Hum. Genet. 99:1292-1304(2016).
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       {ECO:0000269|PubMed:1778991}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. The skin of 7-week-old null
CC       mice appeared normal, but scanning electron microscopy revealed
CC       structural alterations in the whiskers and hair coat morphology
CC       (PubMed:27866708). {ECO:0000269|PubMed:27866708}.
CC   -!- SIMILARITY: Belongs to the protein arginine deiminase family.
CC       {ECO:0000305}.
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DR   EMBL; AB013849; BAA34182.1; -; mRNA.
DR   EMBL; AL807805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS18855.1; -.
DR   RefSeq; NP_035190.3; NM_011060.4.
DR   AlphaFoldDB; Q9Z184; -.
DR   SMR; Q9Z184; -.
DR   STRING; 10090.ENSMUSP00000026377; -.
DR   iPTMnet; Q9Z184; -.
DR   PhosphoSitePlus; Q9Z184; -.
DR   MaxQB; Q9Z184; -.
DR   PaxDb; 10090-ENSMUSP00000026377; -.
DR   ProteomicsDB; 287935; -.
DR   Antibodypedia; 29341; 114 antibodies from 17 providers.
DR   DNASU; 18601; -.
DR   Ensembl; ENSMUST00000026377.9; ENSMUSP00000026377.3; ENSMUSG00000025328.10.
DR   GeneID; 18601; -.
DR   KEGG; mmu:18601; -.
DR   UCSC; uc008vng.1; mouse.
DR   AGR; MGI:1338891; -.
DR   CTD; 51702; -.
DR   MGI; MGI:1338891; Padi3.
DR   VEuPathDB; HostDB:ENSMUSG00000025328; -.
DR   eggNOG; ENOG502QVJA; Eukaryota.
DR   GeneTree; ENSGT00940000153217; -.
DR   HOGENOM; CLU_021911_0_0_1; -.
DR   InParanoid; Q9Z184; -.
DR   OMA; QKCGHGR; -.
DR   OrthoDB; 3956477at2759; -.
DR   PhylomeDB; Q9Z184; -.
DR   TreeFam; TF331952; -.
DR   Reactome; R-MMU-3247509; Chromatin modifying enzymes.
DR   BioGRID-ORCS; 18601; 0 hits in 81 CRISPR screens.
DR   PRO; PR:Q9Z184; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9Z184; Protein.
DR   Bgee; ENSMUSG00000025328; Expressed in lip and 33 other cell types or tissues.
DR   ExpressionAtlas; Q9Z184; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:MGI.
DR   GO; GO:0004668; F:protein-arginine deiminase activity; ISS:UniProtKB.
DR   CDD; cd04214; PAD_N; 1.
DR   Gene3D; 2.60.40.1700; Protein-arginine deiminase, central domain; 1.
DR   Gene3D; 2.60.40.1860; Protein-arginine deiminase, N-terminal domain; 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; PEPTIDYLARGININE DEIMINASE; 1.
DR   PANTHER; PTHR10837:SF21; PROTEIN-ARGININE DEIMINASE TYPE-3; 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; SSF49503; Cupredoxins; 1.
DR   SUPFAM; SSF55909; Pentein; 1.
DR   SUPFAM; SSF110083; Peptidylarginine deiminase Pad4, middle domain; 1.
DR   Genevisible; Q9Z184; MM.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..664
FT                   /note="Protein-arginine deiminase type-3"
FT                   /id="PRO_0000220030"
FT   CONFLICT        32
FT                   /note="A -> S (in Ref. 1; BAA34182)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="V -> L (in Ref. 1; BAA34182)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59
FT                   /note="S -> N (in Ref. 1; BAA34182)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79
FT                   /note="I -> V (in Ref. 1; BAA34182)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="S -> A (in Ref. 1; BAA34182)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   664 AA;  75073 MW;  FA6E065DF5D9CB83 CRC64;
     MSLQRIVRVS LEHPTSAVCV AGVETIVDIY GAVPEGTDMF EVYGTPGVDI YVSPSMERSR
     ERADTRRWCF NKGLEIIVIM NSPSNDLNDS HVQIAYHSSR EHLPLAYAVL YLTCVDITLD
     CDMNCADRQD RSFVDKRQWV WGPDGYGAIL LVNCDRDNVD SNAQDNCDQY VRCLQDLEDM
     SVMVLRTQGP EALFEDHRLI LHTSSCDAER ARVFHVCGPE DSCESYKCVL GPDRMSYEVP
     RLKGYEERFF VEGLSFPDAG FPGLISFHVT LLDDSNEDFS ETPIFTDTAV FRVAPWIMTP
     STLPPLEVYV CRVRNNTCFV EAVEELARKA GCKLTICPQA ENRNDRWIQD EMELGYVQAP
     HKTLPVVFDS PRNGELQGFP YKRILGLDFG YVTREPKDSS VSGLDSFGNL EVSPPVVANG
     KEYPLGRILI GGNLPGSRGR RVTQVVRNFL HAQKVQPLVE LFVDWLAVGH VDEFLSFVPA
     PDGKGFRLLL ASPGACFRLF QEKQKWGHGR SLLFEGVIGD RRVQTVSINQ ILNNQSLINF
     NKFAQSCIDW NREVLKRELG LAEGDIIDIP QLFKTEKRKA VAFFPDLVNM LVLGKHLGIP
     KPFGPIINGR CCLEEKVRSL LEPLGLHCTF IDDFTPYHML HGEVHCGTNV RREPFAFKWW
     HMVP
//