PADI3_MOUSE
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 03-AUG-2022, entry version 132.
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; Q9Z184; -.
DR PRIDE; Q9Z184; -.
DR ProteomicsDB; 287935; -.
DR Antibodypedia; 29341; 97 antibodies from 16 providers.
DR DNASU; 18601; -.
DR Ensembl; ENSMUST00000026377; ENSMUSP00000026377; ENSMUSG00000025328.
DR GeneID; 18601; -.
DR KEGG; mmu:18601; -.
DR UCSC; uc008vng.1; mouse.
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; RDNCDQH; -.
DR OrthoDB; 787070at2759; -.
DR PhylomeDB; Q9Z184; -.
DR TreeFam; TF331952; -.
DR Reactome; R-MMU-3247509; Chromatin modifying enzymes.
DR BioGRID-ORCS; 18601; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q9Z184; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9Z184; protein.
DR Bgee; ENSMUSG00000025328; Expressed in lip and 31 other tissues.
DR ExpressionAtlas; Q9Z184; baseline and differential.
DR Genevisible; Q9Z184; MM.
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:MGI.
DR GO; GO:0004668; F:protein-arginine deiminase activity; ISS:UniProtKB.
DR GO; GO:0036414; P:histone citrullination; IBA:GO_Central.
DR GO; GO:0018101; P:protein citrullination; ISO:MGI.
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; 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
