ID   PADI1_MOUSE             Reviewed;         662 AA.
AC   Q9Z185;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=Protein-arginine deiminase type-1;
DE            EC=3.5.3.15 {ECO:0000250|UniProtKB:Q9ULC6};
DE   AltName: Full=Peptidylarginine deiminase I;
DE   AltName: Full=Protein-arginine deiminase type I;
GN   Name=Padi1; Synonyms=Pad1, Pdi1;
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, and Uterus;
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 [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=15087120; DOI=10.1016/j.gene.2003.12.038;
RA   Chavanas S., Mechin M.-C., Takahara H., Kawada A., Nachat R., Serre G.,
RA   Simon M.;
RT   "Comparative analysis of the mouse and human peptidylarginine deiminase
RT   gene clusters reveals highly conserved non-coding segments and a new human
RT   gene, PADI6.";
RL   Gene 330:19-27(2004).
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).
CC   -!- FUNCTION: Catalyzes the deimination of arginine residues of proteins.
CC       {ECO:0000250|UniProtKB:Q9ULC6}.
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:Q9ULC6};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9ULC6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ULC6}.
CC   -!- TISSUE SPECIFICITY: Expressed only in the epidermis and uterus.
CC       {ECO:0000269|PubMed:1778991}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during the estrus cycle. Expression is
CC       maximum at proestrus and moderate at estrus. Not expressed in diestrus
CC       and metaestrus phases.
CC   -!- INDUCTION: By estrogen.
CC   -!- SIMILARITY: Belongs to the protein arginine deiminase family.
CC       {ECO:0000305}.
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DR   EMBL; AB013848; BAA34181.1; -; mRNA.
DR   EMBL; AB121692; BAD16625.1; -; Genomic_DNA.
DR   CCDS; CCDS18856.1; -.
DR   PIR; PH0203; PH0203.
DR   RefSeq; NP_035189.1; NM_011059.2.
DR   AlphaFoldDB; Q9Z185; -.
DR   SMR; Q9Z185; -.
DR   STRING; 10090.ENSMUSP00000026378; -.
DR   PhosphoSitePlus; Q9Z185; -.
DR   MaxQB; Q9Z185; -.
DR   PaxDb; 10090-ENSMUSP00000026378; -.
DR   ProteomicsDB; 294101; -.
DR   Antibodypedia; 14640; 104 antibodies from 16 providers.
DR   DNASU; 18599; -.
DR   Ensembl; ENSMUST00000026378.4; ENSMUSP00000026378.4; ENSMUSG00000025329.4.
DR   GeneID; 18599; -.
DR   KEGG; mmu:18599; -.
DR   UCSC; uc008vnh.1; mouse.
DR   AGR; MGI:1338893; -.
DR   CTD; 29943; -.
DR   MGI; MGI:1338893; Padi1.
DR   VEuPathDB; HostDB:ENSMUSG00000025329; -.
DR   eggNOG; ENOG502QVJA; Eukaryota.
DR   GeneTree; ENSGT00940000153217; -.
DR   HOGENOM; CLU_021911_0_0_1; -.
DR   InParanoid; Q9Z185; -.
DR   OMA; VEVFMVY; -.
DR   OrthoDB; 3956477at2759; -.
DR   PhylomeDB; Q9Z185; -.
DR   TreeFam; TF331952; -.
DR   Reactome; R-MMU-3247509; Chromatin modifying enzymes.
DR   BioGRID-ORCS; 18599; 4 hits in 80 CRISPR screens.
DR   PRO; PR:Q9Z185; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9Z185; Protein.
DR   Bgee; ENSMUSG00000025329; Expressed in uterine cervix and 34 other cell types or tissues.
DR   ExpressionAtlas; Q9Z185; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; 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; ISS:UniProtKB.
DR   GO; GO:0004668; F:protein-arginine deiminase activity; ISS:UniProtKB.
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:SF11; PROTEIN-ARGININE DEIMINASE TYPE-1; 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; Q9Z185; MM.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..662
FT                   /note="Protein-arginine deiminase type-1"
FT                   /id="PRO_0000220024"
FT   ACT_SITE        644
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT   BINDING         153
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         155
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         155
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         157
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         157
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         164
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         175
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         178
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         178
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         350
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         352
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         363
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         370
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         371
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         374
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         408
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
FT   BINDING         411
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULC6"
SQ   SEQUENCE   662 AA;  73824 MW;  F9A6C7DFF1031D8A CRC64;
     MASPRAVQLS LRKPTHAVCV VGVETLVNVY SDVPKGAKTF GVSGSSEVKI YMVYDPSRVA
     EPAGWAHWPL DANVDVVVVA DTVSKDLYDF KVKVSYFESQ EAAALAHSVL YLTAVDVSLD
     VDTGRTGKVK KGSGDKKTWR WGPGGSGAIL LVNCDRDIHG SREDLHANHL KSLEDLQDMS
     PMVLSCGGPD ELFESHKLVL KASLSDSRRL KVFCARGGTS LSNYKQVLGP RHSSYEVERH
     SGERAIQFYV EGLAFPDASF SGLLSLSVSL VDTRPLSEVS VFTDSVTFRV APWIMTPNTQ
     PPLELYVCSV TDIHGRNDKF LEDMSHLATK ANCKLVVCPR AENRNDRWIQ DELEFGYIDA
     PHKSFPVVFD SPRNRGLRDF ALKRILGPDF GYVTREIEFA GASGLDSFGN LDVSPPVRVG
     NTDYPLGRIL IGGSFPKPSG RRMARVVRDF LQAQQVQSPV ELYSDWLSVG HVDEFLSFVP
     TSDQKGFRLL LASPSACLQL FQEKKEEGYG EAEQFDGLKH KAKRSINDIL ADKHLRRDSA
     HVQKCIDWNR EVLKRELGLS ESDIVDIPQL FFLKGAYAEA FFPDMVNMVV LGKYLGIPKP
     FGPLINGRCC LEEKVRSLLE PLGLRCVFID DFLFYHQLLG EIHCGTNVRR KPFTFKWWNS
     VP
//