PADI1_MOUSE
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 03-AUG-2022, entry version 150.
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; Q9Z185; -.
DR PRIDE; Q9Z185; -.
DR ProteomicsDB; 294101; -.
DR Antibodypedia; 14640; 89 antibodies from 16 providers.
DR DNASU; 18599; -.
DR Ensembl; ENSMUST00000026378; ENSMUSP00000026378; ENSMUSG00000025329.
DR GeneID; 18599; -.
DR KEGG; mmu:18599; -.
DR UCSC; uc008vnh.1; mouse.
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; VQKCIDW; -.
DR OrthoDB; 787070at2759; -.
DR PhylomeDB; Q9Z185; -.
DR TreeFam; TF331952; -.
DR Reactome; R-MMU-3247509; Chromatin modifying enzymes.
DR BioGRID-ORCS; 18599; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q9Z185; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9Z185; protein.
DR Bgee; ENSMUSG00000025329; Expressed in uterine cervix and 33 other tissues.
DR ExpressionAtlas; Q9Z185; baseline and differential.
DR Genevisible; Q9Z185; MM.
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 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; 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
