PADI1_RAT
ID PADI1_RAT Reviewed; 662 AA.
AC O88806;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein-arginine deiminase type-1;
DE EC=3.5.3.15;
DE AltName: Full=PAD-R11 {ECO:0000303|PubMed:9738944};
DE AltName: Full=Peptidylarginine deiminase I;
DE AltName: Full=Protein-arginine deiminase type I;
GN Name=Padi1; Synonyms=Pad1, Pdi1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY
RP RETINOIC ACID.
RX PubMed=9738944; DOI=10.1016/s0014-5793(98)00893-x;
RA Ishigami A., Kuramoto M., Yamada M., Watanabe K., Senshu T.;
RT "Molecular cloning of two novel types of peptidylarginine deiminase cDNAs
RT from retinoic acid-treated culture of a newborn rat keratinocyte cell
RT line.";
RL FEBS Lett. 433:113-118(1998).
CC -!- FUNCTION: Catalyzes the deimination of arginine residues of proteins.
CC {ECO:0000269|PubMed:9738944}.
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:0000269|PubMed:9738944};
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 -!- INDUCTION: Induced by all-trans retinoic acid.
CC {ECO:0000269|PubMed:9738944}.
CC -!- SIMILARITY: Belongs to the protein arginine deiminase family.
CC {ECO:0000305}.
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DR EMBL; AB010998; BAA32099.1; -; mRNA.
DR RefSeq; NP_062205.1; NM_019332.1.
DR AlphaFoldDB; O88806; -.
DR SMR; O88806; -.
DR STRING; 10116.ENSRNOP00000009921; -.
DR PaxDb; O88806; -.
DR PRIDE; O88806; -.
DR GeneID; 54282; -.
DR KEGG; rno:54282; -.
DR UCSC; RGD:3287; rat.
DR CTD; 29943; -.
DR RGD; 3287; Padi1.
DR eggNOG; ENOG502QVJA; Eukaryota.
DR InParanoid; O88806; -.
DR OrthoDB; 787070at2759; -.
DR PhylomeDB; O88806; -.
DR BRENDA; 3.5.3.15; 5301.
DR Reactome; R-RNO-3247509; Chromatin modifying enzymes.
DR PRO; PR:O88806; -.
DR Proteomes; UP000002494; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0004668; F:protein-arginine deiminase activity; IDA:UniProtKB.
DR GO; GO:0036414; P:histone citrullination; IBA:GO_Central.
DR GO; GO:0018101; P:protein citrullination; ISO:RGD.
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_0000220025"
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; 73857 MW; 3A51464C7089D2DF CRC64;
MASQRAVQLS LRKPAHAVCV IGVGTLVDVY SDVPKGAKTF EVSGSSEVKI YMVYDPSRVA
EPAGPAHWPL DANVDVVVVA DTVSKNLHDL KVKVSYFKSQ DTAALAHSLL YLTAVDVSLD
VDTGRTGKVK KGSGDKKNWR WGSGGSGAIL LVNCDRDVHG SREDLHDSHL RSLEDLQDMS
PMVLSCDGPD DLFKSHKPVL KASLPDSRRL GVFCARGGTS LSNYKQVLGP RHNSYEVERH
PGERDIQFYV EGLAFPDASF SGLLSLSVSL VDTRPLSEVL VFTDSVTFRV APWIMTPNTQ
PPLELYVCSV TDMHGSNDKF LEDMSHLATK ANCKLVVCPR LENRNDRWIQ DEMEFGYIDA
PHKSFPVVFD SPRNRGLRDF ALKKILGPDF GYVTREIQFA GASGLDSFGN LDVSPPVRVG
NTEYPLGRIL IGGNFPKSSG RRMARVVRDF LHAQQVQAPV ELYSDWLSVG HVDEFLSFVP
TSDQKGFRLL LASPSACLQL FQEKKEEGYG EAKQFDGLKH KTKRSINDIL ADRHLRRDSA
HVQKCIDWNR EVLKQELGLS ESDIVDIPQL FFLKGAYAEA FFPDMVNMVV LGKYLGIPKP
FGPIINGRCC LEEKVRSLLE PLGLRCVFID DFLFYHQLLG EIHCGTNVRR KPFAFRWWNS
VP
