PADI2_RAT
ID PADI2_RAT Reviewed; 665 AA.
AC P20717;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein-arginine deiminase type-2;
DE EC=3.5.3.15 {ECO:0000250|UniProtKB:Q9Y2J8};
DE AltName: Full=Peptidylarginine deiminase II;
DE AltName: Full=Protein-arginine deiminase type II;
GN Name=Padi2; Synonyms=Pad2, Pdi, Pdi2;
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], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=2768262; DOI=10.1016/s0021-9258(19)84818-4;
RA Watanabe K., Senshu T.;
RT "Isolation and characterization of cDNA clones encoding rat skeletal muscle
RT peptidylarginine deiminase.";
RL J. Biol. Chem. 264:15255-15260(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX PubMed=1601308; DOI=10.1016/0378-1119(92)90585-d;
RA Watanabe K., Nomoto M., Nagata S., Itoh Y., Hikichi K., Maruyama N.,
RA Mita T., Senshu T.;
RT "The rat peptidylarginine deiminase-encoding gene: structural analysis and
RT the 5'-flanking sequence.";
RL Gene 114:261-265(1992).
CC -!- FUNCTION: Catalyzes the deimination of arginine residues of proteins.
CC {ECO:0000250|UniProtKB:Q9Y2J8}.
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:Q9Y2J8};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2J8};
CC Note=Binding of Ca(2+) triggers a conformation change that is essential
CC for catalytic activity. {ECO:0000250|UniProtKB:Q9Y2J8};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2J8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2J8}.
CC -!- TISSUE SPECIFICITY: Spinal cord, submaxillary gland, cerebrum,
CC cerebellum, and skeletal muscle. {ECO:0000269|PubMed:2768262}.
CC -!- SIMILARITY: Belongs to the protein arginine deiminase family.
CC {ECO:0000305}.
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DR EMBL; J05022; AAA41793.1; -; mRNA.
DR EMBL; D10459; BAA01253.1; -; Genomic_DNA.
DR PIR; A34339; DIRTR1.
DR RefSeq; NP_058922.1; NM_017226.1.
DR AlphaFoldDB; P20717; -.
DR SMR; P20717; -.
DR CORUM; P20717; -.
DR STRING; 10116.ENSRNOP00000010183; -.
DR iPTMnet; P20717; -.
DR PhosphoSitePlus; P20717; -.
DR PaxDb; P20717; -.
DR PRIDE; P20717; -.
DR GeneID; 29511; -.
DR KEGG; rno:29511; -.
DR UCSC; RGD:3288; rat.
DR CTD; 11240; -.
DR RGD; 3288; Padi2.
DR eggNOG; ENOG502QVJA; Eukaryota.
DR InParanoid; P20717; -.
DR OrthoDB; 787070at2759; -.
DR PhylomeDB; P20717; -.
DR BRENDA; 3.5.3.15; 5301.
DR Reactome; R-RNO-3247509; Chromatin modifying enzymes.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P20717; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004668; F:protein-arginine deiminase activity; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; ISO:RGD.
DR GO; GO:0036414; P:histone citrullination; IBA:GO_Central.
DR GO; GO:0036413; P:histone H3-R26 citrullination; ISO:RGD.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISO:RGD.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:1901624; P:negative regulation of lymphocyte chemotaxis; ISO:RGD.
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; Direct protein sequencing; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..665
FT /note="Protein-arginine deiminase type-2"
FT /id="PRO_0000220028"
FT ACT_SITE 647
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
SQ SEQUENCE 665 AA; 75356 MW; 96C38C8ECD7A0799 CRC64;
MLRERTVRLQ YGSRVEAVYV LGTQLWTDVY SAAPAGAKTF SLKHSEGVKV EVVRDGEAEE
VVTNGKQRWA LSPSTTLRLS MAQASTEASS DKVTVNYYEE DGSAPIDQAG LFLTAIEISL
DVDADRDGEV EKNNPKKASW TWGPEGQGAI LLVNCDRDTP WLPKEDCSDE KVYSKQDLQD
MSQMILRTKG PDRLPAGYEI VLYISMSDSD KVGVFYVENP FFGQRYIHIL GRQKLYHVVK
YTGGSAELLF FVEGLRFPDE SFSGLVSIHV SLLEYMAEDI PLTPIFTDTV TFRIAPWIMT
PNILPPVSVF VCCMKDNYLF LKEVKNLVEK TNCELKVCFQ YMNRGDRWIQ DEIEFGYIEA
PHKGFPVVLD SPRDGNLKDF PIKQLLGPDF GYVTREPLFE TVTSLDSFGN LEVSPPVTVN
GKAYPLGRIL IGSSFPLSGG RRMTKVVRDF LQAQQVQAPV ELYSDWLTVG HVDEFMTFVP
IPGKKEFRLL MASTSACYQL FREKQKEGHG EAIMFKGLGG MSSKRITINK ILSNESLTQE
NQYFQRCLDW NRDILKKELA LTEKDIIDLP ALFKMDEDRQ ARAFFPNMVN MIVLDKDLGI
PKPFGPQVEE ECCLETHVRG LLEPLGLACT FIDDISAYHK FLGEVHCGTN VRRKPFTFKW
WHMVP
