PADI2_MOUSE
ID PADI2_MOUSE Reviewed; 673 AA.
AC Q08642; Q75WD0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
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 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], ACETYLATION AT MET-1, CITRULLINATION AT
RP ARG-352, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8354274; DOI=10.1111/j.1432-1033.1993.tb18079.x;
RA Tsuchida M., Takahara H., Minami N., Arai T., Kobayashi Y., Tsujimoto H.,
RA Fukazawa C., Sugawara K.;
RT "cDNA nucleotide sequence and primary structure of mouse uterine
RT peptidylarginine deiminase. Detection of a 3'-untranslated nucleotide
RT sequence common to the mRNA of transiently expressed genes and rapid
RT turnover of this enzyme's mRNA in the estrous cycle.";
RL Eur. J. Biochem. 215:677-685(1993).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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: Expressed in various tissues including muscle,
CC uterus, spinal cord, salivary gland and pancreas.
CC {ECO:0000269|PubMed:1778991}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the estrus cycle. Expressed
CC during diestrus and proestrus with an eight fold decline when estrus
CC cycle is reached.
CC -!- SIMILARITY: Belongs to the protein arginine deiminase family.
CC {ECO:0000305}.
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DR EMBL; D16580; BAA04012.1; -; mRNA.
DR EMBL; AB121692; BAD16624.1; -; Genomic_DNA.
DR EMBL; AL645625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040350; AAH40350.1; -; mRNA.
DR EMBL; BC049947; AAH49947.1; -; mRNA.
DR CCDS; CCDS18857.1; -.
DR PIR; S35038; DIMSR1.
DR RefSeq; NP_032838.2; NM_008812.2.
DR AlphaFoldDB; Q08642; -.
DR SMR; Q08642; -.
DR BioGRID; 202093; 2.
DR STRING; 10090.ENSMUSP00000030765; -.
DR BindingDB; Q08642; -.
DR ChEMBL; CHEMBL2321611; -.
DR iPTMnet; Q08642; -.
DR PhosphoSitePlus; Q08642; -.
DR SwissPalm; Q08642; -.
DR EPD; Q08642; -.
DR MaxQB; Q08642; -.
DR PaxDb; Q08642; -.
DR PeptideAtlas; Q08642; -.
DR PRIDE; Q08642; -.
DR ProteomicsDB; 294148; -.
DR Antibodypedia; 29317; 270 antibodies from 28 providers.
DR DNASU; 18600; -.
DR Ensembl; ENSMUST00000030765; ENSMUSP00000030765; ENSMUSG00000028927.
DR GeneID; 18600; -.
DR KEGG; mmu:18600; -.
DR UCSC; uc008vni.2; mouse.
DR CTD; 11240; -.
DR MGI; MGI:1338892; Padi2.
DR VEuPathDB; HostDB:ENSMUSG00000028927; -.
DR eggNOG; ENOG502QVJA; Eukaryota.
DR GeneTree; ENSGT00940000153217; -.
DR HOGENOM; CLU_021911_0_0_1; -.
DR InParanoid; Q08642; -.
DR OMA; DFPIKQL; -.
DR OrthoDB; 787070at2759; -.
DR PhylomeDB; Q08642; -.
DR TreeFam; TF331952; -.
DR BRENDA; 3.5.3.15; 3474.
DR Reactome; R-MMU-3247509; Chromatin modifying enzymes.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 18600; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Padi2; mouse.
DR PRO; PR:Q08642; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q08642; protein.
DR Bgee; ENSMUSG00000028927; Expressed in vestibular membrane of cochlear duct and 150 other tissues.
DR Genevisible; Q08642; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004668; F:protein-arginine deiminase activity; ISS:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; ISO:MGI.
DR GO; GO:0036414; P:histone citrullination; IBA:GO_Central.
DR GO; GO:0036413; P:histone H3-R26 citrullination; ISO:MGI.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISO:MGI.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:1901624; P:negative regulation of lymphocyte chemotaxis; ISO:MGI.
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 Acetylation; Calcium; Citrullination; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..673
FT /note="Protein-arginine deiminase type-2"
FT /id="PRO_0000220027"
FT ACT_SITE 655
FT /note="Nucleophile"
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 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 164
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="3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 174
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="4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:8354274"
FT MOD_RES 352
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:8354274"
FT CONFLICT 665
FT /note="T -> A (in Ref. 1; BAA04012 and 4; AAH40350/
FT AAH49947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 76250 MW; F72A36079DA914E0 CRC64;
MQPPIRENML RERTVRLQYG SRVEAVYVLG TQLWTDVYSA APAGAKTFSL KHSEGVKVEV
VRDGEAEEVV TNGKQRWALS PSSTLRLSMA QASTEASSDK VTVNYYEEEG SAPIDQAGLF
LTAIEISLDV DADRDGEVEK NNPKKASWTW GPEGQGAILL VNCDRDTPWL PKEDCSDEKV
YSKQDLQDMS QMILRTKGPD RLPAGYEIVL YISMSDSDKV GVFYVENPFF GQRYIHILGR
QKLYHVVKYT GGSAELLFFV EGLCFPDESF SGLVSIHVSL LEYMAEGIPL TPIFTDTVMF
RIAPWIMTPN ILPPVSVFVC CMKDNYLFLK EVKNLVEKTN CELKVCFQYM NRGDRWIQDE
IEFGYIEAPH KGFPVVLDSP RDGNLKDFPI KQLLGPDFGY VTREPLFETV TSLDSFGNLE
VSPPVTVNGK EYPLGRILIG SSFPLSGGRR MTKVVRDFLQ AQQVQAPVEL YSDWLTVGHV
DEFMTFIPIP GKKEFRLLMA STSACYQLFR EKQKAGHGEA VMFKGLGGMS SKRITINKIL
SNESLTQENQ YFQRCLDWNR DILKRELALT EKDIIDLPAL FKMDENHQAR AFFPNMVNMI
VLDKDLGIPK PFGPQVEEEC CLETHVRGLL EPLGLACTFI DDISAYHKFL GEVHCGTNVR
RKPFTFKWWH MVP
