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Q08642

- PADI2_MOUSE

UniProt

Q08642 - PADI2_MOUSE

Protein

Protein-arginine deiminase type-2

Gene

Padi2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the deimination of arginine residues of proteins.

    Catalytic activityi

    Protein L-arginine + H2O = protein L-citrulline + NH3.

    Cofactori

    Calcium.

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein-arginine deiminase activity Source: UniProtKB-EC

    GO - Biological processi

    1. protein citrullination Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    BRENDAi3.5.3.15. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-arginine deiminase type-2 (EC:3.5.3.15)
    Alternative name(s):
    Peptidylarginine deiminase II
    Protein-arginine deiminase type II
    Gene namesi
    Name:Padi2
    Synonyms:Pdi, Pdi2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1338892. Padi2.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 673673Protein-arginine deiminase type-2PRO_0000220027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei352 – 3521Citrulline1 Publication

    Keywords - PTMi

    Acetylation, Citrullination

    Proteomic databases

    MaxQBiQ08642.
    PaxDbiQ08642.
    PRIDEiQ08642.

    PTM databases

    PhosphoSiteiQ08642.

    Expressioni

    Tissue specificityi

    Expressed in various tissues including muscle, uterus, spinal cord, salivary gland and pancreas.1 Publication

    Developmental stagei

    Expressed during the estrus cycle. Expressed during diestrus and proestrus with an eight fold decline when estrus cycle is reached.

    Gene expression databases

    BgeeiQ08642.
    CleanExiMM_PADI2.
    GenevestigatoriQ08642.

    Interactioni

    Protein-protein interaction databases

    BioGridi202093. 1 interaction.
    IntActiQ08642. 1 interaction.
    MINTiMINT-4106481.

    Structurei

    3D structure databases

    ProteinModelPortaliQ08642.
    SMRiQ08642. Positions 15-673.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the protein arginine deiminase family.Curated

    Phylogenomic databases

    eggNOGiNOG42085.
    GeneTreeiENSGT00390000008680.
    HOGENOMiHOG000220908.
    HOVERGENiHBG053016.
    InParanoidiQ75WD0.
    KOiK01481.
    OMAiCLETHVR.
    OrthoDBiEOG7P5T09.
    TreeFamiTF331952.

    Family and domain databases

    InterProiIPR008972. Cupredoxin.
    IPR004303. PAD.
    IPR013530. PAD_C.
    IPR013732. PAD_N.
    IPR013733. Prot_Arg_deaminase_cen_dom.
    IPR016296. Protein-arginine_deiminase_sub.
    [Graphical view]
    PANTHERiPTHR10837. PTHR10837. 1 hit.
    PfamiPF03068. PAD. 1 hit.
    PF08527. PAD_M. 1 hit.
    PF08526. PAD_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001247. Protein-arginine_deiminase. 1 hit.
    SUPFAMiSSF110083. SSF110083. 1 hit.
    SSF49503. SSF49503. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q08642-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQPPIRENML RERTVRLQYG SRVEAVYVLG TQLWTDVYSA APAGAKTFSL    50
    KHSEGVKVEV VRDGEAEEVV TNGKQRWALS PSSTLRLSMA QASTEASSDK 100
    VTVNYYEEEG SAPIDQAGLF LTAIEISLDV DADRDGEVEK NNPKKASWTW 150
    GPEGQGAILL VNCDRDTPWL PKEDCSDEKV YSKQDLQDMS QMILRTKGPD 200
    RLPAGYEIVL YISMSDSDKV GVFYVENPFF GQRYIHILGR QKLYHVVKYT 250
    GGSAELLFFV EGLCFPDESF SGLVSIHVSL LEYMAEGIPL TPIFTDTVMF 300
    RIAPWIMTPN ILPPVSVFVC CMKDNYLFLK EVKNLVEKTN CELKVCFQYM 350
    NRGDRWIQDE IEFGYIEAPH KGFPVVLDSP RDGNLKDFPI KQLLGPDFGY 400
    VTREPLFETV TSLDSFGNLE VSPPVTVNGK EYPLGRILIG SSFPLSGGRR 450
    MTKVVRDFLQ AQQVQAPVEL YSDWLTVGHV DEFMTFIPIP GKKEFRLLMA 500
    STSACYQLFR EKQKAGHGEA VMFKGLGGMS SKRITINKIL SNESLTQENQ 550
    YFQRCLDWNR DILKRELALT EKDIIDLPAL FKMDENHQAR AFFPNMVNMI 600
    VLDKDLGIPK PFGPQVEEEC CLETHVRGLL EPLGLACTFI DDISAYHKFL 650
    GEVHCGTNVR RKPFTFKWWH MVP 673
    Length:673
    Mass (Da):76,250
    Last modified:July 27, 2011 - v2
    Checksum:iF72A36079DA914E0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti665 – 6651T → A in BAA04012. (PubMed:8354274)Curated
    Sequence conflicti665 – 6651T → A in AAH40350. (PubMed:15489334)Curated
    Sequence conflicti665 – 6651T → A in AAH49947. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16580 mRNA. Translation: BAA04012.1.
    AB121692 Genomic DNA. Translation: BAD16624.1.
    AL645625, AL807805 Genomic DNA. Translation: CAM16760.1.
    AL807805, AL645625 Genomic DNA. Translation: CAM25735.1.
    BC040350 mRNA. Translation: AAH40350.1.
    BC049947 mRNA. Translation: AAH49947.1.
    CCDSiCCDS18857.1.
    PIRiS35038. DIMSR1.
    RefSeqiNP_032838.2. NM_008812.2.
    UniGeneiMm.2296.

    Genome annotation databases

    EnsembliENSMUST00000030765; ENSMUSP00000030765; ENSMUSG00000028927.
    GeneIDi18600.
    KEGGimmu:18600.
    UCSCiuc008vni.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16580 mRNA. Translation: BAA04012.1 .
    AB121692 Genomic DNA. Translation: BAD16624.1 .
    AL645625 , AL807805 Genomic DNA. Translation: CAM16760.1 .
    AL807805 , AL645625 Genomic DNA. Translation: CAM25735.1 .
    BC040350 mRNA. Translation: AAH40350.1 .
    BC049947 mRNA. Translation: AAH49947.1 .
    CCDSi CCDS18857.1.
    PIRi S35038. DIMSR1.
    RefSeqi NP_032838.2. NM_008812.2.
    UniGenei Mm.2296.

    3D structure databases

    ProteinModelPortali Q08642.
    SMRi Q08642. Positions 15-673.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202093. 1 interaction.
    IntActi Q08642. 1 interaction.
    MINTi MINT-4106481.

    Chemistry

    ChEMBLi CHEMBL2321611.

    PTM databases

    PhosphoSitei Q08642.

    Proteomic databases

    MaxQBi Q08642.
    PaxDbi Q08642.
    PRIDEi Q08642.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030765 ; ENSMUSP00000030765 ; ENSMUSG00000028927 .
    GeneIDi 18600.
    KEGGi mmu:18600.
    UCSCi uc008vni.2. mouse.

    Organism-specific databases

    CTDi 11240.
    MGIi MGI:1338892. Padi2.

    Phylogenomic databases

    eggNOGi NOG42085.
    GeneTreei ENSGT00390000008680.
    HOGENOMi HOG000220908.
    HOVERGENi HBG053016.
    InParanoidi Q75WD0.
    KOi K01481.
    OMAi CLETHVR.
    OrthoDBi EOG7P5T09.
    TreeFami TF331952.

    Enzyme and pathway databases

    BRENDAi 3.5.3.15. 3474.

    Miscellaneous databases

    NextBioi 294502.
    PROi Q08642.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q08642.
    CleanExi MM_PADI2.
    Genevestigatori Q08642.

    Family and domain databases

    InterProi IPR008972. Cupredoxin.
    IPR004303. PAD.
    IPR013530. PAD_C.
    IPR013732. PAD_N.
    IPR013733. Prot_Arg_deaminase_cen_dom.
    IPR016296. Protein-arginine_deiminase_sub.
    [Graphical view ]
    PANTHERi PTHR10837. PTHR10837. 1 hit.
    Pfami PF03068. PAD. 1 hit.
    PF08527. PAD_M. 1 hit.
    PF08526. PAD_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001247. Protein-arginine_deiminase. 1 hit.
    SUPFAMi SSF110083. SSF110083. 1 hit.
    SSF49503. SSF49503. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "cDNA nucleotide sequence and primary structure of mouse uterine peptidylarginine deiminase. Detection of a 3'-untranslated nucleotide sequence common to the mRNA of transiently expressed genes and rapid turnover of this enzyme's mRNA in the estrous cycle."
      Tsuchida M., Takahara H., Minami N., Arai T., Kobayashi Y., Tsujimoto H., Fukazawa C., Sugawara K.
      Eur. J. Biochem. 215:677-685(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT MET-1, CITRULLINATION AT ARG-352, PARTIAL PROTEIN SEQUENCE.
    2. "Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6."
      Chavanas S., Mechin M.-C., Takahara H., Kawada A., Nachat R., Serre G., Simon M.
      Gene 330:19-27(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Mammary gland and Salivary gland.
    5. "Three types of mouse peptidylarginine deiminase: characterization and tissue distribution."
      Terakawa H., Takahara H., Sugawara K.
      J. Biochem. 110:661-666(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPADI2_MOUSE
    AccessioniPrimary (citable) accession number: Q08642
    Secondary accession number(s): Q75WD0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3