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Q9ULW8

- PADI3_HUMAN

UniProt

Q9ULW8 - PADI3_HUMAN

Protein

Protein-arginine deiminase type-3

Gene

PADI3

Organism
Homo sapiens (Human)
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 (21 Dec 2004)
      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.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein citrullination Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06944-MONOMER.
    BRENDAi3.5.3.15. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-arginine deiminase type-3 (EC:3.5.3.15)
    Alternative name(s):
    Peptidylarginine deiminase III
    Protein-arginine deiminase type III
    Gene namesi
    Name:PADI3
    Synonyms:PDI3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18337. PADI3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32901.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 664664Protein-arginine deiminase type-3PRO_0000220029Add
    BLAST

    Proteomic databases

    MaxQBiQ9ULW8.
    PaxDbiQ9ULW8.
    PeptideAtlasiQ9ULW8.
    PRIDEiQ9ULW8.

    PTM databases

    PhosphoSiteiQ9ULW8.

    Expressioni

    Tissue specificityi

    Hair follicles, and epidermis at very low levels.

    Gene expression databases

    BgeeiQ9ULW8.
    CleanExiHS_PADI3.
    GenevestigatoriQ9ULW8.

    Organism-specific databases

    HPAiHPA043739.

    Interactioni

    Protein-protein interaction databases

    BioGridi119686. 1 interaction.
    STRINGi9606.ENSP00000364609.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ULW8.
    SMRiQ9ULW8. Positions 6-664.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the protein arginine deiminase family.Curated

    Phylogenomic databases

    eggNOGiNOG42085.
    HOGENOMiHOG000220908.
    HOVERGENiHBG053016.
    InParanoidiQ9ULW8.
    KOiK01481.
    OMAiMSLQRIV.
    OrthoDBiEOG7P5T09.
    PhylomeDBiQ9ULW8.
    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.

    Q9ULW8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLQRIVRVS LEHPTSAVCV AGVETLVDIY GSVPEGTEMF EVYGTPGVDI    50
    YISPNMERGR ERADTRRWRF DATLEIIVVM NSPSNDLNDS HVQISYHSSH 100
    EPLPLAYAVL YLTCVDISLD CDLNCEGRQD RNFVDKRQWV WGPSGYGGIL 150
    LVNCDRDDPS CDVQDNCDQH VHCLQDLEDM SVMVLRTQGP AALFDDHKLV 200
    LHTSSYDAKR AQVFHICGPE DVCEAYRHVL GQDKVSYEVP RLHGDEERFF 250
    VEGLSFPDAG FTGLISFHVT LLDDSNEDFS ASPIFTDTVV FRVAPWIMTP 300
    STLPPLEVYV CRVRNNTCFV DAVAELARKA GCKLTICPQA ENRNDRWIQD 350
    EMELGYVQAP HKTLPVVFDS PRNGELQDFP YKRILGPDFG YVTREPRDRS 400
    VSGLDSFGNL EVSPPVVANG KEYPLGRILI GGNLPGSSGR RVTQVVRDFL 450
    HAQKVQPPVE LFVDWLAVGH VDEFLSFVPA PDGKGFRMLL ASPGACFKLF 500
    QEKQKCGHGR ALLFQGVVDD EQVKTISINQ VLSNKDLINY NKFVQSCIDW 550
    NREVLKRELG LAECDIIDIP QLFKTERKKA TAFFPDLVNM LVLGKHLGIP 600
    KPFGPIINGC CCLEEKVRSL LEPLGLHCTF IDDFTPYHML HGEVHCGTNV 650
    CRKPFSFKWW NMVP 664
    Length:664
    Mass (Da):74,743
    Last modified:December 21, 2004 - v2
    Checksum:i90C22A50BF6FD480
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti480 – 4801A → V in BAA85974. (PubMed:11069618)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti52 – 521I → V.
    Corresponds to variant rs3750300 [ dbSNP | Ensembl ].
    VAR_020462
    Natural varianti171 – 1711V → M.
    Corresponds to variant rs2272629 [ dbSNP | Ensembl ].
    VAR_020463
    Natural varianti509 – 5091G → R in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035502
    Natural varianti582 – 5821A → T.
    Corresponds to variant rs34097903 [ dbSNP | Ensembl ].
    VAR_053558
    Natural varianti618 – 6181R → Q.
    Corresponds to variant rs35624745 [ dbSNP | Ensembl ].
    VAR_053559

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB026831 mRNA. Translation: BAA85974.1.
    AJ549502 Genomic DNA. Translation: CAE47742.1.
    AL590644 Genomic DNA. Translation: CAH73166.1.
    BC041592 mRNA. Translation: AAH41592.1.
    BC109091 mRNA. Translation: AAI09092.1.
    BC109092 mRNA. Translation: AAI09093.1.
    CCDSiCCDS179.1.
    RefSeqiNP_057317.2. NM_016233.2.
    UniGeneiHs.149195.

    Genome annotation databases

    EnsembliENST00000375460; ENSP00000364609; ENSG00000142619.
    GeneIDi51702.
    KEGGihsa:51702.
    UCSCiuc001bai.3. human.

    Polymorphism databases

    DMDMi56757696.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB026831 mRNA. Translation: BAA85974.1 .
    AJ549502 Genomic DNA. Translation: CAE47742.1 .
    AL590644 Genomic DNA. Translation: CAH73166.1 .
    BC041592 mRNA. Translation: AAH41592.1 .
    BC109091 mRNA. Translation: AAI09092.1 .
    BC109092 mRNA. Translation: AAI09093.1 .
    CCDSi CCDS179.1.
    RefSeqi NP_057317.2. NM_016233.2.
    UniGenei Hs.149195.

    3D structure databases

    ProteinModelPortali Q9ULW8.
    SMRi Q9ULW8. Positions 6-664.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119686. 1 interaction.
    STRINGi 9606.ENSP00000364609.

    Chemistry

    BindingDBi Q9ULW8.
    ChEMBLi CHEMBL1909488.
    DrugBanki DB00155. L-Citrulline.

    PTM databases

    PhosphoSitei Q9ULW8.

    Polymorphism databases

    DMDMi 56757696.

    Proteomic databases

    MaxQBi Q9ULW8.
    PaxDbi Q9ULW8.
    PeptideAtlasi Q9ULW8.
    PRIDEi Q9ULW8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375460 ; ENSP00000364609 ; ENSG00000142619 .
    GeneIDi 51702.
    KEGGi hsa:51702.
    UCSCi uc001bai.3. human.

    Organism-specific databases

    CTDi 51702.
    GeneCardsi GC01P017575.
    HGNCi HGNC:18337. PADI3.
    HPAi HPA043739.
    MIMi 606755. gene.
    neXtProti NX_Q9ULW8.
    PharmGKBi PA32901.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42085.
    HOGENOMi HOG000220908.
    HOVERGENi HBG053016.
    InParanoidi Q9ULW8.
    KOi K01481.
    OMAi MSLQRIV.
    OrthoDBi EOG7P5T09.
    PhylomeDBi Q9ULW8.
    TreeFami TF331952.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06944-MONOMER.
    BRENDAi 3.5.3.15. 2681.

    Miscellaneous databases

    GeneWikii PADI3.
    GenomeRNAii 51702.
    NextBioi 55728.
    PROi Q9ULW8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9ULW8.
    CleanExi HS_PADI3.
    Genevestigatori Q9ULW8.

    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. "Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin."
      Kanno T., Kawada A., Yamanouchi J., Yosida-Noro C., Yoshiki A., Shiraiwa M., Kusakabe M., Manabe M., Tezuka T., Takahara H.
      J. Invest. Dermatol. 115:813-823(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
      Tissue: Keratinocyte.
    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].
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Brain.
    5. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-509.

    Entry informationi

    Entry nameiPADI3_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULW8
    Secondary accession number(s): Q58EY7, Q70SX5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: December 21, 2004
    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
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3