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Protein

Protein-arginine deiminase type-3

Gene

Padi3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the deimination of arginine residues of proteins.

Catalytic activityi

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

Cofactori

GO - Molecular functioni

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

GO - Biological processi

  1. protein citrullination Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1338891. Padi3.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 664664Protein-arginine deiminase type-3PRO_0000220030Add
BLAST

Proteomic databases

PRIDEiQ9Z184.

PTM databases

PhosphoSiteiQ9Z184.

Expressioni

Tissue specificityi

Epidermis and hair follicles.1 Publication

Gene expression databases

BgeeiQ9Z184.
CleanExiMM_PADI3.
ExpressionAtlasiQ9Z184. baseline and differential.
GenevestigatoriQ9Z184.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026377.

Structurei

3D structure databases

ProteinModelPortaliQ9Z184.
SMRiQ9Z184. Positions 6-664.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the protein arginine deiminase family.Curated

Phylogenomic databases

eggNOGiNOG42085.
GeneTreeiENSGT00390000008680.
HOVERGENiHBG053016.
InParanoidiQ9Z184.
KOiK01481.
OMAiADTRRWH.
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.

Q9Z184-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLQRIVRVS LEHPTSAVCV AGVETIVDIY GAVPEGTDMF EVYGTPGVDI
60 70 80 90 100
YVSPSMERSR ERADTRRWCF NKGLEIIVIM NSPSNDLNDS HVQIAYHSSR
110 120 130 140 150
EHLPLAYAVL YLTCVDITLD CDMNCADRQD RSFVDKRQWV WGPDGYGAIL
160 170 180 190 200
LVNCDRDNVD SNAQDNCDQY VRCLQDLEDM SVMVLRTQGP EALFEDHRLI
210 220 230 240 250
LHTSSCDAER ARVFHVCGPE DSCESYKCVL GPDRMSYEVP RLKGYEERFF
260 270 280 290 300
VEGLSFPDAG FPGLISFHVT LLDDSNEDFS ETPIFTDTAV FRVAPWIMTP
310 320 330 340 350
STLPPLEVYV CRVRNNTCFV EAVEELARKA GCKLTICPQA ENRNDRWIQD
360 370 380 390 400
EMELGYVQAP HKTLPVVFDS PRNGELQGFP YKRILGLDFG YVTREPKDSS
410 420 430 440 450
VSGLDSFGNL EVSPPVVANG KEYPLGRILI GGNLPGSRGR RVTQVVRNFL
460 470 480 490 500
HAQKVQPLVE LFVDWLAVGH VDEFLSFVPA PDGKGFRLLL ASPGACFRLF
510 520 530 540 550
QEKQKWGHGR SLLFEGVIGD RRVQTVSINQ ILNNQSLINF NKFAQSCIDW
560 570 580 590 600
NREVLKRELG LAEGDIIDIP QLFKTEKRKA VAFFPDLVNM LVLGKHLGIP
610 620 630 640 650
KPFGPIINGR CCLEEKVRSL LEPLGLHCTF IDDFTPYHML HGEVHCGTNV
660
RREPFAFKWW HMVP
Length:664
Mass (Da):75,073
Last modified:July 27, 2011 - v2
Checksum:iFA6E065DF5D9CB83
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321A → S in BAA34182 (PubMed:10092850).Curated
Sequence conflicti52 – 521V → L in BAA34182 (PubMed:10092850).Curated
Sequence conflicti59 – 591S → N in BAA34182 (PubMed:10092850).Curated
Sequence conflicti79 – 791I → V in BAA34182 (PubMed:10092850).Curated
Sequence conflicti225 – 2251S → A in BAA34182 (PubMed:10092850).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013849 mRNA. Translation: BAA34182.1.
AL807805 Genomic DNA. Translation: CAM25733.1.
CCDSiCCDS18855.1.
RefSeqiNP_035190.3. NM_011060.4.
UniGeneiMm.20851.

Genome annotation databases

EnsembliENSMUST00000026377; ENSMUSP00000026377; ENSMUSG00000025328.
GeneIDi18601.
KEGGimmu:18601.
UCSCiuc008vng.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013849 mRNA. Translation: BAA34182.1.
AL807805 Genomic DNA. Translation: CAM25733.1.
CCDSiCCDS18855.1.
RefSeqiNP_035190.3. NM_011060.4.
UniGeneiMm.20851.

3D structure databases

ProteinModelPortaliQ9Z184.
SMRiQ9Z184. Positions 6-664.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026377.

PTM databases

PhosphoSiteiQ9Z184.

Proteomic databases

PRIDEiQ9Z184.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026377; ENSMUSP00000026377; ENSMUSG00000025328.
GeneIDi18601.
KEGGimmu:18601.
UCSCiuc008vng.1. mouse.

Organism-specific databases

CTDi51702.
MGIiMGI:1338891. Padi3.

Phylogenomic databases

eggNOGiNOG42085.
GeneTreeiENSGT00390000008680.
HOVERGENiHBG053016.
InParanoidiQ9Z184.
KOiK01481.
OMAiADTRRWH.
OrthoDBiEOG7P5T09.
TreeFamiTF331952.

Miscellaneous databases

NextBioi294506.
PROiQ9Z184.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z184.
CleanExiMM_PADI3.
ExpressionAtlasiQ9Z184. baseline and differential.
GenevestigatoriQ9Z184.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse."
    Rusd A.A., Ikejiri Y., Ono H., Yonekawa T., Shiraiwa M., Kawada A., Takahara H.
    Eur. J. Biochem. 259:660-669(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Epidermis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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 nameiPADI3_MOUSE
AccessioniPrimary (citable) accession number: Q9Z184
Secondary accession number(s): A2AMU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: January 7, 2015
This is version 95 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, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.