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Q9ULW8 (PADI3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-arginine deiminase type-3

EC=3.5.3.15
Alternative name(s):
Peptidylarginine deiminase III
Protein-arginine deiminase type III
Gene names
Name:PADI3
Synonyms:PDI3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the deimination of arginine residues of proteins.

Catalytic activity

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

Cofactor

Calcium By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Hair follicles, and epidermis at very low levels.

Sequence similarities

Belongs to the protein arginine deiminase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandCalcium
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein citrullination

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

protein-arginine deiminase activity

Traceable author statement PubMed 10092850. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 664664Protein-arginine deiminase type-3
PRO_0000220029

Natural variations

Natural variant521I → V.
Corresponds to variant rs3750300 [ dbSNP | Ensembl ].
VAR_020462
Natural variant1711V → M.
Corresponds to variant rs2272629 [ dbSNP | Ensembl ].
VAR_020463
Natural variant5091G → R in a breast cancer sample; somatic mutation. Ref.5
VAR_035502
Natural variant5821A → T.
Corresponds to variant rs34097903 [ dbSNP | Ensembl ].
VAR_053558
Natural variant6181R → Q.
Corresponds to variant rs35624745 [ dbSNP | Ensembl ].
VAR_053559

Experimental info

Sequence conflict4801A → V in BAA85974. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9ULW8 [UniParc].

Last modified December 21, 2004. Version 2.
Checksum: 90C22A50BF6FD480

FASTA66474,743
        10         20         30         40         50         60 
MSLQRIVRVS LEHPTSAVCV AGVETLVDIY GSVPEGTEMF EVYGTPGVDI YISPNMERGR 

        70         80         90        100        110        120 
ERADTRRWRF DATLEIIVVM NSPSNDLNDS HVQISYHSSH EPLPLAYAVL YLTCVDISLD 

       130        140        150        160        170        180 
CDLNCEGRQD RNFVDKRQWV WGPSGYGGIL LVNCDRDDPS CDVQDNCDQH VHCLQDLEDM 

       190        200        210        220        230        240 
SVMVLRTQGP AALFDDHKLV LHTSSYDAKR AQVFHICGPE DVCEAYRHVL GQDKVSYEVP 

       250        260        270        280        290        300 
RLHGDEERFF VEGLSFPDAG FTGLISFHVT LLDDSNEDFS ASPIFTDTVV FRVAPWIMTP 

       310        320        330        340        350        360 
STLPPLEVYV CRVRNNTCFV DAVAELARKA GCKLTICPQA ENRNDRWIQD EMELGYVQAP 

       370        380        390        400        410        420 
HKTLPVVFDS PRNGELQDFP YKRILGPDFG YVTREPRDRS VSGLDSFGNL EVSPPVVANG 

       430        440        450        460        470        480 
KEYPLGRILI GGNLPGSSGR RVTQVVRDFL HAQKVQPPVE LFVDWLAVGH VDEFLSFVPA 

       490        500        510        520        530        540 
PDGKGFRMLL ASPGACFKLF QEKQKCGHGR ALLFQGVVDD EQVKTISINQ VLSNKDLINY 

       550        560        570        580        590        600 
NKFVQSCIDW NREVLKRELG LAECDIIDIP QLFKTERKKA TAFFPDLVNM LVLGKHLGIP 

       610        620        630        640        650        660 
KPFGPIINGC CCLEEKVRSL LEPLGLHCTF IDDFTPYHML HGEVHCGTNV CRKPFSFKWW 


NMVP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-509.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_057317.2. NM_016233.2.
UniGeneHs.149195.

3D structure databases

ProteinModelPortalQ9ULW8.
SMRQ9ULW8. Positions 6-664.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119686. 1 interaction.
STRING9606.ENSP00000364609.

Chemistry

BindingDBQ9ULW8.
ChEMBLCHEMBL1909488.
DrugBankDB00155. L-Citrulline.

PTM databases

PhosphoSiteQ9ULW8.

Polymorphism databases

DMDM56757696.

Proteomic databases

PaxDbQ9ULW8.
PeptideAtlasQ9ULW8.
PRIDEQ9ULW8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375460; ENSP00000364609; ENSG00000142619.
GeneID51702.
KEGGhsa:51702.
UCSCuc001bai.3. human.

Organism-specific databases

CTD51702.
GeneCardsGC01P017575.
HGNCHGNC:18337. PADI3.
HPAHPA043739.
MIM606755. gene.
neXtProtNX_Q9ULW8.
PharmGKBPA32901.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42085.
HOGENOMHOG000220908.
HOVERGENHBG053016.
InParanoidQ9ULW8.
KOK01481.
OMAMSLQRIV.
OrthoDBEOG7P5T09.
PhylomeDBQ9ULW8.
TreeFamTF331952.

Enzyme and pathway databases

BioCycMetaCyc:HS06944-MONOMER.
BRENDA3.5.3.15. 2681.

Gene expression databases

BgeeQ9ULW8.
CleanExHS_PADI3.
GenevestigatorQ9ULW8.

Family and domain databases

InterProIPR008972. Cupredoxin.
IPR004303. PAD.
IPR013530. PAD_C.
IPR013732. PAD_N.
IPR013733. Prot_Arg_deaminase_cen_dom.
IPR016296. Protein-arginine_deiminase_sub.
[Graphical view]
PANTHERPTHR10837. PTHR10837. 1 hit.
PfamPF03068. PAD. 1 hit.
PF08527. PAD_M. 1 hit.
PF08526. PAD_N. 1 hit.
[Graphical view]
PIRSFPIRSF001247. Protein-arginine_deiminase. 1 hit.
SUPFAMSSF110083. SSF110083. 1 hit.
SSF49503. SSF49503. 1 hit.
ProtoNetSearch...

Other

GeneWikiPADI3.
GenomeRNAi51702.
NextBio55728.
PROQ9ULW8.
SOURCESearch...

Entry information

Entry namePADI3_HUMAN
AccessionPrimary (citable) accession number: Q9ULW8
Secondary accession number(s): Q58EY7, Q70SX5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM