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Q9ULC6 (PADI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 103. 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-1

EC=3.5.3.15
Alternative name(s):
Peptidylarginine deiminase I
Protein-arginine deiminase type I
Gene names
Name:PADI1
Synonyms:PDI1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the deimination of arginine residues of proteins By similarity.

Catalytic activity

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

Cofactor

Calcium By similarity.

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Epidermis, prostate, testis, placenta, spleen and thymus. Ref.1

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

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 663663Protein-arginine deiminase type-1
PRO_0000220023

Natural variations

Natural variant6491V → M.
Corresponds to variant rs16824215 [ dbSNP | Ensembl ].
VAR_053557

Experimental info

Sequence conflict4201V → G in BAA85771. Ref.1
Sequence conflict4991L → P in BAA85771. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9ULC6 [UniParc].

Last modified December 21, 2004. Version 2.
Checksum: 4674CEBC03A7E7CA

FASTA66374,666
        10         20         30         40         50         60 
MAPKRVVQLS LKMPTHAVCV VGVEAHVDIH SDVPKGANSF RVSGSSGVEV FMVYNRTRVK 

        70         80         90        100        110        120 
EPIGKARWPL DTDADMVVSV GTASKELKDF KVRVSYFGEQ EDQALGRSVL YLTGVDISLE 

       130        140        150        160        170        180 
VDTGRTGKVK RSQGDKKTWR WGPEGYGAIL LVNCDRDNHR SAEPDLTHSW LMSLADLQDM 

       190        200        210        220        230        240 
SPMLLSCNGP DKLFDSHKLV LNVPFSDSKR VRVFCARGGN SLSDYKQVLG PQCLSYEVER 

       250        260        270        280        290        300 
QPGEQEIKFY VEGLTFPDAD FLGLVSLSVS LVDPGTLPEV TLFTDTVGFR MAPWIMTPNT 

       310        320        330        340        350        360 
QPPEELYVCR VMDTHGSNEK FLEDMSYLTL KANCKLTICP QVENRNDRWI QDEMEFGYIE 

       370        380        390        400        410        420 
APHKSFPVVF DSPRNRGLKD FPYKRILGPD FGYVTREIPL PGPSSLDSFG NLDVSPPVTV 

       430        440        450        460        470        480 
GGTEYPLGRI LIGSSFPKSG GRQMARAVRN FLKAQQVQAP VELYSDWLSV GHVDEFLTFV 

       490        500        510        520        530        540 
PTSDQKGFRL LLASPSACLK LFQEKKEEGY GEAAQFDGLK HQAKRSINEM LADRHLQRDN 

       550        560        570        580        590        600 
LHAQKCIDWN RNVLKRELGL AESDIVDIPQ LFFLKNFYAE AFFPDMVNMV VLGKYLGIPK 

       610        620        630        640        650        660 
PYGPIINGRC CLEEKVQSLL EPLGLHCIFI DDYLSYHELQ GEIHCGTNVR RKPFPFKWWN 


MVP 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I."
Guerrin M., Ishigami A., Mechin M.-C., Nachat R., Valmary S., Sebbag M., Simon M., Senshu T., Serre G.
Biochem. J. 370:167-174(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Epidermis.
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB033768 mRNA. Translation: BAA85771.1.
AJ549502 Genomic DNA. Translation: CAE47741.1.
AL590644 Genomic DNA. Translation: CAH73165.1.
CH471134 Genomic DNA. Translation: EAW94833.1.
BC130574 mRNA. Translation: AAI30575.1.
BC136402 mRNA. Translation: AAI36403.1.
RefSeqNP_037490.2. NM_013358.2.
UniGeneHs.412941.

3D structure databases

ProteinModelPortalQ9ULC6.
SMRQ9ULC6. Positions 6-663.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118980. 1 interaction.

Chemistry

BindingDBQ9ULC6.
ChEMBLCHEMBL1909486.
DrugBankDB00155. L-Citrulline.

PTM databases

PhosphoSiteQ9ULC6.

Polymorphism databases

DMDM56757695.

Proteomic databases

PaxDbQ9ULC6.
PeptideAtlasQ9ULC6.
PRIDEQ9ULC6.

Protocols and materials databases

DNASU29943.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375471; ENSP00000364620; ENSG00000142623.
GeneID29943.
KEGGhsa:29943.
UCSCuc001bah.1. human.

Organism-specific databases

CTD29943.
GeneCardsGC01P017531.
HGNCHGNC:18367. PADI1.
HPAHPA028133.
MIM607934. gene.
neXtProtNX_Q9ULC6.
PharmGKBPA32899.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42085.
HOGENOMHOG000220908.
HOVERGENHBG053016.
InParanoidQ9ULC6.
KOK01481.
OMADIPQLFF.
OrthoDBEOG7P5T09.
PhylomeDBQ9ULC6.
TreeFamTF331952.

Enzyme and pathway databases

BioCycMetaCyc:HS06945-MONOMER.
BRENDA3.5.3.15. 2681.

Gene expression databases

ArrayExpressQ9ULC6.
BgeeQ9ULC6.
CleanExHS_PADI1.
GenevestigatorQ9ULC6.

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

GeneWikiPADI1.
GenomeRNAi29943.
NextBio52603.
PROQ9ULC6.
SOURCESearch...

Entry information

Entry namePADI1_HUMAN
AccessionPrimary (citable) accession number: Q9ULC6
Secondary accession number(s): A1L4K6, Q70SX6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: December 21, 2004
Last modified: February 19, 2014
This is version 103 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