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O08557 (DDAH1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
N(G),N(G)-dimethylarginine dimethylaminohydrolase 1

Short name=DDAH-1
Short name=Dimethylarginine dimethylaminohydrolase 1
EC=3.5.3.18
Alternative name(s):
DDAHI
Dimethylargininase-1
Gene names
Name:Ddah1
Synonyms:Ddah
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation. Ref.3

Catalytic activity

N(omega),N(omega)-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline.

Enzyme regulation

Inhibited by zinc ions. Ref.3

Subunit structure

Monomer By similarity.

Tissue specificity

Detected in red blood cells (at protein level). Widely distributed, high amounts found in kidney, brain, aorta and pancreas. Ref.3

Sequence similarities

Belongs to the DDAH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 285284N(G),N(G)-dimethylarginine dimethylaminohydrolase 1
PRO_0000171120

Sites

Active site1731Proton donor By similarity
Active site2741Nucleophile By similarity
Metal binding2741Zinc By similarity
Binding site301Substrate; via carbonyl oxygen By similarity
Binding site731Substrate By similarity
Binding site781Substrate By similarity
Binding site791Substrate By similarity
Binding site981Substrate By similarity
Binding site1451Substrate By similarity
Binding site2681Substrate; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.1
Modified residue2221S-nitrosocysteine By similarity
Modified residue2741S-nitrosocysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
O08557 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9FE8DF56E37A7E4A

FASTA28531,426
        10         20         30         40         50         60 
MAGLSHPSVF GRATHAVVRA PPESLCRHAL RRSQGEEVDF ARAERQHQLY VGVLGSKLGL 

        70         80         90        100        110        120 
QVVQLPADES LPDCVFVEDV AVVCEETALI TRPGAPSRRK EVDMMKEALE KLQLNIVEMK 

       130        140        150        160        170        180 
DENATLDGGD VLFTGREFFV GLSKRTNQRG AEILADTFKD YAVSTVPVAD SLHLKSFCSM 

       190        200        210        220        230        240 
AGPNLIAIGS SESAQKALKI MQQMSDHRYD KLTVPDDMAA NCIYLNIPSK GHVLLHRTPE 

       250        260        270        280 
EYPESAKVYE KLKDHLLIPV SNSEMEKVDG LLTCCSVFIN KKTDS 

« Hide

References

[1]"Cloning and sequencing of cDNA encoding NG,NG-dimethylarginine dimethylaminohydrolase from rat kidney."
Kimoto M., Sasakawa T., Tsuji H., Miyatake S., Oka T., Nio N., Ogawa T.
Biochim. Biophys. Acta 1337:6-10(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION AT ALA-2.
Strain: Wistar.
Tissue: Kidney.
[2]Lubec G., Afjehi-Sadat L., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 46-57; 112-136 AND 160-175, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
[3]"Contribution of whole blood to the control of plasma asymmetrical dimethylarginine."
Billecke S.S., Kitzmiller L.A., Northrup J.J., Whitesall S.E., Kimoto M., Hinz A.V., D'Alecy L.G.
Am. J. Physiol. 291:H1788-H1796(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D86041 mRNA. Translation: BAA18993.1.
RefSeqNP_071633.1. NM_022297.2.
UniGeneRn.7398.

3D structure databases

ProteinModelPortalO08557.
SMRO08557. Positions 8-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4567619.
STRING10116.ENSRNOP00000044971.

Chemistry

BindingDBO08557.
ChEMBLCHEMBL4196.

PTM databases

PhosphoSiteO08557.

Proteomic databases

PaxDbO08557.
PRIDEO08557.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000045016; ENSRNOP00000044971; ENSRNOG00000014613.
GeneID64157.
KEGGrno:64157.

Organism-specific databases

CTD23576.
RGD70968. Ddah1.

Phylogenomic databases

eggNOGCOG1834.
GeneTreeENSGT00390000009331.
HOGENOMHOG000161035.
HOVERGENHBG055937.
KOK01482.
OMAKTMQQMS.
OrthoDBEOG73V6KV.
PhylomeDBO08557.

Gene expression databases

GenevestigatorO08557.

Family and domain databases

InterProIPR003198. Amidino_trans.
[Graphical view]
PfamPF02274. Amidinotransf. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio612794.
PROO08557.

Entry information

Entry nameDDAH1_RAT
AccessionPrimary (citable) accession number: O08557
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families