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Protein

N(G),N(G)-dimethylarginine dimethylaminohydrolase 1

Gene

Ddah1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibited by zinc ions.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301Substrate; via carbonyl oxygenBy similarity
Binding sitei73 – 731SubstrateBy similarity
Binding sitei78 – 781SubstrateBy similarity
Binding sitei79 – 791SubstrateBy similarity
Binding sitei98 – 981SubstrateBy similarity
Binding sitei145 – 1451SubstrateBy similarity
Active sitei173 – 1731Proton donorBy similarity
Binding sitei268 – 2681Substrate; via carbonyl oxygenBy similarity
Active sitei274 – 2741NucleophileBy similarity
Metal bindingi274 – 2741ZincBy similarity

GO - Molecular functioni

  1. amino acid binding Source: RGD
  2. dimethylargininase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine metabolic process Source: RGD
  2. citrulline metabolic process Source: UniProtKB
  3. positive regulation of angiogenesis Source: RGD
  4. positive regulation of nitric oxide biosynthetic process Source: RGD
  5. regulation of systemic arterial blood pressure Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.3.18. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (EC:3.5.3.18)
Short name:
DDAH-1
Short name:
Dimethylarginine dimethylaminohydrolase 1
Alternative name(s):
DDAHI
Dimethylargininase-1
Gene namesi
Name:Ddah1
Synonyms:Ddah
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi70968. Ddah1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrion Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 285284N(G),N(G)-dimethylarginine dimethylaminohydrolase 1PRO_0000171120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei222 – 2221S-nitrosocysteineBy similarity
Modified residuei274 – 2741S-nitrosocysteineBy similarity

Keywords - PTMi

Acetylation, S-nitrosylation

Proteomic databases

PaxDbiO08557.
PRIDEiO08557.

PTM databases

PhosphoSiteiO08557.

Expressioni

Tissue specificityi

Detected in red blood cells (at protein level). Widely distributed, high amounts found in kidney, brain, aorta and pancreas.1 Publication

Gene expression databases

GenevestigatoriO08557.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

MINTiMINT-4567619.
STRINGi10116.ENSRNOP00000044971.

Structurei

3D structure databases

ProteinModelPortaliO08557.
SMRiO08557. Positions 8-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DDAH family.Curated

Phylogenomic databases

eggNOGiCOG1834.
GeneTreeiENSGT00390000009331.
HOGENOMiHOG000161035.
HOVERGENiHBG055937.
InParanoidiO08557.
KOiK01482.
OMAiMAYPEYP.
OrthoDBiEOG73V6KV.
PhylomeDBiO08557.

Family and domain databases

InterProiIPR003198. Amidino_trans.
[Graphical view]
PfamiPF02274. Amidinotransf. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O08557-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGLSHPSVF GRATHAVVRA PPESLCRHAL RRSQGEEVDF ARAERQHQLY
60 70 80 90 100
VGVLGSKLGL QVVQLPADES LPDCVFVEDV AVVCEETALI TRPGAPSRRK
110 120 130 140 150
EVDMMKEALE KLQLNIVEMK DENATLDGGD VLFTGREFFV GLSKRTNQRG
160 170 180 190 200
AEILADTFKD YAVSTVPVAD SLHLKSFCSM AGPNLIAIGS SESAQKALKI
210 220 230 240 250
MQQMSDHRYD KLTVPDDMAA NCIYLNIPSK GHVLLHRTPE EYPESAKVYE
260 270 280
KLKDHLLIPV SNSEMEKVDG LLTCCSVFIN KKTDS
Length:285
Mass (Da):31,426
Last modified:January 22, 2007 - v3
Checksum:i9FE8DF56E37A7E4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86041 mRNA. Translation: BAA18993.1.
RefSeqiNP_071633.1. NM_022297.2.
UniGeneiRn.7398.

Genome annotation databases

EnsembliENSRNOT00000045016; ENSRNOP00000044971; ENSRNOG00000014613.
GeneIDi64157.
KEGGirno:64157.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86041 mRNA. Translation: BAA18993.1.
RefSeqiNP_071633.1. NM_022297.2.
UniGeneiRn.7398.

3D structure databases

ProteinModelPortaliO08557.
SMRiO08557. Positions 8-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4567619.
STRINGi10116.ENSRNOP00000044971.

Chemistry

BindingDBiO08557.
ChEMBLiCHEMBL4196.

PTM databases

PhosphoSiteiO08557.

Proteomic databases

PaxDbiO08557.
PRIDEiO08557.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000045016; ENSRNOP00000044971; ENSRNOG00000014613.
GeneIDi64157.
KEGGirno:64157.

Organism-specific databases

CTDi23576.
RGDi70968. Ddah1.

Phylogenomic databases

eggNOGiCOG1834.
GeneTreeiENSGT00390000009331.
HOGENOMiHOG000161035.
HOVERGENiHBG055937.
InParanoidiO08557.
KOiK01482.
OMAiMAYPEYP.
OrthoDBiEOG73V6KV.
PhylomeDBiO08557.

Enzyme and pathway databases

BRENDAi3.5.3.18. 5301.

Miscellaneous databases

NextBioi612794.
PROiO08557.

Gene expression databases

GenevestigatoriO08557.

Family and domain databases

InterProiIPR003198. Amidino_trans.
[Graphical view]
PfamiPF02274. Amidinotransf. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1996) [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 (MAR-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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiDDAH1_RAT
AccessioniPrimary (citable) accession number: O08557
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2000
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.