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P21816 (CDO1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Cysteine dioxygenase type 1

EC=1.13.11.20
Alternative name(s):
Cysteine dioxygenase type I
Short name=CDO
Short name=CDO-I
Gene names
Name:Cdo1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-cysteine + O2 = 3-sulfinoalanine.

Cofactor

Binds 1 iron ion per subunit.

Pathway

Organosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Subunit structure

Monomer.

Tissue specificity

Highest levels in liver. Significant expression also in kidney, lung and brain. Ref.2

Developmental stage

From neonate to weaning.

Induction

By increase of sulfur amino acid intake.

Post-translational modification

The thioether cross-link between Cys-93 and Tyr-157 plays a structural role through stabilizing the Fe2+ ion, and prevents the production of highly damaging free hydroxyl radicals by holding the oxygen radical via hydroxyl hydrogen.

Sequence similarities

Belongs to the cysteine dioxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200Cysteine dioxygenase type 1
PRO_0000206609

Sites

Metal binding861Iron; catalytic
Metal binding881Iron; catalytic
Metal binding1401Iron; catalytic

Amino acid modifications

Cross-link93 ↔ 1573'-(S-cysteinyl)-tyrosine (Cys-Tyr)

Experimental info

Sequence conflict891T → S in AAH70509. Ref.3

Secondary structure

........................................ 200
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21816 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 118F1A3326B340F9

FASTA20023,026
        10         20         30         40         50         60 
MERTELLKPR TLADLIRILH ELFAGDEVNV EEVQAVLEAY ESNPAEWALY AKFDQYRYTR 

        70         80         90        100        110        120 
NLVDQGNGKF NLMILCWGEG HGSSIHDHTD SHCFLKLLQG NLKETLFDWP DKKSNEMIKK 

       130        140        150        160        170        180 
SERTLRENQC AYINDSIGLH RVENVSHTEP AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT 

       190        200 
FHSKFGIRTP FTTSGSLENN 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a cDNA for rat liver cysteine dioxygenase."
Hosokawa Y., Matsumoto A., Oka J., Itakura H., Yamaguchi K.
Biochem. Biophys. Res. Commun. 168:473-478(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Structural organization and tissue-specific expression of the gene encoding rat cysteine dioxygenase."
Tsuboyama N., Hosokawa Y., Totani M., Oka J., Matsumoto A., Koide T., Kodama H.
Gene 181:161-165(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"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: Lung.
[4]"Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation."
Simmons C.R., Liu Q., Huang Q., Hao Q., Begley T.P., Karplus P.A., Stipanuk M.H.
J. Biol. Chem. 281:18723-18733(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH IRON, CROSS-LINK.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35266 mRNA. Translation: AAA40904.1.
D83481 Genomic DNA. Translation: BAA11925.1.
BC070509 mRNA. Translation: AAH70509.1.
PIRA34632.
RefSeqNP_434696.1. NM_052809.1.
UniGeneRn.2589.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B5HX-ray1.50A1-200[»]
2GH2X-ray1.50A1-200[»]
3ELNX-ray1.42A1-200[»]
4IEOX-ray1.55A1-200[»]
4IEPX-ray1.45A1-200[»]
4IEQX-ray1.40A1-200[»]
4IERX-ray1.45A1-200[»]
4IESX-ray1.40A1-200[»]
4IETX-ray1.40A1-200[»]
4IEUX-ray1.25A1-200[»]
4IEVX-ray1.60A1-200[»]
4IEWX-ray1.45A1-200[»]
4IEXX-ray2.15A1-200[»]
4IEYX-ray1.63A1-200[»]
4IEZX-ray1.39A1-200[»]
4JTNX-ray1.59A1-200[»]
4JTOX-ray2.00A1-200[»]
4KWJX-ray1.75A1-200[»]
4KWKX-ray1.95A1-200[»]
4KWLX-ray1.63A1-200[»]
ProteinModelPortalP21816.
SMRP21816. Positions 5-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000000172.

Protocols and materials databases

DNASU81718.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000000172; ENSRNOP00000000172; ENSRNOG00000000158.
GeneID81718.
KEGGrno:81718.
UCSCRGD:69262. rat.

Organism-specific databases

CTD1036.
RGD69262. Cdo1.

Phylogenomic databases

eggNOGNOG126313.
GeneTreeENSGT00390000018226.
HOGENOMHOG000177818.
HOVERGENHBG004469.
InParanoidP21816.
KOK00456.
OMAKMTFWSK.
OrthoDBEOG77M8PK.
PhylomeDBP21816.
TreeFamTF105636.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-8844.
SABIO-RKP21816.
UniPathwayUPA00012; UER00537.

Gene expression databases

GenevestigatorP21816.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR010300. Cys_dOase_I.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF05995. CDO_I. 1 hit.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP21816.
NextBio615363.
PROP21816.

Entry information

Entry nameCDO1_RAT
AccessionPrimary (citable) accession number: P21816
Secondary accession number(s): Q6NS32
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 107 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways