[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Liver; DOI=10.1016/0006-291X(90)92345-Z; PubMed=2334417 [NCBI, ExPASy, EBI, Israel, Japan] Hosokawa Y., Matsumoto A., Oka J., Itakura H., Yamaguchi K.; "Isolation and characterization of a cDNA for rat liver cysteine dioxygenase."; Biochem. Biophys. Res. Commun. 168:473-478(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. STRAIN=Sprague-Dawley; TISSUE=Liver; DOI=10.1016/S0378-1119(96)00496-9; PubMed=8973325 [NCBI, ExPASy, EBI, Israel, Japan] Tsuboyama N., Hosokawa Y., Totani M., Oka J., Matsumoto A., Koide T., Kodama H.; "Structural organization and tissue-specific expression of the gene encoding rat cysteine dioxygenase."; Gene 181:161-165(1996).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH IRON, AND CROSS-LINK. DOI=10.1074/jbc.M601555200; PubMed=16611640 [NCBI, ExPASy, EBI, Israel, Japan] Simmons C.R., Liu Q., Huang Q., Hao Q., Begley T.P., Karplus P.A., Stipanuk M.H.; "Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation."; J. Biol. Chem. 281:18723-18733(2006).

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: Monomer.
TISSUE SPECIFICITY: Highest levels in liver. Significant expression also in kidney, lung and brain.
DEVELOPMENTAL STAGE: From neonate to weaning.
INDUCTION: By increase of sulfur amino acid intake.
PTM: The thioether cross-link between Cys-93 and Tyr-157 plays a structural role through stabilizing the ferrous ion, and prevents the production of highly damaging free hydroxyl radicals by holding the oxygen radical via hydroxyl hydrogen.
SIMILARITY: Belongs to the cysteine dioxygenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M35266; AAA40904.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D83481; BAA11925.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070509; AAH70509.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A34632; A34632.

NP_434696.1; -.

3D structure databases

PDB

2B5H; X-ray; 1.50 A; A=1-200.	[ExPASy / RCSB / EBI]
2GH2; X-ray; 1.50 A; A=1-200.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2B5H; -.
2GH2; -.

ModBase

P21816.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-8844; -.

Organism-specific databases

RGD

69262; Cdo1.

Gene expression databases

ArrayExpress

P21816; -.

GermOnline

ENSRNOG00000000158; Rattus norvegicus.

Ontologies

GO:0017172;	Molecular function: cysteine dioxygenase activity (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR010300; Cys_dOase_I.
Graphical view of domain structure.

Pfam

PF05995; CDO_I; 1.
Pfam graphical view of domain structure.

BLOCKS

P21816.

Genome annotation databases

Ensembl

ENSRNOG00000000158; Rattus norvegicus. [Contig view]

GeneID

81718; -.

KEGG

rno:81718; -.

Phylogenomic databases

HOVERGEN

P21816; -.

Other

ProtoNet

P21816.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Dioxygenase; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase; Phosphoprotein; Thioether bond.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 200`	`200`	`Cysteine dioxygenase type 1.`	`PRO_0000206609`
`METAL`	`86 86`		`Iron; catalytic.`
`METAL`	`88 88`		`Iron; catalytic.`
`METAL`	`140 140`		`Iron; catalytic.`
`MOD_RES`	`59 59`		`Phosphothreonine (By similarity).`
`CROSSLNK`	`93 157`		`3'-(S-cysteinyl)-tyrosine (Cys-Tyr).`
`CONFLICT`	`89 89`		`T -> S (in Ref. 3; AAH70509).`
`HELIX`	`12 22`	`11`
`STRAND`	`24 27`	`4`
`HELIX`	`30 39`	`10`
`HELIX`	`44 47`	`4`
`HELIX`	`48 50`	`3`
`STRAND`	`55 57`	`3`
`STRAND`	`59 64`	`6`
`HELIX`	`66 68`	`3`
`STRAND`	`71 77`	`7`
`STRAND`	`92 100`	`9`
`STRAND`	`102 107`	`6`
`STRAND`	`121 125`	`5`
`STRAND`	`130 133`	`4`
`TURN`	`135 137`	`3`
`STRAND`	`139 143`	`5`
`STRAND`	`151 159`	`9`
`STRAND`	`162 167`	`6`
`TURN`	`169 171`	`3`
`STRAND`	`174 178`	`5`
`STRAND`	`182 184`	`3`

Sequence information

Length: 200 AA [This is the length of the unprocessed precursor]

Molecular weight: 23026 Da [This is the MW of the unprocessed precursor]

CRC64: 118F1A3326B340F9 [This is a checksum on the sequence]

        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

P21816 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools