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UniProtKB/Swiss-Prot entry Q16878


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CDO1_HUMAN
Primary accession number Q16878
Secondary accession numbers P78513 Q6FHZ8 Q8TB64
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on September 27, 2005 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 67)
Name and origin of the protein
Protein name Cysteine dioxygenase type 1
Synonyms EC 1.13.11.20
Cysteine dioxygenase type I
CDO-I
CDO
Gene name
Name: CDO1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-45.
TISSUE=Liver;
DOI=10.1016/0167-4838(94)90144-9; PubMed=7524679 [NCBI, ExPASy, EBI, Israel, Japan]
McCann K.P., Akbari M.T., Williams A.C., Ramsden D.B.;
"Human cysteine dioxygenase type I: primary structure derived from base sequencing of cDNA.";
Biochim. Biophys. Acta 1209:107-110(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10427686 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuboyama-Kasaoka N., Hosokawa Y., Kodama H., Matsumoto A., Oka J., Totani M.;
"Human cysteine dioxygenase gene: structural organization, tissue-specific expression and downregulation by phorbol 12-myristate 13-acetate.";
Biosci. Biotechnol. Biochem. 63:1017-1024(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-45.
PubMed=9497919 [NCBI, ExPASy, EBI, Israel, Japan]
Ramsden D.B., Kapadi A.L., Fitch N.J., Farmer M.J., Bennett P., Williams A.C.;
"Human cysteine dioxygenase type I (CDO-I; EC 1.13.11.20): 5' flanking region and intron-exon structure of the gene.";
Mol. Pathol. 50:269-271(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[7]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-200 OF WILD-TYPE AND MUTANTS ARG-60; CYS-93; TYR-157 AND CYS-164 IN COMPLEX WITH L-CYSTEINE AND DIVALENT METAL IONS, CROSS-LINK, SUBUNIT, AND MASS SPECTROMETRY.
DOI=10.1074/jbc.M609337200; PubMed=17135237 [NCBI, ExPASy, EBI, Israel, Japan]
Ye S., Wu X., Wei L., Tang D., Sun P., Bartlam M., Rao Z.;
"An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor.";
J. Biol. Chem. 282:3391-3402(2007).
[8]
VARIANT [LARGE SCALE ANALYSIS] GLN-143.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
  • FUNCTION: Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations. Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range.
  • CATALYTIC ACTIVITY: L-cysteine + O2 = 3-sulfinoalanine.
  • COFACTOR: Binds 1 iron ion per subunit. Zinc to a much lesser extent.
  • PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.
  • SUBUNIT: Monomer.
  • TISSUE SPECIFICITY: Highly expressed in liver and placenta. Low expression in heart, brain and pancreas. Also detected in hepatoblastoma HepG2 cells.
  • INDUCTION: In hepatoblastoma HepG2 cells, down-regulated by phorbol 12-myristate 13-acetate.
  • 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
Z31357; CAA83234.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z23010; CAA80552.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D85782; BAA12873.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D85777; BAA12872.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U80055; AAB58352.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U60232; AAB58352.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U78979; AAB58352.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR536540; CAG38777.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024241; AAH24241.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S50192; S50192.
RefSeq NP_001792.2; -.
UniGene Hs.442378
3D structure databases
PDB
2IC1; X-ray; 2.70 A; A=2-200.[ExPASy / RCSB / EBI]
PDBsum 2IC1; -.
ModBase Q16878.
PTM databases
PhosphoSite Q16878; -.
Organism-specific databases
HGNC HGNC:1795; CDO1.
GenAtlas CDO1.
MIM 603943; gene. [NCBI / EBI]
PharmGKB PA26327; -.
GeneCards Q16878.
Gene expression databases
ArrayExpress Q16878; -.
CleanEx HS_CDO1; -.
GermOnline ENSG00000129596; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from UniProtKB).
GO:0017172; Molecular function: cysteine dioxygenase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006534; Biological process: cysteine metabolic process (traceable author statement from UniProtKB).
GO:0006954; Biological process: inflammatory response (traceable author statement from UniProtKB).
GO:0055114; Biological process: oxidation reduction (traceable author statement from UniProtKB).
GO:0000097; Biological process: sulfur amino acid biosynthetic process (traceable author statement from UniProtKB).
GO:0042412; Biological process: taurine biosynthetic process (traceable author statement 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 Q16878.
Genome annotation databases
Ensembl ENSG00000129596; Homo sapiens. [Contig view]
GeneID 1036; -.
KEGG hsa:1036; -.
Phylogenomic databases
HOGENOM Q16878; -.
HOVERGEN Q16878; -.
Other
DrugBank DB00151; L-Cysteine.
DB00157; NADH.
SOURCE CDO1; Homo sapiens.
ProtoNet Q16878.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phosphoprotein; Polymorphism; Thioether bond.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   200  200     Cysteine dioxygenase type 1. PRO_0000206606
METAL   86    86        Iron; catalytic. 
METAL   88    88        Iron; catalytic. 
METAL   140   140        Iron; catalytic. 
MOD_RES   59    59        Phosphothreonine. 
CROSSLNK   93   157        3'-(S-cysteinyl)-tyrosine (Cys-Tyr). 
VARIANT   45    45  1     T -> I (in dbSNP:rs1042867 [NCBI]). VAR_023536 [3D]
VARIANT   143   143  1     E -> Q (in a colorectal cancer sample; somatic mutation). VAR_036170 [3D]
MUTAGEN   60    60        R->Q: Reduces enzyme activity by 70%. Reduces iron and zinc incorporation by 50%. 
MUTAGEN   93    93        C->S: Reduces enzyme activity and iron incorporation by 50%. Zinc incorporation increased by 20%. 
MUTAGEN   157   157        Y->F: Almost total loss of enzyme activity and iron incorporation. Reduces zinc incorporation by 20%. 
MUTAGEN   164   164        C->S: Reduces enzyme activity by 20%. Little effect on iron incorporation. No effect on zinc incorporation. 
CONFLICT   137   137        I -> V (in Ref. 5; AAH24241). 
HELIX   12    22  11      
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   119   124  6      
STRAND   130   133  4      
TURN   135   137  3      
STRAND   139   144  6      
STRAND   147   149  3      
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: 22972 Da [This is the MW of the unprocessed precursor] CRC64: E4EF87221D05C14D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEQTEVLKPR TLADLIRILH QLFAGDEVNV EEVQAIMEAY ESDPTEWAMY AKFDQYRYTR 

        70         80         90        100        110        120 
NLVDQGNGKF NLMILCWGEG HGSSIHDHTN SHCFLKMLQG NLKETLFAWP DKKSNEMVKK 

       130        140        150        160        170        180 
SERVLRENQC AYINDSIGLH RVENISHTEP AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT 

       190        200 
FHSKFGIRTP NATSGSLENN 

Q16878 in FASTA format

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