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UniProtKB/Swiss-Prot entry P60334


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

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Entry information
Entry name CDO1_MOUSE
Primary accession number P60334
Secondary accession number Q3UED8
Integrated into Swiss-Prot on February 16, 2004
Sequence was last modified on February 16, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 45)
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
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
DOI=10.1016/S0378-1119(01)00691-6; PubMed=11602353 [NCBI, ExPASy, EBI, Israel, Japan]
Hirschberger L.L., Daval S., Stover P.J., Stipanuk M.H.;
"Murine cysteine dioxygenase gene: structural organization, tissue-specific expression and promoter identification.";
Gene 277:153-161(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Liver;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Liver;
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 (1.75 ANGSTROMS) IN COMPLEX WITH NICKEL IONS, CROSS-LINK, AND SUBUNIT.
DOI=10.1073/pnas.0509262103; PubMed=16492780 [NCBI, ExPASy, EBI, Israel, Japan]
McCoy J.G., Bailey L.J., Bitto E., Bingman C.A., Aceti D.J., Fox B.G., Phillips G.N. Jr.;
"Structure and mechanism of mouse cysteine dioxygenase.";
Proc. Natl. Acad. Sci. U.S.A. 103:3084-3089(2006).
Comments
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
AF355472; AAK53364.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF355469; AAK53364.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF355470; AAK53364.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF355471; AAK53364.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK004249; BAB23236.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK149582; BAE28973.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013638; AAH13638.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_149026.1; -.
UniGene Mm.241056
3D structure databases
PDB
2ATF; X-ray; 1.75 A; A=2-200.[ExPASy / RCSB / EBI]
2Q4S; X-ray; 1.75 A; A=2-200.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2ATF; -.
2Q4S; -.
ModBase P60334.
PTM databases
PhosphoSite P60334; -.
2D gel databases
REPRODUCTION-2DPAGE P60334; -.
Organism-specific databases
MGI MGI:105925; Cdo1.
Gene expression databases
ArrayExpress P60334; -.
CleanEx MM_CDO1; -.
GermOnline ENSMUSG00000033022; Mus musculus.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from MGI).
GO:0017172; Molecular function: cysteine dioxygenase activity (traceable author statement from MGI).
GO:0019452; Biological process: L-cysteine catabolic process to taurine (traceable author statement from MGI).
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 P60334.
Genome annotation databases
Ensembl ENSMUSG00000033022; Mus musculus. [Contig view]
GeneID 12583; -.
KEGG mmu:12583; -.
Phylogenomic databases
HOGENOM P60334; -.
HOVERGEN P60334; -.
Other
SOURCE Cdo1; Mus musculus.
ProtoNet P60334.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phosphoprotein; Thioether bond.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   200  200     Cysteine dioxygenase type 1. PRO_0000206607
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). 
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 

P60334 in FASTA format

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