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Reviewed, UniProtKB/Swiss-Prot P60334 (CDO1_MOUSE)

Last modified November 25, 2008. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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-I
      Short name=CDO
Gene names
Name: Cdo1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

L-cysteine + O(2) = 3-sulfinoalanine.

Cofactor

Binds 1 iron ion per subunit. Nickel and zinc to a lesser extent.

Pathway

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

Subunit structure

Monomer.

Tissue specificity

Highest expression in liver. Also expressed in kidney, lung, brain and small intestine.

Post-translational modification

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.

Sequence similarities

Belongs to the cysteine dioxygenase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200Cysteine dioxygenase type 1
PRO_0000206607

Sites

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

Amino acid modifications

Modified residue591Phosphothreonine By similarity
Cross-link93 ↔ 1573'-(S-cysteinyl)-tyrosine (Cys-Tyr)

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P60334-1 [UniParc].

Last modified February 16, 2004. 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]"Murine cysteine dioxygenase gene: structural organization, tissue-specific expression and promoter identification."
Hirschberger L.L., Daval S., Stover P.J., Stipanuk M.H.
Gene 277:153-161(2001) [PubMed: 11602353] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[4]"Structure and mechanism of mouse cysteine dioxygenase."
McCoy J.G., Bailey L.J., Bitto E., Bingman C.A., Aceti D.J., Fox B.G., Phillips G.N. Jr.
Proc. Natl. Acad. Sci. U.S.A. 103:3084-3089(2006) [PubMed: 16492780] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NICKEL IONS, CROSS-LINK, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF355472 expand/collapse EMBL AC list , AF355469, AF355470, AF355471 Genomic DNA. Translation: AAK53364.1.
AK004249 mRNA. Translation: BAB23236.1.
AK149582 mRNA. Translation: BAE28973.1.
BC013638 mRNA. Translation: AAH13638.1.
RefSeqNP_149026.1.
UniGeneMm.241056

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2ATFX-ray1.75A2-200[»]
2Q4SX-ray1.75A2-200[»]
ModBaseSearch...

PTM databases

PhosphoSiteP60334.

2-D gel databases

REPRODUCTION-2DPAGEP60334.

Genome annotation databases

EnsemblENSMUSG00000033022. Mus musculus. [Contig view]
GeneID12583.
KEGGmmu:12583.

Organism-specific databases

MGIMGI:105925. Cdo1.

Phylogenomic databases

HOGENOMP60334.
HOVERGENP60334.

Gene expression databases

ArrayExpressP60334.
CleanExMM_CDO1.
GermOnlineENSMUSG00000033022. Mus musculus.

Family and domain databases

InterProIPR010300. Cys_dOase_I.
[Graphical view]
PfamPF05995. CDO_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio281718.
SOURCESearch...

Entry information

Entry nameCDO1_MOUSE
AccessionPrimary (citable) accession number: P60334
Secondary accession number(s): Q3UED8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: February 16, 2004
Last modified: November 25, 2008
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents