Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P60334 (CDO1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Nickel and zinc to a lesser extent.

Pathway

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

Subunit structure

Monomer. Ref.4

Tissue specificity

Highest expression in liver. Also expressed in kidney, lung, brain and small intestine. Ref.1

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_0000206607

Sites

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

Amino acid modifications

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P60334 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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

EMBL
GenBank
DDBJ
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.
CCDSCCDS29234.1.
RefSeqNP_149026.1. NM_033037.3.
UniGeneMm.241056.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ATFX-ray1.75A2-200[»]
2Q4SX-ray1.75A2-200[»]
ProteinModelPortalP60334.
SMRP60334. Positions 5-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000046517.

PTM databases

PhosphoSiteP60334.

2D gel databases

REPRODUCTION-2DPAGEP60334.

Proteomic databases

MaxQBP60334.
PaxDbP60334.
PRIDEP60334.

Protocols and materials databases

DNASU12583.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035804; ENSMUSP00000046517; ENSMUSG00000033022.
GeneID12583.
KEGGmmu:12583.
UCSCuc008evt.1. mouse.

Organism-specific databases

CTD1036.
MGIMGI:105925. Cdo1.

Phylogenomic databases

eggNOGNOG126313.
GeneTreeENSGT00390000018226.
HOGENOMHOG000177818.
HOVERGENHBG004469.
InParanoidP60334.
KOK00456.
OMAKMTFWSK.
OrthoDBEOG77M8PK.
PhylomeDBP60334.
TreeFamTF105636.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.
UniPathwayUPA00012; UER00537.

Gene expression databases

BgeeP60334.
CleanExMM_CDO1.
GenevestigatorP60334.

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

EvolutionaryTraceP60334.
NextBio281718.
PROP60334.
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: July 9, 2014
This is version 95 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

MGD cross-references

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