Reviewed, UniProtKB/Swiss-Prot P60334 (CDO1_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	200 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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

Keywords
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
PTM	Phosphoprotein Thioether bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	L-cysteine catabolic process to taurine Ref.1 Traceable author statement. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.1 Inferred from direct assay. Source: MGI
Molecular function	cysteine dioxygenase activity Ref.1 Traceable author statement. Source: MGI iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 200

200

Cysteine dioxygenase type 1

PRO_0000206607

Sites

Metal binding

86

1

Iron; catalytic

Metal binding

88

1

Iron; catalytic

Metal binding

140

1

Iron; catalytic

Amino acid modifications

Modified residue

59

1

Phosphothreonine By similarity

Cross-link

93 ↔ 157

3'-(S-cysteinyl)-tyrosine (Cys-Tyr)

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

200

Helix Strand Turn

Details...

Helix

12 – 22

11

Beta strand

24 – 27

4

Helix

30 – 39

10

Helix

44 – 47

4

Helix

48 – 50

3

Beta strand

55 – 57

3

Beta strand

59 – 64

6

Helix

66 – 68

3

Beta strand

71 – 77

7

Beta strand

92 – 100

9

Beta strand

102 – 107

6

Beta strand

121 – 125

5

Beta strand

130 – 133

4

Turn

135 – 137

3

Beta strand

139 – 143

5

Beta strand

151 – 159

9

Beta strand

162 – 167

6

Turn

169 – 171

3

Beta strand

174 – 178

5

Beta strand

182 – 184

3

Sequences

	Sequence		Length	Mass (Da)
	P60334-1 [UniParc]. Last modified February 16, 2004. Version 1. Checksum: 118F1A3326B340F9	FASTA	200	23,026
	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

References

	« Hide 'large scale' referencesShow '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. , 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

EMBLGenBankDDBJ

AF355472 , AF355469, AF355470, AF355471 Genomic DNA. Translation: AAK53364.1.
AK004249 mRNA. Translation: BAB23236.1.
AK149582 mRNA. Translation: BAE28973.1.
BC013638 mRNA. Translation: AAH13638.1.

RefSeq

NP_149026.1.

UniGene

Mm.241056

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ATF	X-ray	1.75	A	2-200	[»]
2Q4S	X-ray	1.75	A	2-200	[»]

ModBase

Search...

PTM databases

PhosphoSite

P60334.

2-D gel databases

REPRODUCTION-2DPAGE

P60334.

Genome annotation databases

Ensembl

ENSMUSG00000033022. Mus musculus. [Contig view]

GeneID

12583.

KEGG

mmu:12583.

Organism-specific databases

MGI

MGI:105925. Cdo1.

Phylogenomic databases

HOGENOM

P60334.

HOVERGEN

P60334.

Gene expression databases

ArrayExpress

P60334.

CleanEx

MM_CDO1.

GermOnline

ENSMUSG00000033022. Mus musculus.

Family and domain databases

InterPro

IPR010300. Cys_dOase_I.
[Graphical view]

Pfam

PF05995. CDO_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

281718.

SOURCE

Search...

Entry information

Entry name

CDO1_MOUSE

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)