P60334 (CDO1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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
Short name=CDO-I

Gene names

Name:

Cdo1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	200 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
PTM	Thioether bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-cysteine catabolic process to taurine Traceable author statement Ref.1. Source: MGI lactation Inferred from electronic annotation. Source: Compara response to amino acid stimulus Inferred from electronic annotation. Source: Compara response to cAMP Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to glucagon stimulus Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara taurine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytosol Inferred from direct assay Ref.1. Source: MGI plasma membrane Traceable author statement. Source: Reactome
Molecular_function	cysteine dioxygenase activity Traceable author statement Ref.1. Source: MGI ferrous iron binding Inferred from electronic annotation. Source: Compara
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

Cross-link

93 ↔ 157

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

Secondary structure

1

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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

112 – 114

3

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

IPI

IPI00134144.

RefSeq

NP_149026.1. NM_033037.3.

UniGene

Mm.241056.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P60334.

SMR

P60334. Positions 4-190.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000046517.

PTM databases

PhosphoSite

P60334.

2D gel databases

REPRODUCTION-2DPAGE

P60334.

Proteomic databases

PaxDb

P60334.

PRIDE

P60334.

Protocols and materials databases

DNASU

12583.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000035804; ENSMUSP00000046517; ENSMUSG00000033022.

GeneID

12583.

KEGG

mmu:12583.

UCSC

uc008evt.1. mouse.

Organism-specific databases

CTD

1036.

MGI

MGI:105925. Cdo1.

Phylogenomic databases

eggNOG

NOG126313.

GeneTree

ENSGT00390000018226.

HOGENOM

HOG000177818.

HOVERGEN

HBG004469.

InParanoid

P60334.

KO

K00456.

OMA

KVAYIND.

OrthoDB

EOG4W6NWZ.

Enzyme and pathway databases

Reactome

REACT_127416. Developmental Biology.

UniPathway

UPA00012; UER00537.

Gene expression databases

Bgee

P60334.

CleanEx

MM_CDO1.

Genevestigator

P60334.

GermOnline

ENSMUSG00000033022. Mus musculus.

Family and domain databases

Gene3D

2.60.120.10. 1 hit.

InterPro

IPR010300. Cys_dOase_I.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]

Pfam

PF05995. CDO_I. 1 hit.
[Graphical view]

SUPFAM

SSF51182. RmlC_like_cupin. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P60334.

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:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program