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P60334

- CDO1_MOUSE

UniProt

P60334 - CDO1_MOUSE

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Protein
Cysteine dioxygenase type 1
Gene
Cdo1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-cysteine + O2 = 3-sulfinoalanine.

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi86 – 861Iron; catalytic
Metal bindingi88 – 881Iron; catalytic
Metal bindingi140 – 1401Iron; catalytic

GO - Molecular functioni

  1. cysteine dioxygenase activity Source: MGI
  2. ferrous iron binding Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. L-cysteine catabolic process to taurine Source: MGI
  2. lactation Source: Ensembl
  3. response to amino acid Source: Ensembl
  4. response to cAMP Source: Ensembl
  5. response to ethanol Source: Ensembl
  6. response to glucagon Source: Ensembl
  7. response to glucocorticoid Source: Ensembl
  8. taurine biosynthetic process Source: UniProtKB-UniPathway
  9. taurine metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198964. Degradation of cysteine and homocysteine.
UniPathwayiUPA00012; UER00537.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Cdo1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:105925. Cdo1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: MGI
  2. plasma membrane Source: Reactome
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 200200Cysteine dioxygenase type 1
PRO_0000206607Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki93 ↔ 1573'-(S-cysteinyl)-tyrosine (Cys-Tyr)

Post-translational modificationi

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.

Keywords - PTMi

Thioether bond

Proteomic databases

MaxQBiP60334.
PaxDbiP60334.
PRIDEiP60334.

2D gel databases

REPRODUCTION-2DPAGEP60334.

PTM databases

PhosphoSiteiP60334.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP60334.
CleanExiMM_CDO1.
GenevestigatoriP60334.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000046517.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 2211
Beta strandi24 – 274
Helixi30 – 3910
Helixi44 – 474
Helixi48 – 503
Beta strandi55 – 573
Beta strandi59 – 646
Helixi66 – 683
Beta strandi71 – 777
Beta strandi92 – 1009
Beta strandi102 – 1076
Beta strandi112 – 1143
Beta strandi121 – 1255
Beta strandi130 – 1334
Turni135 – 1373
Beta strandi139 – 1435
Beta strandi151 – 1599
Beta strandi162 – 1676
Turni169 – 1713
Beta strandi174 – 1785
Beta strandi182 – 1843

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ATFX-ray1.75A2-200[»]
2Q4SX-ray1.75A2-200[»]
ProteinModelPortaliP60334.
SMRiP60334. Positions 5-190.

Miscellaneous databases

EvolutionaryTraceiP60334.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG126313.
GeneTreeiENSGT00390000018226.
HOGENOMiHOG000177818.
HOVERGENiHBG004469.
InParanoidiP60334.
KOiK00456.
OMAiKMTFWSK.
OrthoDBiEOG77M8PK.
PhylomeDBiP60334.
TreeFamiTF105636.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR010300. Cys_dOase_I.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF05995. CDO_I. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

P60334-1 [UniParc]FASTAAdd to Basket

« Hide

MERTELLKPR TLADLIRILH ELFAGDEVNV EEVQAVLEAY ESNPAEWALY    50
AKFDQYRYTR NLVDQGNGKF NLMILCWGEG HGSSIHDHTD SHCFLKLLQG 100
NLKETLFDWP DKKSNEMIKK SERTLRENQC AYINDSIGLH RVENVSHTEP 150
AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT FHSKFGIRTP FTTSGSLENN 200
Length:200
Mass (Da):23,026
Last modified:February 16, 2004 - v1
Checksum:i118F1A3326B340F9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF355472
, AF355469, AF355470, AF355471 Genomic DNA. Translation: AAK53364.1.
AK004249 mRNA. Translation: BAB23236.1.
AK149582 mRNA. Translation: BAE28973.1.
BC013638 mRNA. Translation: AAH13638.1.
CCDSiCCDS29234.1.
RefSeqiNP_149026.1. NM_033037.3.
UniGeneiMm.241056.

Genome annotation databases

EnsembliENSMUST00000035804; ENSMUSP00000046517; ENSMUSG00000033022.
GeneIDi12583.
KEGGimmu:12583.
UCSCiuc008evt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF355472
, AF355469 , AF355470 , AF355471 Genomic DNA. Translation: AAK53364.1 .
AK004249 mRNA. Translation: BAB23236.1 .
AK149582 mRNA. Translation: BAE28973.1 .
BC013638 mRNA. Translation: AAH13638.1 .
CCDSi CCDS29234.1.
RefSeqi NP_149026.1. NM_033037.3.
UniGenei Mm.241056.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ATF X-ray 1.75 A 2-200 [» ]
2Q4S X-ray 1.75 A 2-200 [» ]
ProteinModelPortali P60334.
SMRi P60334. Positions 5-190.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000046517.

PTM databases

PhosphoSitei P60334.

2D gel databases

REPRODUCTION-2DPAGE P60334.

Proteomic databases

MaxQBi P60334.
PaxDbi P60334.
PRIDEi P60334.

Protocols and materials databases

DNASUi 12583.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035804 ; ENSMUSP00000046517 ; ENSMUSG00000033022 .
GeneIDi 12583.
KEGGi mmu:12583.
UCSCi uc008evt.1. mouse.

Organism-specific databases

CTDi 1036.
MGIi MGI:105925. Cdo1.

Phylogenomic databases

eggNOGi NOG126313.
GeneTreei ENSGT00390000018226.
HOGENOMi HOG000177818.
HOVERGENi HBG004469.
InParanoidi P60334.
KOi K00456.
OMAi KMTFWSK.
OrthoDBi EOG77M8PK.
PhylomeDBi P60334.
TreeFami TF105636.

Enzyme and pathway databases

UniPathwayi UPA00012 ; UER00537 .
Reactomei REACT_198964. Degradation of cysteine and homocysteine.

Miscellaneous databases

EvolutionaryTracei P60334.
NextBioi 281718.
PROi P60334.
SOURCEi Search...

Gene expression databases

Bgeei P60334.
CleanExi MM_CDO1.
Genevestigatori P60334.

Family and domain databases

Gene3Di 2.60.120.10. 1 hit.
InterProi IPR010300. Cys_dOase_I.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view ]
Pfami PF05995. CDO_I. 1 hit.
[Graphical view ]
SUPFAMi SSF51182. SSF51182. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NICKEL IONS, CROSS-LINK, SUBUNIT.

Entry informationi

Entry nameiCDO1_MOUSE
AccessioniPrimary (citable) accession number: P60334
Secondary accession number(s): Q3UED8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: February 16, 2004
Last modified: September 3, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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