ID   CDO1_MOUSE              Reviewed;         200 AA.
AC   P60334; Q3UED8;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   02-SEP-2026, entry version 161.
DE   RecName: Full=Cysteine dioxygenase type 1;
DE            EC=1.13.11.20 {ECO:0000269|PubMed:16492780};
DE   AltName: Full=Cysteine dioxygenase type I;
DE            Short=CDO;
DE            Short=CDO-I;
GN   Name=Cdo1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=11602353; DOI=10.1016/s0378-1119(01)00691-6;
RA   Hirschberger L.L., Daval S., Stover P.J., Stipanuk M.H.;
RT   "Murine cysteine dioxygenase gene: structural organization, tissue-specific
RT   expression and promoter identification.";
RL   Gene 277:153-161(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NICKEL IONS,
RP   CROSS-LINK, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PTM, AND IRON-BINDING SITES.
RX   PubMed=16492780; DOI=10.1073/pnas.0509262103;
RA   McCoy J.G., Bailey L.J., Bitto E., Bingman C.A., Aceti D.J., Fox B.G.,
RA   Phillips G.N. Jr.;
RT   "Structure and mechanism of mouse cysteine dioxygenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3084-3089(2006).
CC   -!- FUNCTION: Rate-limiting enzyme of the cysteine catabolic process to
CC       taurine, which catalyzes the oxidation of cysteine to cysteine sulfinic
CC       acid with addition of molecular dioxygen.
CC       {ECO:0000269|PubMed:16492780}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteine + O2 = 3-sulfino-L-alanine + H(+);
CC         Xref=Rhea:RHEA:20441, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:61085; EC=1.13.11.20;
CC         Evidence={ECO:0000269|PubMed:16492780};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20442;
CC         Evidence={ECO:0000305|PubMed:16492780};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:16492780};
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000269|PubMed:16492780};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:16492780};
CC       Note=Binds 1 Fe(2+) cation per subunit. Ni(2+) and Zn(2+) can be used
CC       to a lesser extent. {ECO:0000269|PubMed:16492780};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.4 mM for L-cysteine {ECO:0000269|PubMed:16492780};
CC   -!- PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine
CC       from L-cysteine: step 1/2.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16492780}.
CC   -!- TISSUE SPECIFICITY: Highest expression in liver. Also expressed in
CC       kidney, lung, brain and small intestine. {ECO:0000269|PubMed:11602353}.
CC   -!- PTM: The thioether cross-link between Cys-93 and Tyr-157 plays a
CC       structural role through stabilizing the Fe(2+) ion, and prevents the
CC       production of highly damaging free hydroxyl radicals by holding the
CC       oxygen radical via hydroxyl hydrogen. {ECO:0000269|PubMed:16492780}.
CC   -!- PTM: Ubiquitinated and degraded by the ECS(LRRC58) complex, leading to
CC       its degradation. L-cysteine abundance regulates ECS(LRRC58)-mediated
CC       ubiquitination of CDO1: the complex promotes ubiquitination and
CC       degradation of CDO1 in presence of high level of cysteine, but not when
CC       cysteine abundance is low. {ECO:0000250|UniProtKB:Q16878}.
CC   -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}.
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DR   EMBL; AF355472; AAK53364.1; -; Genomic_DNA.
DR   EMBL; AF355469; AAK53364.1; JOINED; Genomic_DNA.
DR   EMBL; AF355470; AAK53364.1; JOINED; Genomic_DNA.
DR   EMBL; AF355471; AAK53364.1; JOINED; Genomic_DNA.
DR   EMBL; AK004249; BAB23236.1; -; mRNA.
DR   EMBL; AK149582; BAE28973.1; -; mRNA.
DR   EMBL; BC013638; AAH13638.1; -; mRNA.
DR   CCDS; CCDS29234.1; -.
DR   RefSeq; NP_149026.1; NM_033037.4.
DR   PDB; 2ATF; X-ray; 1.75 A; A=2-200.
DR   PDB; 2Q4S; X-ray; 1.75 A; A=2-200.
DR   AlphaFoldDB; P60334; -.
DR   SMR; P60334; -.
DR   FunCoup; P60334; 289.
DR   IntAct; P60334; 1.
DR   STRING; 10090.ENSMUSP00000046517; -.
DR   iPTMnet; P60334; -.
DR   PhosphoSitePlus; P60334; -.
DR   SwissPalm; P60334; -.
DR   REPRODUCTION-2DPAGE; P60334; -.
DR   jPOST; P60334; -.
DR   PaxDb; 10090-ENSMUSP00000046517; -.
DR   PeptideAtlas; P60334; -.
DR   ProteomicsDB; 279992; -.
DR   Antibodypedia; 25433; 167 antibodies from 29 providers.
DR   DNASU; 12583; -.
DR   Ensembl; ENSMUST00000035804.9; ENSMUSP00000046517.8; ENSMUSG00000033022.9.
DR   GeneID; 12583; -.
DR   KEGG; mmu:12583; -.
DR   UCSC; uc008evt.1; mouse.
DR   AGR; MGI:105925; -.
DR   CTD; 1036; -.
DR   MGI; MGI:105925; Cdo1.
DR   VEuPathDB; HostDB:ENSMUSG00000033022; -.
DR   eggNOG; KOG4064; Eukaryota.
DR   GeneTree; ENSGT00390000018226; -.
DR   HOGENOM; CLU_079443_1_0_1; -.
DR   InParanoid; P60334; -.
DR   OMA; YTENQVT; -.
DR   OrthoDB; 543511at2759; -.
DR   PhylomeDB; P60334; -.
DR   BRENDA; 1.13.11.20; 3474.
DR   Reactome; R-MMU-1614558; Degradation of cysteine and homocysteine.
DR   UniPathway; UPA00012; UER00537.
DR   BioGRID-ORCS; 12583; 3 hits in 78 CRISPR screens.
DR   EvolutionaryTrace; P60334; -.
DR   PRO; PR:P60334; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; P60334; protein.
DR   Bgee; ENSMUSG00000033022; Expressed in seminal vesicle and 243 other cell types or tissues.
DR   ExpressionAtlas; P60334; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0017172; F:cysteine dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR   GO; GO:0016151; F:nickel cation binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0019448; P:L-cysteine catabolic process; ISO:GO_Central.
DR   GO; GO:0007595; P:lactation; ISO:GO_Central.
DR   GO; GO:0043200; P:response to amino acid; ISO:GO_Central.
DR   GO; GO:0097184; P:response to azide; ISO:GO_Central.
DR   GO; GO:0051591; P:response to cAMP; ISO:GO_Central.
DR   GO; GO:0045471; P:response to ethanol; ISO:GO_Central.
DR   GO; GO:0033762; P:response to glucagon; ISO:GO_Central.
DR   GO; GO:0051384; P:response to glucocorticoid; ISO:GO_Central.
DR   GO; GO:0042412; P:taurine biosynthetic process; IMP:FlyBase.
DR   GO; GO:0019530; P:taurine metabolic process; TAS:MGI.
DR   CDD; cd10548; cupin_CDO; 1.
DR   FunFam; 2.60.120.10:FF:000045; Cysteine dioxygenase 1; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR010300; CDO_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR12918; CYSTEINE DIOXYGENASE; 1.
DR   PANTHER; PTHR12918:SF1; CYSTEINE DIOXYGENASE TYPE 1; 1.
DR   Pfam; PF05995; CDO_I; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   PDBsum; 2ATF; -.
DR   PDBsum; 2Q4S; -.
PE   1: Evidence at protein level;
KW   3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome; Thioether bond; Ubl conjugation.
FT   CHAIN           1..200
FT                   /note="Cysteine dioxygenase type 1"
FT                   /id="PRO_0000206607"
FT   BINDING         34
FT                   /ligand="L-cysteine"
FT                   /ligand_id="ChEBI:CHEBI:35235"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         58
FT                   /ligand="L-cysteine"
FT                   /ligand_id="ChEBI:CHEBI:35235"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         60
FT                   /ligand="L-cysteine"
FT                   /ligand_id="ChEBI:CHEBI:35235"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         86
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:16492780"
FT   BINDING         88
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:16492780"
FT   BINDING         123
FT                   /ligand="L-cysteine"
FT                   /ligand_id="ChEBI:CHEBI:35235"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         129
FT                   /ligand="L-cysteine"
FT                   /ligand_id="ChEBI:CHEBI:35235"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         132
FT                   /ligand="L-cysteine"
FT                   /ligand_id="ChEBI:CHEBI:35235"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         140
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:16492780"
FT   BINDING         157
FT                   /ligand="L-cysteine"
FT                   /ligand_id="ChEBI:CHEBI:35235"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   CROSSLNK        93..157
FT                   /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT                   /evidence="ECO:0000269|PubMed:16492780"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   HELIX           12..22
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          24..27
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   HELIX           30..39
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   HELIX           44..47
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          71..77
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          92..100
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          102..107
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:2Q4S"
FT   STRAND          119..125
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          130..133
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   TURN            135..137
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          139..143
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          151..159
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          162..167
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   TURN            169..171
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          174..178
FT                   /evidence="ECO:0007829|PDB:2ATF"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:2ATF"
SQ   SEQUENCE   200 AA;  23026 MW;  118F1A3326B340F9 CRC64;
     MERTELLKPR TLADLIRILH ELFAGDEVNV EEVQAVLEAY ESNPAEWALY AKFDQYRYTR
     NLVDQGNGKF NLMILCWGEG HGSSIHDHTD SHCFLKLLQG NLKETLFDWP DKKSNEMIKK
     SERTLRENQC AYINDSIGLH RVENVSHTEP AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT
     FHSKFGIRTP FTTSGSLENN
//