CDO1_MOUSE
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 03-AUG-2022, entry version 143.
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,
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: Catalyzes the oxidation of cysteine to cysteine sulfinic acid
CC with addition of molecular dioxygen. {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 -!- 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_033037.3.
DR PDB; 2ATF; X-ray; 1.75 A; A=2-200.
DR PDB; 2Q4S; X-ray; 1.75 A; A=2-200.
DR PDBsum; 2ATF; -.
DR PDBsum; 2Q4S; -.
DR AlphaFoldDB; P60334; -.
DR SMR; P60334; -.
DR IntAct; P60334; 1.
DR STRING; 10090.ENSMUSP00000046517; -.
DR iPTMnet; P60334; -.
DR PhosphoSitePlus; P60334; -.
DR SwissPalm; P60334; -.
DR REPRODUCTION-2DPAGE; P60334; -.
DR MaxQB; P60334; -.
DR PaxDb; P60334; -.
DR PeptideAtlas; P60334; -.
DR PRIDE; P60334; -.
DR ProteomicsDB; 279992; -.
DR Antibodypedia; 25433; 179 antibodies from 29 providers.
DR DNASU; 12583; -.
DR Ensembl; ENSMUST00000035804; ENSMUSP00000046517; ENSMUSG00000033022.
DR GeneID; 12583; -.
DR KEGG; mmu:12583; -.
DR UCSC; uc008evt.1; mouse.
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; WPDRKSH; -.
DR OrthoDB; 1516232at2759; -.
DR PhylomeDB; P60334; -.
DR TreeFam; TF105636; -.
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 73 CRISPR screens.
DR ChiTaRS; Cdo1; mouse.
DR EvolutionaryTrace; P60334; -.
DR PRO; PR:P60334; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P60334; protein.
DR Bgee; ENSMUSG00000033022; Expressed in seminal vesicle and 241 other tissues.
DR ExpressionAtlas; P60334; baseline and differential.
DR Genevisible; P60334; MM.
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:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0019448; P:L-cysteine catabolic process; ISO:MGI.
DR GO; GO:0019452; P:L-cysteine catabolic process to taurine; TAS:MGI.
DR GO; GO:0007595; P:lactation; ISO:MGI.
DR GO; GO:0043200; P:response to amino acid; ISO:MGI.
DR GO; GO:0051591; P:response to cAMP; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR GO; GO:0033762; P:response to glucagon; ISO:MGI.
DR GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
DR GO; GO:0010243; P:response to organonitrogen compound; ISO:MGI.
DR GO; GO:0042412; P:taurine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019530; P:taurine metabolic process; TAS:MGI.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR010300; CDO_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR12918; PTHR12918; 1.
DR Pfam; PF05995; CDO_I; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Thioether bond.
FT CHAIN 1..200
FT /note="Cysteine dioxygenase type 1"
FT /id="PRO_0000206607"
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 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16492780"
FT CROSSLNK 93..157
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000269|PubMed:16492780"
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 STRAND 112..114
FT /evidence="ECO:0007829|PDB:2Q4S"
FT STRAND 121..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
