ID CDO1_RAT Reviewed; 200 AA. AC P21816; Q6NS32; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 24-JAN-2024, entry version 160. DE RecName: Full=Cysteine dioxygenase type 1; DE EC=1.13.11.20 {ECO:0000269|PubMed:9824269}; DE AltName: Full=Cysteine dioxygenase type I; DE Short=CDO; DE Short=CDO-I; GN Name=Cdo1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RX PubMed=2334417; DOI=10.1016/0006-291x(90)92345-z; RA Hosokawa Y., Matsumoto A., Oka J., Itakura H., Yamaguchi K.; RT "Isolation and characterization of a cDNA for rat liver cysteine RT dioxygenase."; RL Biochem. Biophys. Res. Commun. 168:473-478(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX PubMed=8973325; DOI=10.1016/s0378-1119(96)00496-9; RA Tsuboyama N., Hosokawa Y., Totani M., Oka J., Matsumoto A., Koide T., RA Kodama H.; RT "Structural organization and tissue-specific expression of the gene RT encoding rat cysteine dioxygenase."; RL Gene 181:161-165(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=9824269; DOI=10.1016/s0168-8278(98)80155-4; RA Parsons R.B., Ramsden D.B., Waring R.H., Barber P.C., Williams A.C.; RT "Hepatic localisation of rat cysteine dioxygenase."; RL J. Hepatol. 29:595-602(1998). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH IRON, CROSS-LINK, RP SUBUNIT, COFACTOR, PTM, AND IRON-BINDING SITES. RX PubMed=16611640; DOI=10.1074/jbc.m601555200; RA Simmons C.R., Liu Q., Huang Q., Hao Q., Begley T.P., Karplus P.A., RA Stipanuk M.H.; RT "Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear RT iron center for cysteine thiol oxidation."; RL J. Biol. Chem. 281:18723-18733(2006). CC -!- FUNCTION: Catalyzes the oxidation of cysteine to cysteine sulfinic acid CC with addition of molecular dioxygen. {ECO:0000269|PubMed:9824269}. 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:9824269}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20442; CC Evidence={ECO:0000269|PubMed:9824269}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000269|PubMed:16611640}; CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000250|UniProtKB:P60334}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P60334}; CC Note=Binds 1 Fe cation per subunit (PubMed:16611640). Ni(2+) and Zn(2+) CC can be used to a lesser extent (By similarity). CC {ECO:0000250|UniProtKB:P60334, ECO:0000269|PubMed:16611640}; CC -!- PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine CC from L-cysteine: step 1/2. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16611640}. CC -!- TISSUE SPECIFICITY: Highest levels in liver. Significant expression CC also in kidney, lung and brain. {ECO:0000269|PubMed:8973325, CC ECO:0000269|PubMed:9824269}. CC -!- DEVELOPMENTAL STAGE: From neonate to weaning. CC -!- INDUCTION: By increase of sulfur amino acid intake. CC {ECO:0000269|PubMed:9824269}. 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:16611640}. CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M35266; AAA40904.1; -; mRNA. DR EMBL; D83481; BAA11925.1; -; Genomic_DNA. DR EMBL; BC070509; AAH70509.1; -; mRNA. DR PIR; A34632; A34632. DR RefSeq; NP_434696.1; NM_052809.1. DR PDB; 2B5H; X-ray; 1.50 A; A=1-200. DR PDB; 2GH2; X-ray; 1.50 A; A=1-200. DR PDB; 3ELN; X-ray; 1.42 A; A=1-200. DR PDB; 4IEO; X-ray; 1.55 A; A=1-200. DR PDB; 4IEP; X-ray; 1.45 A; A=1-200. DR PDB; 4IEQ; X-ray; 1.40 A; A=1-200. DR PDB; 4IER; X-ray; 1.45 A; A=1-200. DR PDB; 4IES; X-ray; 1.40 A; A=1-200. DR PDB; 4IET; X-ray; 1.40 A; A=1-200. DR PDB; 4IEU; X-ray; 1.25 A; A=1-200. DR PDB; 4IEV; X-ray; 1.60 A; A=1-200. DR PDB; 4IEW; X-ray; 1.45 A; A=1-200. DR PDB; 4IEX; X-ray; 2.15 A; A=1-200. DR PDB; 4IEY; X-ray; 1.63 A; A=1-200. DR PDB; 4IEZ; X-ray; 1.39 A; A=1-200. DR PDB; 4JTN; X-ray; 1.59 A; A=1-200. DR PDB; 4JTO; X-ray; 2.00 A; A=1-200. DR PDB; 4KWJ; X-ray; 1.75 A; A=1-200. DR PDB; 4KWK; X-ray; 1.95 A; A=1-200. DR PDB; 4KWL; X-ray; 1.63 A; A=1-200. DR PDB; 4PIX; X-ray; 1.35 A; A=1-200. DR PDB; 4PIY; X-ray; 1.60 A; A=1-200. DR PDB; 4PIZ; X-ray; 1.40 A; A=1-200. DR PDB; 4PJY; X-ray; 1.50 A; A=1-200. DR PDB; 4UBG; X-ray; 1.90 A; A=1-200. DR PDB; 4UBH; X-ray; 1.81 A; A=1-200. DR PDB; 4XET; X-ray; 1.30 A; A=1-200. DR PDB; 4XEZ; X-ray; 1.25 A; A=1-200. DR PDB; 4XF0; X-ray; 1.40 A; A=1-200. DR PDB; 4XF1; X-ray; 1.55 A; A=1-200. DR PDB; 4XF3; X-ray; 1.55 A; A=1-200. DR PDB; 4XF4; X-ray; 1.35 A; A=1-200. DR PDB; 4XF9; X-ray; 1.30 A; A=1-200. DR PDB; 4XFA; X-ray; 1.65 A; A=1-200. DR PDB; 4XFB; X-ray; 1.35 A; A=1-200. DR PDB; 4XFC; X-ray; 1.35 A; A=1-200. DR PDB; 4XFF; X-ray; 1.25 A; A=1-200. DR PDB; 4XFG; X-ray; 1.40 A; A=1-200. DR PDB; 4XFH; X-ray; 1.35 A; A=1-200. DR PDB; 4XFI; X-ray; 1.40 A; A=1-200. DR PDB; 4YNI; X-ray; 2.40 A; A=1-200. DR PDB; 4YSF; X-ray; 1.94 A; A=1-200. DR PDB; 4YYO; X-ray; 1.77 A; A=1-200. DR PDB; 4Z82; X-ray; 1.70 A; A=1-200. DR PDB; 5EFU; X-ray; 2.80 A; A=1-200. DR PDB; 5EZW; X-ray; 1.65 A; A=1-200. DR PDB; 5FDB; X-ray; 1.75 A; A=1-200. DR PDB; 5I0R; X-ray; 1.35 A; A=1-200. DR PDB; 5I0S; X-ray; 1.30 A; A=1-200. DR PDB; 5I0T; X-ray; 1.37 A; A=1-200. DR PDB; 5I0U; X-ray; 1.25 A; A=1-200. DR PDB; 6U1M; X-ray; 1.61 A; A=1-200. DR PDB; 6U4L; X-ray; 1.91 A; A=1-200. DR PDB; 6U4S; X-ray; 2.49 A; A=1-200. DR PDB; 6U4V; X-ray; 2.30 A; A=1-200. DR PDBsum; 2B5H; -. DR PDBsum; 2GH2; -. DR PDBsum; 3ELN; -. DR PDBsum; 4IEO; -. DR PDBsum; 4IEP; -. DR PDBsum; 4IEQ; -. DR PDBsum; 4IER; -. DR PDBsum; 4IES; -. DR PDBsum; 4IET; -. DR PDBsum; 4IEU; -. DR PDBsum; 4IEV; -. DR PDBsum; 4IEW; -. DR PDBsum; 4IEX; -. DR PDBsum; 4IEY; -. DR PDBsum; 4IEZ; -. DR PDBsum; 4JTN; -. DR PDBsum; 4JTO; -. DR PDBsum; 4KWJ; -. DR PDBsum; 4KWK; -. DR PDBsum; 4KWL; -. DR PDBsum; 4PIX; -. DR PDBsum; 4PIY; -. DR PDBsum; 4PIZ; -. DR PDBsum; 4PJY; -. DR PDBsum; 4UBG; -. DR PDBsum; 4UBH; -. DR PDBsum; 4XET; -. DR PDBsum; 4XEZ; -. DR PDBsum; 4XF0; -. DR PDBsum; 4XF1; -. DR PDBsum; 4XF3; -. DR PDBsum; 4XF4; -. DR PDBsum; 4XF9; -. DR PDBsum; 4XFA; -. DR PDBsum; 4XFB; -. DR PDBsum; 4XFC; -. DR PDBsum; 4XFF; -. DR PDBsum; 4XFG; -. DR PDBsum; 4XFH; -. DR PDBsum; 4XFI; -. DR PDBsum; 4YNI; -. DR PDBsum; 4YSF; -. DR PDBsum; 4YYO; -. DR PDBsum; 4Z82; -. DR PDBsum; 5EFU; -. DR PDBsum; 5EZW; -. DR PDBsum; 5FDB; -. DR PDBsum; 5I0R; -. DR PDBsum; 5I0S; -. DR PDBsum; 5I0T; -. DR PDBsum; 5I0U; -. DR PDBsum; 6U1M; -. DR PDBsum; 6U4L; -. DR PDBsum; 6U4S; -. DR PDBsum; 6U4V; -. DR AlphaFoldDB; P21816; -. DR SMR; P21816; -. DR IntAct; P21816; 13. DR STRING; 10116.ENSRNOP00000000172; -. DR PhosphoSitePlus; P21816; -. DR jPOST; P21816; -. DR PaxDb; 10116-ENSRNOP00000000172; -. DR DNASU; 81718; -. DR Ensembl; ENSRNOT00000000172.6; ENSRNOP00000000172.4; ENSRNOG00000000158.6. DR Ensembl; ENSRNOT00055030795; ENSRNOP00055024784; ENSRNOG00055018164. DR Ensembl; ENSRNOT00060019291; ENSRNOP00060015111; ENSRNOG00060011390. DR Ensembl; ENSRNOT00065032348; ENSRNOP00065025845; ENSRNOG00065019206. DR GeneID; 81718; -. DR KEGG; rno:81718; -. DR UCSC; RGD:69262; rat. DR AGR; RGD:69262; -. DR CTD; 1036; -. DR RGD; 69262; Cdo1. DR eggNOG; KOG4064; Eukaryota. DR GeneTree; ENSGT00390000018226; -. DR HOGENOM; CLU_079443_1_0_1; -. DR InParanoid; P21816; -. DR OMA; MLLCWGE; -. DR OrthoDB; 314969at2759; -. DR PhylomeDB; P21816; -. DR TreeFam; TF105636; -. DR BioCyc; MetaCyc:MONOMER-8844; -. DR BRENDA; 1.13.11.20; 5301. DR Reactome; R-RNO-1614558; Degradation of cysteine and homocysteine. DR SABIO-RK; P21816; -. DR UniPathway; UPA00012; UER00537. DR EvolutionaryTrace; P21816; -. DR PRO; PR:P21816; -. DR Proteomes; UP000002494; Chromosome 18. DR Bgee; ENSRNOG00000000158; Expressed in liver and 20 other cell types or tissues. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0017172; F:cysteine dioxygenase activity; IDA:UniProtKB. DR GO; GO:0008198; F:ferrous iron binding; IDA:RGD. DR GO; GO:0016151; F:nickel cation binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISO:RGD. DR GO; GO:0006534; P:cysteine metabolic process; TAS:RGD. DR GO; GO:0019448; P:L-cysteine catabolic process; IDA:RGD. DR GO; GO:0046439; P:L-cysteine metabolic process; NAS:RGD. DR GO; GO:0007595; P:lactation; IDA:RGD. DR GO; GO:0043200; P:response to amino acid; IDA:RGD. DR GO; GO:0051591; P:response to cAMP; IDA:RGD. DR GO; GO:0045471; P:response to ethanol; IDA:RGD. DR GO; GO:0033762; P:response to glucagon; IDA:RGD. DR GO; GO:0051384; P:response to glucocorticoid; IDA:RGD. DR GO; GO:0010243; P:response to organonitrogen compound; IDA:RGD. DR GO; GO:0042412; P:taurine biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd10548; cupin_CDO; 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 Genevisible; P21816; RN. PE 1: Evidence at protein level; KW 3D-structure; Dioxygenase; Direct protein sequencing; Iron; Metal-binding; KW Oxidoreductase; Reference proteome; Thioether bond. FT CHAIN 1..200 FT /note="Cysteine dioxygenase type 1" FT /id="PRO_0000206609" FT BINDING 86 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:16611640" FT BINDING 88 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:16611640" FT BINDING 140 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:16611640" FT CROSSLNK 93..157 FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)" FT /evidence="ECO:0000269|PubMed:16611640" FT CONFLICT 89 FT /note="T -> S (in Ref. 3; AAH70509)" FT /evidence="ECO:0000305" FT HELIX 12..22 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 24..27 FT /evidence="ECO:0007829|PDB:4XEZ" FT HELIX 30..39 FT /evidence="ECO:0007829|PDB:4XEZ" FT HELIX 44..47 FT /evidence="ECO:0007829|PDB:4XEZ" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 59..64 FT /evidence="ECO:0007829|PDB:4XEZ" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:4XFF" FT STRAND 71..77 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 92..100 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:6U1M" FT STRAND 121..125 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 130..133 FT /evidence="ECO:0007829|PDB:4XEZ" FT TURN 135..137 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 151..159 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 162..167 FT /evidence="ECO:0007829|PDB:4XEZ" FT TURN 169..171 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 174..178 FT /evidence="ECO:0007829|PDB:4XEZ" FT STRAND 182..184 FT /evidence="ECO:0007829|PDB:4XEZ" 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 //