GenomeNet

Database: UniProt
Entry: P21816
LinkDB: P21816
Original site: P21816 
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   07-APR-2021, entry version 147.
DE   RecName: Full=Cysteine dioxygenase type 1;
DE            EC=1.13.11.20;
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   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   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH IRON, AND CROSS-LINK.
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   -!- 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   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 1 Fe cation per subunit.;
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   -!- DEVELOPMENTAL STAGE: From neonate to weaning.
CC   -!- INDUCTION: By increase of sulfur amino acid intake.
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}.
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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   SMR; P21816; -.
DR   IntAct; P21816; 13.
DR   STRING; 10116.ENSRNOP00000000172; -.
DR   jPOST; P21816; -.
DR   PaxDb; P21816; -.
DR   PRIDE; P21816; -.
DR   DNASU; 81718; -.
DR   Ensembl; ENSRNOT00000000172; ENSRNOP00000000172; ENSRNOG00000000158.
DR   GeneID; 81718; -.
DR   KEGG; rno:81718; -.
DR   UCSC; RGD:69262; rat.
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; TETRYAF; -.
DR   OrthoDB; 1516232at2759; -.
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 21 other tissues.
DR   Genevisible; P21816; RN.
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: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: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   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; 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   METAL           86
FT                   /note="Iron; via tele nitrogen; catalytic"
FT                   /evidence="ECO:0000269|PubMed:16611640"
FT   METAL           88
FT                   /note="Iron; via tele nitrogen; catalytic"
FT                   /evidence="ECO:0000269|PubMed:16611640"
FT   METAL           140
FT                   /note="Iron; via tele nitrogen; 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:0007744|PDB:4XEZ"
FT   STRAND          24..27
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   HELIX           30..39
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   HELIX           44..47
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   HELIX           48..50
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   STRAND          55..57
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   STRAND          59..64
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   HELIX           66..68
FT                   /evidence="ECO:0007744|PDB:4XFF"
FT   STRAND          71..77
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   STRAND          92..100
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   STRAND          102..107
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   STRAND          112..114
FT                   /evidence="ECO:0007744|PDB:6U1M"
FT   STRAND          121..125
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   STRAND          130..133
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   TURN            135..137
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   STRAND          139..143
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   STRAND          151..159
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   STRAND          162..167
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   TURN            169..171
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   STRAND          174..178
FT                   /evidence="ECO:0007744|PDB:4XEZ"
FT   STRAND          182..184
FT                   /evidence="ECO:0007744|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
//
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