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1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial (24-OHase) (Vitamin D(3) 24-hydroxylase) (EC 1.14.15.16) (Cytochrome P450 24A1) (Cytochrome P450-CC24)

 CP24A_RAT               Reviewed;         514 AA.
Q09128; Q498V4; Q63685;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
17-JUN-2020, entry version 138.
RecName: Full=1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial;
Short=24-OHase;
Short=Vitamin D(3) 24-hydroxylase;
EC=1.14.15.16 {ECO:0000269|PubMed:2026586};
AltName: Full=Cytochrome P450 24A1;
AltName: Full=Cytochrome P450-CC24;
Flags: Precursor;
Name=Cyp24a1; Synonyms=Cyp24;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 36-43.
TISSUE=Kidney;
PubMed=1991512; DOI=10.1016/0014-5793(91)80115-j;
Ohyama Y., Noshiro M., Okuda K.;
"Cloning and expression of cDNA encoding 25-hydroxyvitamin D3 24-
hydroxylase.";
FEBS Lett. 278:195-198(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8418863; DOI=10.1021/bi00052a011;
Ohyama Y., Noshiro M., Eggertsen G., Gotoh O., Kato Y., Bjoerkhem I.,
Okuda K.;
"Structural characterization of the gene encoding rat 25-hydroxyvitamin D3
24-hydroxylase.";
Biochemistry 32:76-82(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
PubMed=8036172; DOI=10.1093/nar/22.12.2410;
Hahn C.N., Kerry D.M., Omdahl J.L., May B.K.;
"Identification of a vitamin D responsive element in the promoter of the
rat cytochrome P450(24) gene.";
Nucleic Acids Res. 22:2410-2416(1994).
[5]
PROTEIN SEQUENCE OF 36-43, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
PubMed=2026586;
Ohyama Y., Okuda K.;
"Isolation and characterization of a cytochrome P-450 from rat kidney
mitochondria that catalyzes the 24-hydroxylation of 25-hydroxyvitamin D3.";
J. Biol. Chem. 266:8690-8695(1991).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=10231362; DOI=10.1046/j.1432-1327.1999.00375.x;
Sakaki T., Sawada N., Nonaka Y., Ohyama Y., Inouye K.;
"Metabolic studies using recombinant escherichia coli cells producing rat
mitochondrial CYP24 CYP24 can convert 1alpha,25-dihydroxyvitamin D3 to
calcitroic acid.";
Eur. J. Biochem. 262:43-48(1999).
[7]
SUBSTRATE SPECIFICITY.
PubMed=15574355; DOI=10.2741/1514;
Sakaki T., Kagawa N., Yamamoto K., Inouye K.;
"Metabolism of vitamin D3 by cytochromes P450.";
Front. Biosci. 10:119-134(2005).
[8]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF THR-416 AND ILE-500.
PubMed=16617161; DOI=10.1124/mol.106.023275;
Hamamoto H., Kusudo T., Urushino N., Masuno H., Yamamoto K., Yamada S.,
Kamakura M., Ohta M., Inouye K., Sakaki T.;
"Structure-function analysis of vitamin D 24-hydroxylase (CYP24A1) by site-
directed mutagenesis: amino acid residues responsible for species-based
difference of CYP24A1 between humans and rats.";
Mol. Pharmacol. 70:120-128(2006).
[9]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=25727742; DOI=10.1016/j.jsbmb.2015.02.010;
Tieu E.W., Li W., Chen J., Kim T.K., Ma D., Slominski A.T., Tuckey R.C.;
"Metabolism of 20-hydroxyvitamin D3 and 20,23-dihydroxyvitamin D3 by rat
and human CYP24A1.";
J. Steroid Biochem. Mol. Biol. 149:153-165(2015).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-514 IN COMPLEX WITH HEME, AND
COFACTOR.
PubMed=19961857; DOI=10.1016/j.jmb.2009.11.057;
Annalora A.J., Goodin D.B., Hong W.X., Zhang Q., Johnson E.F., Stout C.D.;
"Crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in
vitamin D metabolism.";
J. Mol. Biol. 396:441-451(2010).
-!- FUNCTION: A cytochrome P450 monooxygenase with a key role in vitamin D
catabolism and calcium homeostasis. Via C24-oxidation pathway,
catalyzes the inactivation of both the vitamin D precursor calcidiol
(25-hydroxyvitamin D(3)) and the active hormone calcitriol (1-alpha,25-
dihydroxyvitamin D(3)) (PubMed:2026586, PubMed:16617161,
PubMed:10231362). With initial hydroxylation at C-24 (via C24-oxidation
pathway), performs a sequential 6-step oxidation of calcitriol leading
to the formation of the biliary metabolite calcitroic acid
(PubMed:10231362, PubMed:16617161). Hydroxylates at C-24 or C-25 other
vitamin D active metabolites, such as CYP11A1-derived secosteroids 20S-
hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol
(PubMed:25727742). Mechanistically, uses molecular oxygen inserting one
oxygen atom into a substrate, and reducing the second into a water
molecule, with two electrons provided by NADPH via FDXR/adrenodoxin
reductase and FDX1/adrenodoxin (PubMed:2026586).
{ECO:0000269|PubMed:10231362, ECO:0000269|PubMed:16617161,
ECO:0000269|PubMed:2026586, ECO:0000269|PubMed:25727742}.
-!- CATALYTIC ACTIVITY:
Reaction=calcitriol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
calcitetrol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:24964,
Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17823,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47799;
EC=1.14.15.16; Evidence={ECO:0000269|PubMed:10231362,
ECO:0000269|PubMed:16617161, ECO:0000269|PubMed:2026586};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24965;
Evidence={ECO:0000305|PubMed:2026586};
-!- CATALYTIC ACTIVITY:
Reaction=calcitetrol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-
1,25-dihydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin];
Xref=Rhea:RHEA:24972, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47799,
ChEBI:CHEBI:47812; EC=1.14.15.16;
Evidence={ECO:0000269|PubMed:10231362, ECO:0000269|PubMed:16617161};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24973;
Evidence={ECO:0000305|PubMed:16617161};
-!- CATALYTIC ACTIVITY:
Reaction=(1S)-1,25-dihydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = (1S)-1,23,25-trihydroxy-24-oxocalciol + H2O + 2
oxidized [adrenodoxin]; Xref=Rhea:RHEA:24976, Rhea:RHEA-COMP:9998,
Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:47812, ChEBI:CHEBI:47813; EC=1.14.15.16;
Evidence={ECO:0000269|PubMed:10231362, ECO:0000269|PubMed:16617161};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24977;
Evidence={ECO:0000305|PubMed:16617161};
-!- CATALYTIC ACTIVITY:
Reaction=(1S)-1,23-dihydroxy-24,25,26,27-tetranorcalciol + 2 H(+) + O2
+ 2 reduced [adrenodoxin] = (1S)-1-hydroxy-23-oxo-24,25,26,27-
tetranorcalciol + 2 H2O + 2 oxidized [adrenodoxin];
Xref=Rhea:RHEA:24984, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47818,
ChEBI:CHEBI:47820; EC=1.14.15.16;
Evidence={ECO:0000269|PubMed:10231362};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24985;
Evidence={ECO:0000305|PubMed:10231362};
-!- CATALYTIC ACTIVITY:
Reaction=(1S)-1-hydroxy-23-oxo-24,25,26,27-tetranorcalciol + H(+) + O2
+ 2 reduced [adrenodoxin] = calcitroate + H2O + 2 oxidized
[adrenodoxin]; Xref=Rhea:RHEA:24988, Rhea:RHEA-COMP:9998, Rhea:RHEA-
COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47820,
ChEBI:CHEBI:58715; EC=1.14.15.16;
Evidence={ECO:0000269|PubMed:10231362};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24989;
Evidence={ECO:0000305|PubMed:10231362};
-!- CATALYTIC ACTIVITY:
Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = H2O + 2
oxidized [adrenodoxin] + secalciferol; Xref=Rhea:RHEA:24968,
Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17933,
ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738;
EC=1.14.15.16; Evidence={ECO:0000269|PubMed:10231362,
ECO:0000269|PubMed:2026586};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24969;
Evidence={ECO:0000305|PubMed:2026586};
-!- CATALYTIC ACTIVITY:
Reaction=2 H(+) + O2 + 2 reduced [adrenodoxin] + secalciferol = 25-
hydroxy-24-oxocalciol + 2 H2O + 2 oxidized [adrenodoxin];
Xref=Rhea:RHEA:49196, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:47805; Evidence={ECO:0000269|PubMed:10231362};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49197;
Evidence={ECO:0000305|PubMed:10231362};
-!- CATALYTIC ACTIVITY:
Reaction=25-hydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 23S,25-dihydroxy-24-oxocholecalciferol + H2O + 2
oxidized [adrenodoxin]; Xref=Rhea:RHEA:49268, Rhea:RHEA-COMP:9998,
Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:47805, ChEBI:CHEBI:90980;
Evidence={ECO:0000269|PubMed:10231362};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49269;
Evidence={ECO:0000305|PubMed:10231362};
-!- CATALYTIC ACTIVITY:
Reaction=20S,23-dihydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 20S,23,25-trihydroxycholecalciferol + H2O + 2
oxidized [adrenodoxin]; Xref=Rhea:RHEA:49396, Rhea:RHEA-COMP:9998,
Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:91306, ChEBI:CHEBI:91308;
Evidence={ECO:0000269|PubMed:25727742};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49397;
Evidence={ECO:0000305|PubMed:25727742};
-!- CATALYTIC ACTIVITY:
Reaction=20S,23-dihydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 20S,23,24-trihydroxycholecalciferol + H2O + 2
oxidized [adrenodoxin]; Xref=Rhea:RHEA:49392, Rhea:RHEA-COMP:9998,
Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:91306, ChEBI:CHEBI:91307;
Evidence={ECO:0000269|PubMed:25727742};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49393;
Evidence={ECO:0000305|PubMed:25727742};
-!- CATALYTIC ACTIVITY:
Reaction=20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 20S,25-dihydroxycholecalciferol + H2O + 2 oxidized
[adrenodoxin]; Xref=Rhea:RHEA:49212, Rhea:RHEA-COMP:9998, Rhea:RHEA-
COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:90983,
ChEBI:CHEBI:90984; Evidence={ECO:0000269|PubMed:25727742};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49213;
Evidence={ECO:0000305|PubMed:25727742};
-!- CATALYTIC ACTIVITY:
Reaction=20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 20S,24S-dihydroxycholecalciferol + H2O + 2 oxidized
[adrenodoxin]; Xref=Rhea:RHEA:49208, Rhea:RHEA-COMP:9998, Rhea:RHEA-
COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:90983,
ChEBI:CHEBI:90986; Evidence={ECO:0000269|PubMed:25727742};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49209;
Evidence={ECO:0000305|PubMed:25727742};
-!- CATALYTIC ACTIVITY:
Reaction=20S-hydroxycholecalciferol + 2 H(+) + O2 + 2 reduced
[adrenodoxin] = 20S,24R-dihydroxycholecalciferol + H2O + 2 oxidized
[adrenodoxin]; Xref=Rhea:RHEA:49204, Rhea:RHEA-COMP:9998, Rhea:RHEA-
COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:90983,
ChEBI:CHEBI:90985; Evidence={ECO:0000269|PubMed:25727742};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49205;
Evidence={ECO:0000305|PubMed:25727742};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:19961857};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.8 uM for calcidiol {ECO:0000269|PubMed:2026586};
KM=0.19 uM for calcitriol {ECO:0000269|PubMed:16617161};
pH dependence:
Optimum pH is 7.7. {ECO:0000269|PubMed:2026586};
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:2026586}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; X59506; CAA42093.1; -; mRNA.
EMBL; L04618; AAA42340.1; -; Genomic_DNA.
EMBL; L04608; AAA42340.1; JOINED; Genomic_DNA.
EMBL; L04609; AAA42340.1; JOINED; Genomic_DNA.
EMBL; L04610; AAA42340.1; JOINED; Genomic_DNA.
EMBL; L04611; AAA42340.1; JOINED; Genomic_DNA.
EMBL; L04612; AAA42340.1; JOINED; Genomic_DNA.
EMBL; L04613; AAA42340.1; JOINED; Genomic_DNA.
EMBL; L04614; AAA42340.1; JOINED; Genomic_DNA.
EMBL; L04615; AAA42340.1; JOINED; Genomic_DNA.
EMBL; L04616; AAA42340.1; JOINED; Genomic_DNA.
EMBL; L04617; AAA42340.1; JOINED; Genomic_DNA.
EMBL; BC100059; AAI00060.1; -; mRNA.
EMBL; Z28351; CAA82206.1; -; Genomic_DNA.
PIR; A45228; A45228.
RefSeq; NP_963966.1; NM_201635.3.
PDB; 3K9V; X-ray; 2.50 A; A/B=34-514.
PDB; 3K9Y; X-ray; 2.80 A; A/B=34-514.
PDBsum; 3K9V; -.
PDBsum; 3K9Y; -.
SMR; Q09128; -.
STRING; 10116.ENSRNOP00000043298; -.
BindingDB; Q09128; -.
ChEMBL; CHEMBL3748; -.
DrugCentral; Q09128; -.
SwissLipids; SLP:000001482; -.
PaxDb; Q09128; -.
PRIDE; Q09128; -.
Ensembl; ENSRNOT00000046011; ENSRNOP00000043298; ENSRNOG00000013062.
GeneID; 25279; -.
KEGG; rno:25279; -.
CTD; 1591; -.
RGD; 2462; Cyp24a1.
eggNOG; KOG0159; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00950000182905; -.
HOGENOM; CLU_001570_28_1_1; -.
InParanoid; Q09128; -.
KO; K07436; -.
OMA; HIGAPCL; -.
OrthoDB; 1273535at2759; -.
PhylomeDB; Q09128; -.
TreeFam; TF105094; -.
BioCyc; MetaCyc:MONOMER-14357; -.
Reactome; R-RNO-196791; Vitamin D (calciferol) metabolism.
Reactome; R-RNO-211916; Vitamins.
SABIO-RK; Q09128; -.
EvolutionaryTrace; Q09128; -.
PRO; PR:Q09128; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000013062; Expressed in adult mammalian kidney and 1 other tissue.
GO; GO:0005739; C:mitochondrion; TAS:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0062181; F:1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity; ISO:RGD.
GO; GO:0030342; F:1-alpha,25-dihydroxyvitamin D3 24-hydroxylase activity; IDA:UniProtKB.
GO; GO:0062180; F:25-hydroxycholecalciferol-23-hydroxylase activity; ISO:RGD.
GO; GO:0008403; F:25-hydroxycholecalciferol-24-hydroxylase activity; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0070576; F:vitamin D 24-hydroxylase activity; IDA:UniProtKB.
GO; GO:0070643; F:vitamin D 25-hydroxylase activity; IDA:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
GO; GO:0055114; P:oxidation-reduction process; ISO:RGD.
GO; GO:0033280; P:response to vitamin D; ISO:RGD.
GO; GO:0042369; P:vitamin D catabolic process; IDA:UniProtKB.
GO; GO:0042359; P:vitamin D metabolic process; IDA:RGD.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002949; Cyt_P450_E_CYP24A_mit.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR01238; MITP450CC24.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
Mitochondrion; Monooxygenase; Oxidoreductase; Reference proteome;
Transit peptide.
TRANSIT 1..35
/note="Mitochondrion"
/evidence="ECO:0000269|PubMed:1991512,
ECO:0000269|PubMed:2026586"
CHAIN 36..514
/note="1,25-dihydroxyvitamin D(3) 24-hydroxylase,
mitochondrial"
/id="PRO_0000003617"
METAL 462
/note="Iron (heme axial ligand)"
/evidence="ECO:0000244|PDB:3K9V, ECO:0000244|PDB:3K9Y"
MUTAGEN 416
/note="T->F: Increases the C23:C24 hydroxylation ratio from
0.01 to 0.12."
/evidence="ECO:0000269|PubMed:16617161"
MUTAGEN 416
/note="T->I: Increases the C23:C24 hydroxylation ratio from
0.01 to 0.19."
/evidence="ECO:0000269|PubMed:16617161"
MUTAGEN 416
/note="T->M: Increases the C23:C24 hydroxylation ratio from
0.01 to 0.08."
/evidence="ECO:0000269|PubMed:16617161"
MUTAGEN 416
/note="T->V: Increases the C23:C24 hydroxylation ratio from
0.01 to 0.16."
/evidence="ECO:0000269|PubMed:16617161"
MUTAGEN 500
/note="I->A: Increases the C23:C24 hydroxylation ratio from
0.01 to 0.15."
/evidence="ECO:0000269|PubMed:16617161"
MUTAGEN 500
/note="I->T,L: Increases the C23:C24 hydroxylation ratio
from 0.01 to 0.16."
/evidence="ECO:0000269|PubMed:16617161"
MUTAGEN 500
/note="I->V: Increases the C23:C24 hydroxylation ratio from
0.01 to 0.13."
/evidence="ECO:0000269|PubMed:16617161"
HELIX 55..57
/evidence="ECO:0000244|PDB:3K9V"
TURN 65..67
/evidence="ECO:0000244|PDB:3K9V"
HELIX 70..75
/evidence="ECO:0000244|PDB:3K9V"
HELIX 79..81
/evidence="ECO:0000244|PDB:3K9V"
HELIX 82..93
/evidence="ECO:0000244|PDB:3K9V"
STRAND 95..101
/evidence="ECO:0000244|PDB:3K9V"
STRAND 104..109
/evidence="ECO:0000244|PDB:3K9V"
HELIX 112..120
/evidence="ECO:0000244|PDB:3K9V"
HELIX 132..141
/evidence="ECO:0000244|PDB:3K9V"
TURN 147..149
/evidence="ECO:0000244|PDB:3K9V"
HELIX 152..166
/evidence="ECO:0000244|PDB:3K9V"
HELIX 169..172
/evidence="ECO:0000244|PDB:3K9V"
HELIX 173..175
/evidence="ECO:0000244|PDB:3K9V"
HELIX 176..193
/evidence="ECO:0000244|PDB:3K9V"
STRAND 196..198
/evidence="ECO:0000244|PDB:3K9Y"
HELIX 203..220
/evidence="ECO:0000244|PDB:3K9V"
STRAND 226..228
/evidence="ECO:0000244|PDB:3K9V"
HELIX 236..246
/evidence="ECO:0000244|PDB:3K9V"
HELIX 249..252
/evidence="ECO:0000244|PDB:3K9V"
STRAND 253..255
/evidence="ECO:0000244|PDB:3K9V"
HELIX 257..263
/evidence="ECO:0000244|PDB:3K9V"
HELIX 266..292
/evidence="ECO:0000244|PDB:3K9V"
TURN 293..295
/evidence="ECO:0000244|PDB:3K9V"
HELIX 301..308
/evidence="ECO:0000244|PDB:3K9V"
HELIX 313..343
/evidence="ECO:0000244|PDB:3K9V"
HELIX 346..359
/evidence="ECO:0000244|PDB:3K9V"
HELIX 368..373
/evidence="ECO:0000244|PDB:3K9V"
HELIX 375..387
/evidence="ECO:0000244|PDB:3K9V"
STRAND 393..397
/evidence="ECO:0000244|PDB:3K9V"
STRAND 402..404
/evidence="ECO:0000244|PDB:3K9V"
STRAND 407..409
/evidence="ECO:0000244|PDB:3K9V"
STRAND 414..418
/evidence="ECO:0000244|PDB:3K9V"
HELIX 421..424
/evidence="ECO:0000244|PDB:3K9V"
TURN 426..428
/evidence="ECO:0000244|PDB:3K9V"
STRAND 432..434
/evidence="ECO:0000244|PDB:3K9Y"
HELIX 437..440
/evidence="ECO:0000244|PDB:3K9V"
HELIX 449..451
/evidence="ECO:0000244|PDB:3K9V"
HELIX 465..482
/evidence="ECO:0000244|PDB:3K9V"
STRAND 483..488
/evidence="ECO:0000244|PDB:3K9V"
STRAND 495..506
/evidence="ECO:0000244|PDB:3K9V"
STRAND 509..513
/evidence="ECO:0000244|PDB:3K9V"
SEQUENCE 514 AA; 59448 MW; 2E5CC1CCBA3C2B91 CRC64;
MSCPIDKRRT LIAFLRRLRD LGQPPRSVTS KASASRAPKE VPLCPLMTDG ETRNVTSLPG
PTNWPLLGSL LEIFWKGGLK KQHDTLAEYH KKYGQIFRMK LGSFDSVHLG SPSLLEALYR
TESAHPQRLE IKPWKAYRDH RNEAYGLMIL EGQEWQRVRS AFQKKLMKPV EIMKLDKKIN
EVLADFLERM DELCDERGRI PDLYSELNKW SFESICLVLY EKRFGLLQKE TEEEALTFIT
AIKTMMSTFG KMMVTPVELH KRLNTKVWQA HTLAWDTIFK SVKPCIDNRL QRYSQQPGAD
FLCDIYQQDH LSKKELYAAV TELQLAAVET TANSLMWILY NLSRNPQAQR RLLQEVQSVL
PDNQTPRAED LRNMPYLKAC LKESMRLTPS VPFTTRTLDK PTVLGEYALP KGTVLTLNTQ
VLGSSEDNFE DSHKFRPERW LQKEKKINPF AHLPFGIGKR MCIGRRLAEL QLHLALCWII
QKYDIVATDN EPVEMLHLGI LVPSRELPIA FRPR


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