Sterol 26-hydroxylase, mitochondrial
Details
- Name
- Sterol 26-hydroxylase, mitochondrial
- Synonyms
- 1.14.13.15
- 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase
- CYP27
- Cytochrome P-450C27/25
- Cytochrome P450 27
- Sterol 27-hydroxylase
- Vitamin D(3) 25-hydroxylase
- Gene Name
- CYP27A1
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0018971|Sterol 26-hydroxylase, mitochondrial MAALGCARLRWALRGAGRGLCPHGARAKAAIPAALPSDKATGAPGAGPGVRRRQRSLEEI PRLGQLRFFFQLFVQGYALQLHQLQVLYKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQ EGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAEAALYTDAFNE VIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTF VRSIGLMFQNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAA GPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEA LHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPK NTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGSVPFGYGVRACLGRR IAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGLQFLQRQC
- Number of residues
- 531
- Molecular Weight
- 60234.28
- Theoretical pI
- 9.16
- GO Classification
- Functionscholestanetriol 26-monooxygenase activity / cholesterol 26-hydroxylase activity / heme binding / iron ion binding / steroid hydroxylase activity / vitamin D3 25-hydroxylase activityProcessesbile acid biosynthetic process / bile acid metabolic process / cholesterol metabolic process / small molecule metabolic process / sterol metabolic process / xenobiotic metabolic processComponentsmitochondrial inner membrane / mitochondrial matrix
- General Function
- Vitamin d3 25-hydroxylase activity
- Specific Function
- Catalyzes the first step in the oxidation of the side chain of sterol intermediates; the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3-25-hydroxylase activity.
- Pfam Domain Function
- p450 (PF00067)
- Transmembrane Regions
- Not Available
- Cellular Location
- Mitochondrion membrane
- Gene sequence
>lcl|BSEQ0018972|Sterol 26-hydroxylase, mitochondrial (CYP27A1) ATGGCTGCGCTGGGCTGCGCGAGGCTGAGGTGGGCGCTGCGAGGGGCCGGCCGTGGCCTC TGCCCCCACGGGGCCAGAGCCAAGGCCGCGATCCCTGCCGCCCTCCCCTCGGACAAGGCC ACCGGAGCTCCCGGAGCCGGGCCTGGTGTCCGGCGGCGGCAACGGAGCTTAGAGGAGATT CCACGTCTAGGACAGCTGCGCTTCTTCTTTCAGCTGTTCGTTCAAGGCTATGCCCTGCAA CTGCACCAGTTACAGGTGCTTTACAAGGCCAAGTACGGTCCAATGTGGATGTCCTACTTA GGGCCTCAGATGCACGTGAACCTGGCCAGTGCCCCGCTCTTGGAGCAAGTGATGCGGCAA GAGGGCAAGTACCCAGTACGGAACGACATGGAGCTATGGAAGGAGCACCGGGACCAGCAC GACCTGACCTATGGGCCGTTCACCACGGAAGGACACCACTGGTACCAGCTGCGCCAGGCT CTGAACCAGCGGTTGCTGAAGCCAGCGGAAGCAGCGCTCTATACGGATGCTTTCAATGAG GTGATTGATGACTTTATGACTCGACTGGACCAGCTGCGGGCAGAGAGTGCTTCGGGGAAC CAGGTGTCGGACATGGCTCAACTCTTCTACTACTTTGCCTTGGAAGCTATTTGCTACATC CTGTTCGAGAAACGCATTGGCTGCCTGCAGCGATCCATCCCCGAGGACACCGTGACCTTC GTCAGATCCATCGGGTTAATGTTCCAGAACTCACTCTATGCCACCTTCCTCCCCAAGTGG ACTCGCCCCGTGCTGCCTTTCTGGAAGCGATACCTGGATGGTTGGAATGCCATCTTTTCC TTTGGGAAGAAGCTGATTGATGAGAAGCTCGAAGATATGGAGGCCCAACTGCAGGCAGCA GGGCCAGATGGCATCCAGGTGTCTGGCTACCTGCACTTCTTACTGGCCAGTGGACAGCTC AGTCCTCGGGAGGCCATGGGCAGCCTGCCTGAGCTGCTCATGGCTGGAGTGGACACGACA TCCAACACGCTGACATGGGCCCTGTACCACCTCTCAAAGGACCCTGAGATCCAGGAGGCC TTGCACGAGGAAGTGGTGGGTGTGGTGCCAGCCGGGCAAGTGCCCCAGCACAAGGACTTT GCCCACATGCCGTTGCTCAAAGCTGTGCTTAAGGAGACTCTGCGTCTCTACCCTGTGGTC CCCACAAACTCCCGGATCATAGAAAAGGAAATTGAAGTTGATGGCTTCCTCTTCCCCAAG AACACCCAGTTTGTGTTCTGCCACTATGTGGTGTCCCGGGACCCCACTGCCTTCTCTGAG CCTGAAAGCTTCCAGCCCCACCGCTGGCTGAGAAACAGCCAGCCTGCTACCCCCAGGATC CAGCACCCATTTGGCTCTGTGCCCTTTGGCTATGGGGTCCGGGCCTGCCTGGGCCGCAGG ATTGCAGAGCTGGAGATGCAGCTACTCCTCGCAAGGCTGATCCAGAAGTACAAGGTGGTC CTGGCCCCGGAGACGGGGGAGTTGAAGAGTGTGGCCCGCATTGTCCTGGTTCCCAATAAG AAAGTGGGCCTGCAGTTCCTGCAGAGACAGTGCTGA
- Chromosome Location
- 2
- Locus
- 2q33-qter
- External Identifiers
Resource Link UniProtKB ID Q02318 UniProtKB Entry Name CP27A_HUMAN GenBank Protein ID 181292 GenBank Gene ID M62401 GenAtlas ID CYP27A1 HGNC ID HGNC:2605 - General References
- Cali JJ, Russell DW: Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis. J Biol Chem. 1991 Apr 25;266(12):7774-8. [Article]
- Guo YD, Strugnell S, Back DW, Jones G: Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions. Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8668-72. [Article]
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- Leitersdorf E, Reshef A, Meiner V, Levitzki R, Schwartz SP, Dann EJ, Berkman N, Cali JJ, Klapholz L, Berginer VM: Frameshift and splice-junction mutations in the sterol 27-hydroxylase gene cause cerebrotendinous xanthomatosis in Jews or Moroccan origin. J Clin Invest. 1993 Jun;91(6):2488-96. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
- Cali JJ, Hsieh CL, Francke U, Russell DW: Mutations in the bile acid biosynthetic enzyme sterol 27-hydroxylase underlie cerebrotendinous xanthomatosis. J Biol Chem. 1991 Apr 25;266(12):7779-83. [Article]
- Kim KS, Kubota S, Kuriyama M, Fujiyama J, Bjorkhem I, Eggertsen G, Seyama Y: Identification of new mutations in sterol 27-hydroxylase gene in Japanese patients with cerebrotendinous xanthomatosis (CTX). J Lipid Res. 1994 Jun;35(6):1031-9. [Article]
- Chen W, Kubota S, Kim KS, Cheng J, Kuriyama M, Eggertsen G, Bjorkhem I, Seyama Y: Novel homozygous and compound heterozygous mutations of sterol 27-hydroxylase gene (CYP27) cause cerebrotendinous xanthomatosis in three Japanese patients from two unrelated families. J Lipid Res. 1997 May;38(5):870-9. [Article]
- Chen W, Kubota S, Ujike H, Ishihara T, Seyama Y: A novel Arg362Ser mutation in the sterol 27-hydroxylase gene (CYP27): its effects on pre-mRNA splicing and enzyme activity. Biochemistry. 1998 Oct 27;37(43):15050-6. [Article]
- Lamon-Fava S, Schaefer EJ, Garuti R, Salen G, Calandra S: Two novel mutations in the sterol 27-hydroxylase gene causing cerebrotendinous xanthomatosis. Clin Genet. 2002 Mar;61(3):185-91. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB00153 Ergocalciferol approved, nutraceutical unknown substrate Details DB00169 Cholecalciferol approved, nutraceutical unknown substrate Details DB06777 Chenodeoxycholic acid approved unknown substrate Details DB00082 Pegvisomant approved unknown inducer Details DB06410 Doxercalciferol approved yes substrate Details