| Identification |
|---|
| HMDB Protein ID
| HMDBP01042 |
| Secondary Accession Numbers
| |
| Name
| 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial |
| Synonyms
|
- 25-OHD-1 alpha-hydroxylase
- 25-hydroxyvitamin D(3) 1-alpha-hydroxylase
- Calcidiol 1-monooxygenase
- Cytochrome P450 subfamily XXVIIB polypeptide 1
- Cytochrome P450C1 alpha
- Cytochrome P450VD1-alpha
- Cytochrome p450 27B1
- VD3 1A hydroxylase
|
| Gene Name
| CYP27B1 |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Involved in monooxygenase activity |
| Specific Function
| Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D) plays an important role in normal bone growth, calcium metabolism, and tissue differentiation.
|
| Pathways
|
- cholecalciferol biosynthesis
- Steroid biosynthesis
- Tuberculosis
|
| Reactions
|
| Calcidiol + NADPH + Oxygen → Calcitriol + NADP + Water |
details
|
| Calcidiol + Oxygen + NADPH + Hydrogen Ion → Calcitriol + NADP + Water |
details
|
|
| GO Classification
|
| Biological Process |
| response to lipopolysaccharide |
| vitamin D catabolic process |
| bone mineralization |
| calcium ion homeostasis |
| calcium ion transport |
| decidualization |
| G1 to G0 transition |
| negative regulation of calcidiol 1-monooxygenase activity |
| positive regulation of keratinocyte differentiation |
| positive regulation of vitamin D 24-hydroxylase activity |
| positive regulation of vitamin D receptor signaling pathway |
| xenobiotic metabolic process |
| regulation of bone mineralization |
| response to interferon-gamma |
| response to tumor necrosis factor |
| response to vitamin D |
| vitamin D biosynthetic process |
| negative regulation of cell growth |
| negative regulation of cell proliferation |
| response to estrogen stimulus |
| Cellular Component |
| mitochondrial outer membrane |
| Function |
| ion binding |
| cation binding |
| metal ion binding |
| binding |
| catalytic activity |
| transition metal ion binding |
| electron carrier activity |
| iron ion binding |
| monooxygenase activity |
| heme binding |
| oxidoreductase activity |
| Molecular Function |
| electron carrier activity |
| iron ion binding |
| calcidiol 1-monooxygenase activity |
| heme binding |
| Process |
| metabolic process |
| oxidation reduction |
|
| Cellular Location
|
- Mitochondrion membrane
|
| Gene Properties |
|---|
| Chromosome Location
| 12 |
| Locus
| 12q13.1-q13.3 |
| SNPs
| CYP27B1 |
| Gene Sequence
|
>1527 bp
ATGACCCAGACCCTCAAGTACGCCTCCAGAGTGTTCCATCGCGTCCGCTGGGCGCCCGAG
TTGGGCGCCTCCCTAGGCTACCGAGAGTACCACTCAGCACGCCGGAGCTTGGCAGACATC
CCAGGCCCCTCTACGCCCAGCTTTCTGGCCGAACTTTTCTGCAAGGGGGGGCTGTCGAGG
CTACACGAGCTGCAGGTGCAGGGCGCCGCGCACTTCGGGCCGGTGTGGCTAGCCAGCTTT
GGGACAGTGCGCACCGTGTACGTGGCTGCCCCTGCACTCGTCGAGGAGCTGCTGCGACAG
GAGGGACCCCGGCCCGAGCGCTGCAGCTTCTCGCCCTGGACGGAGCACCGCCGCTGCCGC
CAGCGGGCTTGCGGACTGCTCACTGCGGAAGGCGAAGAATGGCAAAGGCTCCGCAGTCTC
CTGGCCCCGCTCCTCCTCCGGCCTCAAGCGGCCGCCCGCTACGCCGGAACCCTGAACAAC
GTAGTCTGCGACCTTGTGCGGCGTCTGAGGCGCCAGCGGGGACGTGGCACGGGGCCGCCC
GCCCTGGTTCGGGACGTGGCGGGGGAATTTTACAAGTTCGGACTGGAAGGCATCGCCGCG
GTTCTGCTCGGCTCGCGCTTGGGCTGCCTGGAGGCTCAAGTGCCACCCGACACGGAGACC
TTCATCCGCGCTGTGGGCTCGGTGTTTGTGTCCACGCTGTTGACCATGGCGATGCCCCAC
TGGCTGCGCCACCTTGTGCCTGGGCCCTGGGGCCGCCTCTGCCGAGACTGGGACCAGATG
TTTGCATTTGCTCAGAGGCACGTGGAGCGGCGAGAGGCAGAGGCAGCCATGAGGAACGGA
GGACAGCCCGAGAAGGACCTGGAGTCTGGGGCGCACCTGACCCACTTCCTGTTCCGGGAA
GAGTTGCCTGCCCAGTCCATCCTGGGAAATGTGACAGAGTTGCTATTGGCGGGAGTGGAC
ACGGTGTCCAACACGCTCTCTTGGGCTCTGTATGAGCTCTCCCGGCACCCCGAAGTCCAG
ACAGCACTCCACTCAGAGATCACAGCTGCCCTGAGCCCTGGCTCCAGTGCCTACCCCTCA
GCCACTGTTCTGTCCCAGCTGCCCCTGCTGAAGGCGGTGGTCAAGGAAGTGCTAAGACTG
TACCCTGTGGTACCTGGAAATTCTCGTGTCCCAGACAAAGACATTCATGTGGGTGACTAT
ATTATCCCCAAAAATACGCTGGTCACTCTGTGTCACTATGCCACTTCAAGGGACCCTGCC
CAGTTCCCAGAGCCAAATTCTTTTCGTCCAGCTCGCTGGCTGGGGGAGGGTCCCACCCCC
CACCCATTTGCATCTCTTCCCTTTGGCTTTGGCAAGCGCAGCTGTATGGGGAGACGCCTG
GCAGAGCTTGAATTGCAAATGGCTTTGGCCCAGATCCTAACACATTTTGAGGTGCAGCCT
GAGCCAGGTGCGGCCCCAGTTAGACCCAAGACCCGGACTGTCCTGGTACCTGAAAGGAGC
ATCAACCTACAGTTTTTGGACAGATAG
|
| Protein Properties |
|---|
| Number of Residues
| 508 |
| Molecular Weight
| 56503.475 |
| Theoretical pI
| 9.159 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
>25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
MTQTLKYASRVFHRVRWAPELGASLGYREYHSARRSLADIPGPSTPSFLAELFCKGGLSR
LHELQVQGAAHFGPVWLASFGTVRTVYVAAPALVEELLRQEGPRPERCSFSPWTEHRRCR
QRACGLLTAEGEEWQRLRSLLAPLLLRPQAAARYAGTLNNVVCDLVRRLRRQRGRGTGPP
ALVRDVAGEFYKFGLEGIAAVLLGSRLGCLEAQVPPDTETFIRAVGSVFVSTLLTMAMPH
WLRHLVPGPWGRLCRDWDQMFAFAQRHVERREAEAAMRNGGQPEKDLESGAHLTHFLFRE
ELPAQSILGNVTELLLAGVDTVSNTLSWALYELSRHPEVQTALHSEITAALSPGSSAYPS
ATVLSQLPLLKAVVKEVLRLYPVVPGNSRVPDKDIHVGDYIIPKNTLVTLCHYATSRDPA
QFPEPNSFRPARWLGEGPTPHPFASLPFGFGKRSCMGRRLAELELQMALAQILTHFEVQP
EPGAAPVRPKTRTVLVPERSINLQFLDR
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| O15528 |
| UniProtKB/Swiss-Prot Entry Name
| CP27B_HUMAN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| AB005038 |
| GeneCard ID
| CYP27B1 |
| GenAtlas ID
| CYP27B1 |
| HGNC ID
| HGNC:2606 |
| References |
|---|
| General References
| - Fu GK, Portale AA, Miller WL: Complete structure of the human gene for the vitamin D 1alpha-hydroxylase, P450c1alpha. DNA Cell Biol. 1997 Dec;16(12):1499-507. [PubMed:9428799 ]
- Monkawa T, Yoshida T, Wakino S, Shinki T, Anazawa H, Deluca HF, Suda T, Hayashi M, Saruta T: Molecular cloning of cDNA and genomic DNA for human 25-hydroxyvitamin D3 1 alpha-hydroxylase. Biochem Biophys Res Commun. 1997 Oct 20;239(2):527-33. [PubMed:9344864 ]
- Fu GK, Lin D, Zhang MY, Bikle DD, Shackleton CH, Miller WL, Portale AA: Cloning of human 25-hydroxyvitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1. Mol Endocrinol. 1997 Dec;11(13):1961-70. [PubMed:9415400 ]
- Kitanaka S, Takeyama K, Murayama A, Sato T, Okumura K, Nogami M, Hasegawa Y, Niimi H, Yanagisawa J, Tanaka T, Kato S: Inactivating mutations in the 25-hydroxyvitamin D3 1alpha-hydroxylase gene in patients with pseudovitamin D-deficiency rickets. N Engl J Med. 1998 Mar 5;338(10):653-61. [PubMed:9486994 ]
- Wang JT, Lin CJ, Burridge SM, Fu GK, Labuda M, Portale AA, Miller WL: Genetics of vitamin D 1alpha-hydroxylase deficiency in 17 families. Am J Hum Genet. 1998 Dec;63(6):1694-702. [PubMed:9837822 ]
- Smith SJ, Rucka AK, Berry JL, Davies M, Mylchreest S, Paterson CR, Heath DA, Tassabehji M, Read AP, Mee AP, Mawer EB: Novel mutations in the 1alpha-hydroxylase (P450c1) gene in three families with pseudovitamin D-deficiency rickets resulting in loss of functional enzyme activity in blood-derived macrophages. J Bone Miner Res. 1999 May;14(5):730-9. [PubMed:10320521 ]
- Kitanaka S, Murayama A, Sakaki T, Inouye K, Seino Y, Fukumoto S, Shima M, Yukizane S, Takayanagi M, Niimi H, Takeyama K, Kato S: No enzyme activity of 25-hydroxyvitamin D3 1alpha-hydroxylase gene product in pseudovitamin D deficiency rickets, including that with mild clinical manifestation. J Clin Endocrinol Metab. 1999 Nov;84(11):4111-7. [PubMed:10566658 ]
- Wang X, Zhang MY, Miller WL, Portale AA: Novel gene mutations in patients with 1alpha-hydroxylase deficiency that confer partial enzyme activity in vitro. J Clin Endocrinol Metab. 2002 Jun;87(6):2424-30. [PubMed:12050193 ]
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