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Details on Person UniProt:O15528 CYP27B1
| Class:Id | ReferenceGeneProduct:52636 |
|---|---|
| _chainChangeLog | transit peptide:1- added on Fri February 6 2015;chain:-508 added on Fri February 6 2015 |
| _displayName | UniProt:O15528 CYP27B1 |
| _timestamp | 2025-02-21 19:46:46 |
| chain | transit peptide:1- chain:-508 |
| checksum | 7F0611EFAD1B5C1C |
| comment | FUNCTION A cytochrome P450 monooxygenase involved in vitamin D metabolism and in calcium and phosphorus homeostasis. Catalyzes the rate-limiting step in the activation of vitamin D in the kidney, namely the hydroxylation of 25-hydroxyvitamin D3/calcidiol at the C1alpha-position to form the hormonally active form of vitamin D3, 1alpha,25-dihydroxyvitamin D3/calcitriol that acts via the vitamin D receptor (VDR) (PubMed:10518789, PubMed:10566658, PubMed:12050193, PubMed:22862690, PubMed:9486994). Has 1alpha-hydroxylase activity on vitamin D intermediates of the CYP24A1-mediated inactivation pathway (PubMed:10518789, PubMed:22862690). Converts 24R,25-dihydroxyvitamin D3/secalciferol to 1-alpha,24,25-trihydroxyvitamin D3, an active ligand of VDR. Also active on 25-hydroxyvitamin D2 (PubMed:10518789). 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:22862690).CATALYTIC ACTIVITY calcidiol + 2 reduced [adrenodoxin] + O2 + 2 H(+) = calcitriol + 2 oxidized [adrenodoxin] + H2OCATALYTIC ACTIVITY secalciferol + 2 reduced [adrenodoxin] + O2 + 2 H(+) = calcitetrol + 2 oxidized [adrenodoxin] + H2OCATALYTIC ACTIVITY 25-hydroxy-24-oxocalciol + 2 reduced [adrenodoxin] + O2 + 2 H(+) = (1S)-1,25-dihydroxy-24-oxocalciol + 2 oxidized [adrenodoxin] + H2OCATALYTIC ACTIVITY 25-hydroxyvitamin D2 + 2 reduced [adrenodoxin] + O2 + 2 H(+) = 1alpha,25-dihydroxyvitamin D2 + 2 oxidized [adrenodoxin] + H2OCOFACTOR Activated by cardiolipin and dioleoyl phosphatidylethanolamine (DOPE), phospholipids found in the inner mitochondrial membrane. Inhibited by high substrate concentration.BIOPHYSICOCHEMICAL PROPERTIES Hormone biosynthesis; vitamin D biosynthesis.SUBCELLULAR LOCATION Kidney.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the cytochrome P450 family. |
| description | recommendedName: 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial ecNumber evidence="5"1.14.15.18 alternativeName: 25-OHD-1 alpha-hydroxylase alternativeName: 25-hydroxyvitamin D(3) 1-alpha-hydroxylase shortName: VD3 1A hydroxylase alternativeName: Calcidiol 1-monooxygenase alternativeName: Cytochrome P450 subfamily XXVIIB polypeptide 1 alternativeName: Cytochrome P450C1 alpha alternativeName: Cytochrome P450VD1-alpha alternativeName: Cytochrome p450 27B1 |
| geneName | CYP27B1 CYP1ALPHA CYP27B |
| identifier | O15528 |
| isSequenceChanged | FALSE |
| keyword | Disease variant Heme Iron Lipid metabolism Membrane Metal-binding Mitochondrion Monooxygenase Oxidoreductase Proteomics identification Reference proteome Transit peptide |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 |
| name | CYP27B1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:9003462] ENSEMBL:ENSG00000111012 CYP27B1 [Homo sapiens] |
| secondaryIdentifier | CP27B_HUMAN B2RC61 Q548T3 |
| sequenceLength | 508 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:209979] CYP27B1(?-508) [mitochondrial outer membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602085] CYP27B1 G125E [mitochondrial outer membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602093] CYP27B1 R335P [mitochondrial outer membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602108] CYP27B1 R389G [mitochondrial outer membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602109] CYP27B1 R107H [mitochondrial outer membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602124] CYP27B1 L343F [mitochondrial outer membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602144] CYP27B1 P382S [mitochondrial outer membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602176] CYP27B1 R389H [mitochondrial outer membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602192] CYP27B1 D320Tfs*32 [mitochondrial outer membrane] [Homo sapiens] |
| (referenceSequence) | [ReplacedResidue:5602084] L-arginine 389 replaced with L-histidine [ReplacedResidue:5602086] L-arginine 335 replaced with L-proline [ReplacedResidue:5602091] L-arginine 107 replaced with L-histidine [ReplacedResidue:5602136] L-leucine 343 replaced with L-phenylalanine [FragmentReplacedModification:5602152] Replacement of residues 320 to 350 by TRCPTRSLGLCMSSPGTPKSRQHSTQRSQLP [ReplacedResidue:5602157] L-proline 382 replaced with L-serine [ReplacedResidue:5602163] glycine 125 replaced with L-glutamic acid [ReplacedResidue:5602194] L-arginine 389 replaced with glycine |
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No pathways have been reviewed or authored by UniProt:O15528 CYP27B1 (52636)
