Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person UniProt:Q6NT55 CYP4F22
| Class:Id | ReferenceGeneProduct:211029 |
|---|---|
| _chainChangeLog | chain:1-531 added on Sat February 7 2015 |
| _displayName | UniProt:Q6NT55 CYP4F22 |
| _timestamp | 2025-02-21 19:57:52 |
| chain | chain:1-531 |
| checksum | 32E801893EB8C536 |
| comment | FUNCTION A cytochrome P450 monooxygenase involved in epidermal ceramide biosynthesis. Hydroxylates the terminal carbon (omega-hydroxylation) of ultra-long-chain fatty acyls (C28-C36) prior to ceramide synthesis (PubMed:26056268). Contributes to the synthesis of three classes of omega-hydroxy-ultra-long chain fatty acylceramides having sphingosine, 6-hydroxysphingosine and phytosphingosine bases, all major lipid components that underlie the permeability barrier of the stratum corneum (PubMed:26056268). 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 cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:26056268).CATALYTIC ACTIVITY triacontanoate + reduced [NADPH--hemoprotein reductase] + O2 = omega-hydroxy-triacontanoate + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)CATALYTIC ACTIVITY an omega-methyl-ultra-long-chain fatty acid + reduced [NADPH--hemoprotein reductase] + O2 = an omega-hydroxy-ultra-long-chain fatty acid + oxidized [NADPH--hemoprotein reductase] + H2O + H(+)COFACTOR The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the cytochrome P450 family.CAUTION A second transmembrane domain at positions 95-115 is predicted by three programs ESKW, MEMSAT and Phobius. However experimental evidence supports the presence of a single signal-anchor transmembrane domain at the N-terminus. |
| created | [InstanceEdit:211033] Jassal, B, 2008-01-25 15:39:22 |
| description | recommendedName: fullName evidence="6"Ultra-long-chain fatty acid omega-hydroxylase ecNumber evidence="4"1.14.14.177 alternativeName: fullName evidence="5"Cytochrome P450 4F22 |
| geneName | CYP4F22 |
| identifier | Q6NT55 |
| isSequenceChanged | FALSE |
| keyword | Endoplasmic reticulum Heme Ichthyosis Iron Lipid metabolism Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Proteomics identification Reference proteome Transmembrane Transmembrane helix |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 |
| name | CYP4F22 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8992972] ENSEMBL:ENSG00000171954 CYP4F22 [Homo sapiens] |
| secondaryIdentifier | CP4FN_HUMAN Q8N8H4 |
| sequenceLength | 531 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:211056] CYP4F22 [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602276] CYP4F22 H436D [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602287] CYP4F22 H435Y [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602291] CYP4F22 W521* [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:5602296] CYP4F22 R243H [endoplasmic reticulum membrane] [Homo sapiens] |
| (referenceSequence) | [ReplacedResidue:5602267] L-histidine 435 replaced with L-tyrosine [ReplacedResidue:5602269] L-histidine 436 replaced with L-aspartic acid [NonsenseMutation:5602277] Nonsense mutation at L-tryptophan 521 [ReplacedResidue:5602282] L-arginine 243 replaced with L-histidine |
| [Change default viewing format] | |
No pathways have been reviewed or authored by UniProt:Q6NT55 CYP4F22 (211029)
