Pathway candidateNCBI-verifiedprotein-coding

CYP3A7

cytochrome P450 family 3 subfamily A member 7

NCBI Gene: 1551 Ensembl GeneCards UniProt: P24462

Pathway candidate — not linked to PFS or PSSD by any record here

CYP3A7 is in the library because it belongs to the drug metabolism family. No study, report or commentary in the corpus names it, so a variant in CYP3A7 is not, by itself, evidence of anything related to post-drug syndromes.

Gene summary

A protein-coding gene on chromosome 7 (drug metabolism (phase i)). Encodes a member of the cytochrome P450 superfamily of enzymes, which participate in drug metabolism and the synthesis of cholesterol, steroids and other lipids. This enzyme hydroxylates testosterone and dehydroepiandrosterone 3-sulphate, which is involved in the formation of estriol during pregnancy.

Source: NCBI Gene, accessed 2026-10-07.

Protein reference (UniProt)

Protein: Cytochrome P450 3A7
Function: A cytochrome P450 monooxygenase involved in the metabolism of steroid hormones and vitamins during embryogenesis. 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 (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes 3beta-hydroxyandrost-5-en-17-one (dehydroepiandrosterone, DHEA), a precursor in the biosynthesis of androgen and estrogen steroid hormones. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1), particularly D-ring hydroxylated estrone at the C16-alpha position. Mainly hydroxylates all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may play a role in atRA clearance during fetal development. Also involved in the oxidative metabolism of xenobiotics including anticonvulsants.
Pathway: Steroid hormone biosynthesis. Cofactor metabolism; retinol metabolism.
Subcellular location: Endoplasmic reticulum membrane; Microsome membrane.
Tissue specificity: Expressed in fetal liver (at protein level).

Source: UniProtKB/Swiss-Prot P24462, release 2026_03, licensed CC BY 4.0. This is the protein’s normal biology, not evidence about post-drug syndromes; associated conditions are inherited disorders of the gene, not PFS, PSSD or PRSD.

Why its pathway is in the library

Phase I enzymes determine exposure to finasteride, SSRIs, and other implicated drugs; variation here shapes the likelihood and persistence of adverse effects.

Written for the whole drug metabolism family, not for CYP3A7 specifically.

Mentioned in 0 corpus records

No corpus record names CYP3A7 directly yet. It is in the library because it sits in a pathway the corpus tracks (Drug metabolism).

Also in drug metabolism (phase i)

All 23 genes

Browse by family on the gene families page.

Gene summary

Source: NCBI Gene, accessed 2026-10-07.

Protein reference (UniProt)

Protein: Cytochrome P450 3A7
Function: A cytochrome P450 monooxygenase involved in the metabolism of steroid hormones and vitamins during embryogenesis. 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 (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes 3beta-hydroxyandrost-5-en-17-one (dehydroepiandrosterone, DHEA), a precursor in the biosynthesis of androgen and estrogen steroid hormones. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1), particularly D-ring hydroxylated estrone at the C16-alpha position. Mainly hydroxylates all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may play a role in atRA clearance during fetal development. Also involved in the oxidative metabolism of xenobiotics including anticonvulsants.
Pathway: Steroid hormone biosynthesis. Cofactor metabolism; retinol metabolism.
Subcellular location: Endoplasmic reticulum membrane; Microsome membrane.
Tissue specificity: Expressed in fetal liver (at protein level).