Overview
| Uniprot ID | P24462 |
|---|
| Protein Name | Cytochrome P450 3A7 |
|---|
| Gene Name | CYP3A7 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 127 |
IAEDEEWKRIRSLLS |
| 244 |
NITVFPRKVISFLTK |
| 413 |
KYWTEPEKFLPERFS |
Function
A cytochrome P450 monooxygenase involved in the metabolism of steroid hormones and vitamins during embryogenesis (PubMed:11093772, PubMed:12865317, PubMed:14559847, PubMed:17178770, PubMed:9555064). 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) (PubMed:11093772, PubMed:12865317, PubMed:14559847, PubMed:17178770, PubMed:9555064). 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 (PubMed:17178770, PubMed:9555064). Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1), particularly D-ring hydroxylated estrone at the C16-alpha position (PubMed:12865317, PubMed:14559847). Mainly hydroxylates all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may play a role in atRA clearance during fetal development (PubMed:11093772). Also involved in the oxidative metabolism of xenobiotics including anticonvulsants (PubMed:9555064)
Protein Sequence
10
MDLIPNLAVE
20
TWLLLAVSLI
30
LLYLYGTRTH
40
GLFKKLGIPG
50
PTPLPFLGNA
60
LSFRKGYWTF
70
DMECYKKYRK
80
VWGIYDCQQP
90
MLAITDPDMI
100
KTVLVKECYS
110
VFTNRRPFGP
120
VGFMKNAISI
130
AEDEEWKRIR
140
SLLSPTFTSG
150
KLKEMVPIIA
160
QYGDVLVRNL
170
RREAETGKPV
180
TLKHVFGAYS
190
MDVITSTSFG
200
VSIDSLNNPQ
210
DPFVENTKKL
220
LRFNPLDPFV
230
LSIKVFPFLT
240
PILEALNITV
250
FPRKVISFLT
260
KSVKQIKEGR
270
LKETQKHRVD
280
FLQLMIDSQN
290
SKDSETHKAL
300
SDLELMAQSI
310
IFIFAGYETT
320
SSVLSFIIYE
330
LATHPDVQQK
340
VQKEIDTVLP
350
NKAPPTYDTV
360
LQLEYLDMVV
370
NETLRLFPVA
380
MRLERVCKKD
390
VEINGMFIPK
400
GVVVMIPSYV
410
LHHDPKYWTE
420
PEKFLPERFS
430
KKNKDNIDPY
440
IYTPFGSGPR
450
NCIGMRFALV
460
NMKLALVRVL
470
QNFSFKPCKE
480
TQIPLKLRFG
490
GLLLTEKPIV
500
LKAESRDETV
SGA
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005789 |
endoplasmic reticulum membrane |
| Molecular Function |
GO:0062183 |
all-trans retinoic acid 18-hydroxylase activity |
| Molecular Function |
GO:0101020 |
estrogen 16-alpha-hydroxylase activity |
| Molecular Function |
GO:0101021 |
estrogen 2-hydroxylase activity |
| Molecular Function |
GO:0020037 |
heme binding |
| Molecular Function |
GO:0005506 |
iron ion binding |
| Molecular Function |
GO:0004497 |
monooxygenase activity |
| Molecular Function |
GO:0019825 |
oxygen binding |
| Molecular Function |
GO:0008401 |
retinoic acid 4-hydroxylase activity |
| Molecular Function |
GO:0008395 |
steroid hydroxylase activity |
| Molecular Function |
GO:0050649 |
testosterone 6-beta-hydroxylase activity |
| Biological Process |
GO:0008210 |
estrogen metabolic process |
| Biological Process |
GO:0002933 |
lipid hydroxylation |
| Biological Process |
GO:0070989 |
oxidative demethylation |
| Biological Process |
GO:0042573 |
retinoic acid metabolic process |
| Biological Process |
GO:0042572 |
retinol metabolic process |
| Biological Process |
GO:0006694 |
steroid biosynthetic process |
| Biological Process |
GO:0008202 |
steroid metabolic process |
| Biological Process |
GO:0006805 |
xenobiotic metabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.