DHCR7
entrez
1717
canonical
uniprot
Q9UBM7
canonical
ensembl
ENSG00000172893
resolver
ensp
ENSP00000347717
resolver
ensp
ENSP00000384739
resolver
ensp
ENSP00000435047
resolver
ensp
ENSP00000435668
resolver
ensp
ENSP00000435707
resolver
ensp
ENSP00000506866
resolver
ensp
ENSP00000507607
resolver
ensp
ENSP00000510750
resolver
ensp
ENSP00000534921
resolver
ensp
ENSP00000534922
resolver
ensp
ENSP00000534923
resolver
ensp
ENSP00000534924
resolver
ensp
ENSP00000534925
resolver
ensp
ENSP00000608831
resolver
ensp
ENSP00000608832
resolver
ensp
ENSP00000608834
resolver
ensp
ENSP00000608835
resolver
ensp
ENSP00000626249
resolver
ensp
ENSP00000626250
resolver
ensp
ENSP00000660647
resolver
ensp
ENSP00000660648
resolver
ensp
ENSP00000701518
resolver
ensp
ENSP00000755562
resolver
enst
ENST00000355527
resolver
enst
ENST00000407721
resolver
enst
ENST00000525346
resolver
enst
ENST00000526780
resolver
enst
ENST00000527316
resolver
enst
ENST00000682708
resolver
enst
ENST00000683287
resolver
enst
ENST00000690257
resolver
enst
ENST00000864862
resolver
enst
ENST00000864863
resolver
enst
ENST00000864864
resolver
enst
ENST00000864865
resolver
enst
ENST00000864866
resolver
enst
ENST00000938772
resolver
enst
ENST00000938773
resolver
enst
ENST00000938775
resolver
enst
ENST00000938776
resolver
enst
ENST00000956190
resolver
enst
ENST00000956191
resolver
genesymbol
DHCR7
resolver
genesymbol_syn
D7SR
resolver
hgnc
HGNC:2860
resolver
uniprot
A0A024R5F7
resolver
uniprot
A0A804HI25
resolver
uniprot
A0A804HJQ7
resolver
uniprot
A0A8I5KRR9
resolver
uniprot
B2R6Z2
resolver
uniprot
E9PM00
resolver
uniprot
O60492
resolver
uniprot
O60717
resolver
uniprot_entry
A0A024R5F7_HUMAN
resolver
uniprot_entry
A0A804HI25_HUMAN
resolver
uniprot_entry
A0A804HJQ7_HUMAN
resolver
uniprot_entry
A0A8I5KRR9_HUMAN
resolver
uniprot_entry
DHCR7_HUMAN
resolver
uniprot_entry
E9PM00_HUMAN
resolver
uniprot_sec
B2R6Z2
resolver
uniprot_sec
O60492
resolver
uniprot_sec
O60717
resolver
activity_regulation
ACTIVITY REGULATION: 7-DHC reductase and cholesterol-5,6-epoxide hydrolase (ChEH) activities are inhibited by tamoxifen and the selective AEBS ligand (4-benzyl-phenoxy)-ethyl-N-pyrrolidine (PBPE) (PubMed:15175332, PubMed:20615952). ChEH activity is inhibited by oleic acid (PubMed:20615952). {ECO:0000269|PubMed:15175332, ECO:0000269|PubMed:20615952}.
uniprot
proteins
amino_acid_sequence
MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMACDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHKFLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMVKGYFFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDLFRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCLACGGGHLLPYFYIIYMAILLTHRCLRDEHRCASKYGRDWERYTAAVPYRLLPGIF
uniprot
proteins
disease_involvement
DISEASE: Smith-Lemli-Opitz syndrome (SLOS) [MIM:270400]: An autosomal recessive frequent inborn disorder of sterol metabolism with characteristic congenital malformations and intellectual disability. Children with SLOS have elevated serum 7-dehydrocholesterol (7-DHC) levels and low serum cholesterol levels. SLOS occurs in relatively high frequency: approximately 1 in 20,000 to 30,000 births in populations of northern and central European background. Historically, a clinical distinction often was made between classic ('type I') SLOS and the more severely affected ('type II') patients. There is, in reality, a clinical and biochemical continuum from mild to severe SLOS. {ECO:0000269|PubMed:10677299, ECO:0000269|PubMed:10995508, ECO:0000269|PubMed:11175299, ECO:0000269|PubMed:11427181, ECO:0000269|PubMed:12949967, ECO:0000269|PubMed:15954111, ECO:0000269|PubMed:25637936, ECO:0000269|PubMed:38297129, ECO:0000269|PubMed:9653161, ECO:0000269|PubMed:9683613}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.3.1.21
uniprot
proteins
function
FUNCTION: Oxidoreductase that catalyzes the last step of the cholesterol synthesis pathway, which transforms cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol,7-DHC) into cholesterol by reducing the C7-C8 double bond of its sterol core (PubMed:25637936, PubMed:38297129, PubMed:38297130, PubMed:9465114, PubMed:9634533). Can also metabolize cholesta-5,7,24-trien-3beta-ol (7-dehydrodemosterol, 7-DHD) to desmosterol, which is then metabolized by the Delta(24)-sterol reductase (DHCR24) to cholesterol (By similarity). Modulates ferroptosis (a form of regulated cell death driven by iron-dependent lipid peroxidation) through the metabolic breakdown of the anti-ferroptotic metabolites 7-DHC and 7-DHD which, when accumulated, divert the propagation of peroxyl radical-mediated damage from phospholipid components to its sterol core, protecting plasma and mitochondrial membranes from phospholipid autoxidation (PubMed:38297129, PubMed:38297130). {ECO:0000250|UniProtKB:O88455, ECO:0000269|PubMed:25637936, ECO:0000269|PubMed:38297129, ECO:0000269|PubMed:38297130, ECO:0000269|PubMed:9465114, ECO:0000269|PubMed:9634533}.; FUNCTION: Together with cholestenol Delta-isomerase/EBP, forms part of the microsomal antiestrogen binding site (AEBS), a multiprotein complex located in the ER membrane (PubMed:15175332, PubMed:20615952). This complex is responsible for cholesterol-5,6-epoxide hydrolase (ChEH) activity, which consists in the hydration of cholesterol-5,6-epoxides (5,6-EC) into cholestane-3beta,5alpha,6beta-triol (CT) (PubMed:20615952). Within this complex, it cooperates in the binding of substrates to ChEH, while EBP carries the catalytic activity (PubMed:20615952). {ECO:0000269|PubMed:15175332, ECO:0000269|PubMed:20615952}.
uniprot
proteins
mass_dalton
54489
uniprot
proteins
mutagenesis
MUTAGEN 24; /note="A->S: No effect on 7-dehydrocholesterol reductase activity."; /evidence="ECO:0000269|PubMed:38297129"; MUTAGEN 274; /note="N->K: Loss of 7-dehydrocholesterol reductase activity."; /evidence="ECO:0000269|PubMed:38297129"; MUTAGEN 306; /note="L->R: Loss of 7-dehydrocholesterol reductase activity."; /evidence="ECO:0000269|PubMed:38297129"; MUTAGEN 317; /note="L->V: No effect on 7-dehydrocholesterol reductase activity."; /evidence="ECO:0000269|PubMed:38297129
uniprot
proteins
pathway_participation
PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. {ECO:0000269|PubMed:25637936, ECO:0000269|PubMed:9634533}.
uniprot
proteins
protein_family
ERG4/ERG24 family
uniprot
proteins
pubmed
10677299
uniprot
proteins
pubmed
10995508
uniprot
proteins
pubmed
11175299
uniprot
proteins
pubmed
11427181
uniprot
proteins
pubmed
12949967
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15175332
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15954111
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20615952
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25637936
uniprot
proteins
pubmed
25787250
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
32694168
uniprot
proteins
pubmed
38297129
uniprot
proteins
pubmed
38297130
uniprot
proteins
pubmed
9465114
uniprot
proteins
pubmed
9634533
uniprot
proteins
pubmed
9653161
uniprot
proteins
pubmed
9683613
uniprot
proteins
pubmed
9878250
uniprot
proteins
sequence_length
475
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9878250}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 40..60; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 154..174; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 177..197; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 266..286; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 306..326; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 331..351; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 420..440; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins