HSD11B1
entrez
3290
canonical
uniprot
P28845
canonical
ensembl
ENSG00000117594
resolver
ensp
ENSP00000355994
resolver
ensp
ENSP00000355995
resolver
enst
ENST00000367027
resolver
enst
ENST00000367028
resolver
genesymbol
HSD11B1
resolver
genesymbol_syn
HSD11
resolver
genesymbol_syn
HSD11L
resolver
genesymbol_syn
SDR26C1
resolver
hgnc
HGNC:5208
resolver
uniprot
B2R9Z1
resolver
uniprot
D3DT89
resolver
uniprot
X5D2L1
resolver
uniprot_entry
DHI1_HUMAN
resolver
uniprot_entry
X5D2L1_HUMAN
resolver
uniprot_sec
B2R9Z1
resolver
uniprot_sec
D3DT89
resolver
activity_regulation
ACTIVITY REGULATION: Hexose-6-phosphate dehydrogenase (H6PD) provides cosubstrate NADPH, and the glucose-6-phosphate transporter in the ER-membrane supplies the substrate for H6PDH, their activities stimulate the reduction of cortisone and abolish the oxidation of cortisol. {ECO:0000269|PubMed:15280030, ECO:0000269|PubMed:17593962}.
uniprot
proteins
amino_acid_sequence
MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK
uniprot
proteins
disease_involvement
DISEASE: Cortisone reductase deficiency 2 (CORTRD2) [MIM:614662]: An autosomal dominant error of cortisone metabolism characterized by a failure to regenerate cortisol from cortisone, resulting in increased cortisol clearance, activation of the hypothalamic- pituitary axis and ACTH-mediated adrenal androgen excess. Clinical features include hyperandrogenism resulting in hirsutism, oligo- amenorrhea, and infertility in females and premature pseudopuberty in males. {ECO:0000269|PubMed:12858176}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.1.1.146
uniprot
proteins
ec_number
1.1.1.201
uniprot
proteins
function
FUNCTION: Controls the reversible conversion of biologically active glucocorticoids such as cortisone to cortisol, and 11-dehydrocorticosterone to corticosterone in the presence of NADP(H) (PubMed:10497248, PubMed:12460758, PubMed:14973125, PubMed:15152005, PubMed:15280030, PubMed:17593962, PubMed:21453287, PubMed:23685396, PubMed:27927697, PubMed:30902677). Participates in the corticosteroid receptor-mediated anti-inflammatory response, as well as metabolic and homeostatic processes (PubMed:10497248, PubMed:12414862, PubMed:15152005, PubMed:21453287). Plays a role in the secretion of aqueous humor in the eye, maintaining a normotensive, intraocular environment (PubMed:11481269). Bidirectional in vitro, predominantly functions as a reductase in vivo, thereby increasing the concentration of active glucocorticoids (PubMed:10497248, PubMed:11481269, PubMed:12414862, PubMed:12460758). It has broad substrate specificity, besides glucocorticoids, it accepts other steroid and sterol substrates (PubMed:15095019, PubMed:15152005, PubMed:17593962, PubMed:21453287, PubMed:23685396). Interconverts 7-oxo- and 7-hydroxy-neurosteroids such as 7-oxopregnenolone and 7beta-hydroxypregnenolone, 7-oxodehydroepiandrosterone (3beta-hydroxy-5-androstene-7,17-dione) and 7beta-hydroxydehydroepiandrosterone (3beta,7beta-dihydroxyandrost-5-en-17-one), among others (PubMed:17593962). Catalyzes the stereo-specific conversion of the major dietary oxysterol, 7-ketocholesterol (7-oxocholesterol), into the more polar 7-beta-hydroxycholesterol metabolite (PubMed:15095019, PubMed:15152005). 7-oxocholesterol is one of the most important oxysterols, it participates in several events such as induction of apoptosis, accumulation in atherosclerotic lesions, lipid peroxidation, and induction of foam cell formation (PubMed:15095019). Mediates the 7-oxo reduction of 7-oxolithocholate mainly to chenodeoxycholate, and to a lesser extent to ursodeoxycholate, both in its free form and when conjugated to glycine or taurine, providing a link between glucocorticoid activation and bile acid metabolism (PubMed:21453287). Catalyzes the synthesis of 7-beta-25-dihydroxycholesterol from 7-oxo-25-hydroxycholesterol in vitro, which acts as a ligand for the G protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (PubMed:30902677). {ECO:0000269|PubMed:10497248, ECO:0000269|PubMed:12460758, ECO:0000269|PubMed:14973125, ECO:0000269|PubMed:15095019, ECO:0000269|PubMed:15152005, ECO:0000269|PubMed:17593962, ECO:0000269|PubMed:21453287, ECO:0000269|PubMed:23685396, ECO:0000269|PubMed:27927697, ECO:0000269|PubMed:30902677, ECO:0000303|PubMed:10497248, ECO:0000303|PubMed:11481269, ECO:0000303|PubMed:12414862, ECO:0000303|PubMed:12460758, ECO:0000303|PubMed:15095019, ECO:0000303|PubMed:15152005, ECO:0000303|PubMed:21453287}.
uniprot
proteins
mass_dalton
32401
uniprot
proteins
mutagenesis
MUTAGEN 5..6; /note="KK->RR: Predominantly inverted topology. No effect on activity."; /evidence="ECO:0000269|PubMed:10497248, ECO:0000269|PubMed:15152005"; MUTAGEN 5..6; /note="KK->SS: Inverted topology. Reduced Vmax."; /evidence="ECO:0000269|PubMed:10497248, ECO:0000269|PubMed:15152005"; MUTAGEN 5; /note="K->R: Predominantly inverted topology. No effect on activity."; /evidence="ECO:0000269|PubMed:10497248"; MUTAGEN 5; /note="K->S: Inverted topology. No effect on activity."; /evidence="ECO:0000269|PubMed:10497248"; MUTAGEN 6; /note="K->R: No effect on topology. Increased Km for corticosterone."; /evidence="ECO:0000269|PubMed:10497248"; MUTAGEN 6; /note="K->S: No effect on topology or activity."; /evidence="ECO:0000269|PubMed:10497248"; MUTAGEN 18..21; /note="YYYY->AAAA: No effect on topology. Reduced Vmax."; /evidence="ECO:0000269|PubMed:10497248"; MUTAGEN 18..21; /note="YYYY->FFFF: No effect on topology or activity."; /evidence="ECO:0000269|PubMed:10497248"; MUTAGEN 19..21; /note="YYY->AYA: No effect on topology. Reduced Vmax."; /evidence="ECO:0000269|PubMed:10497248"; MUTAGEN 25..26; /note="EE->KK: Inverted topology. Reduced Vmax."; /evidence="ECO:0000269|PubMed:15152005"; MUTAGEN 25..26; /note="EE->KQ: No effect on topology. Reduced Vmax."; /evidence="ECO:0000269|PubMed:15152005"; MUTAGEN 25..26; /note="EE->QQ: Reduced Vmax."; /evidence="ECO:0000269|PubMed:15152005"; MUTAGEN 25; /note="E->K,Q: No effect on activity."; /evidence="ECO:0000269|PubMed:15152005"; MUTAGEN 26; /note="E->K: No effect on activity."; /evidence="ECO:0000269|PubMed:15152005"; MUTAGEN 35..36; /note="KK->SS: Complete loss of activity."; /evidence="ECO:0000269|PubMed:15152005
uniprot
proteins
pathway_participation
PATHWAY: Steroid metabolism. {ECO:0000305}.
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000269|PubMed:10497248, ECO:0000269|PubMed:19159218}.
uniprot
proteins
protein_family
Short-chain dehydrogenases/reductases (SDR) family
uniprot
proteins
pubmed
10497248
uniprot
proteins
pubmed
11481269
uniprot
proteins
pubmed
12414862
uniprot
proteins
pubmed
12460758
uniprot
proteins
pubmed
12858176
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14973125
uniprot
proteins
pubmed
15095019
uniprot
proteins
pubmed
15152005
uniprot
proteins
pubmed
15280030
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15513927
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17070044
uniprot
proteins
pubmed
17593962
uniprot
proteins
pubmed
17919905
uniprot
proteins
pubmed
18069989
uniprot
proteins
pubmed
18485702
uniprot
proteins
pubmed
18553955
uniprot
proteins
pubmed
1885595
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19217779
uniprot
proteins
pubmed
21453287
uniprot
proteins
pubmed
23685396
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27927697
uniprot
proteins
pubmed
30902677
uniprot
proteins
pubmed
8319583
uniprot
proteins
sequence_length
292
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10497248, ECO:0000269|PubMed:15280030}; Single-pass type II membrane protein {ECO:0000269|PubMed:10497248}.
uniprot
proteins
transmembrane_region
TRANSMEM 8..24; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins