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Corticosteroid 11-beta-dehydrogenase isozyme 1 (EC 1.1.1.146) (11-beta-hydroxysteroid dehydrogenase 1) (11-DH) (11-beta-HSD1) (Short chain dehydrogenase/reductase family 26C member 1)

 DHI1_HUMAN              Reviewed;         292 AA.
P28845; B2R9Z1; D3DT89;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 185.
RecName: Full=Corticosteroid 11-beta-dehydrogenase isozyme 1;
EC=1.1.1.146;
AltName: Full=11-beta-hydroxysteroid dehydrogenase 1;
Short=11-DH;
Short=11-beta-HSD1;
AltName: Full=Short chain dehydrogenase/reductase family 26C member 1;
Name=HSD11B1; Synonyms=HSD11, HSD11L, SDR26C1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Testis;
PubMed=1885595;
Tannin G.M., Agarwal A.K., Monder C., New M.I., White P.C.;
"The human gene for 11 beta-hydroxysteroid dehydrogenase. Structure,
tissue distribution, and chromosomal localization.";
J. Biol. Chem. 266:16653-16658(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12414862; DOI=10.1210/jc.2001-011375;
Draper N., Echwald S.M., Lavery G.G., Walker E.A., Fraser R.,
Davies E., Soerensen T.I.A., Astrup A., Adamski J., Hewison M.,
Connell J.M., Pedersen O., Stewart P.M.;
"Association studies between microsatellite markers within the gene
encoding human 11beta-hydroxysteroid dehydrogenase type 1 and body
mass index, waist to hip ratio, and glucocorticoid metabolism.";
J. Clin. Endocrinol. Metab. 87:4984-4990(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION, AND
MUTAGENESIS OF LYS-5; 5-LYS-LYS-6; LYS-6; 18-TYR--TYR-21 AND
19-TYR--TYR-21.
PubMed=10497248; DOI=10.1074/jbc.274.40.28762;
Odermatt A., Arnold P., Stauffer A., Frey B.M., Frey F.J.;
"The N-terminal anchor sequences of 11beta-hydroxysteroid
dehydrogenases determine their orientation in the endoplasmic
reticulum membrane.";
J. Biol. Chem. 274:28762-28770(1999).
[8]
INVOLVEMENT IN CRD.
PubMed=12858176; DOI=10.1038/ng1214;
Draper N., Walker E.A., Bujalska I.J., Tomlinson J.W., Chalder S.M.,
Arlt W., Lavery G.G., Bedendo O., Ray D.W., Laing I., Malunowicz E.,
White P.C., Hewison M., Mason P.J., Connell J.M., Shackleton C.H.L.,
Stewart P.M.;
"Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase
type 1 and hexose-6-phosphate dehydrogenase interact to cause
cortisone reductase deficiency.";
Nat. Genet. 34:434-439(2003).
[9]
CATALYTIC ACTIVITY, TOPOLOGY, AND MUTAGENESIS OF 5-LYS-LYS-6; GLU-25;
25-GLU-GLU-26; GLU-26 AND 35-LYS-LYS-36.
PubMed=15152005; DOI=10.1074/jbc.M313666200;
Frick C., Atanasov A.G., Arnold P., Ozols J., Odermatt A.;
"Appropriate function of 11beta-hydroxysteroid dehydrogenase type 1 in
the endoplasmic reticulum lumen is dependent on its N-terminal region
sharing similar topological determinants with 50-kDa esterase.";
J. Biol. Chem. 279:31131-31138(2004).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-123 AND ASN-162.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP
AND SUBSTRATE ANALOG, AND SUBUNIT.
PubMed=15513927; DOI=10.1074/jbc.M411104200;
Hosfield D.J., Wu Y., Skene R.J., Hilgers M., Jennings A., Snell G.P.,
Aertgeerts K.;
"Conformational flexibility in crystal structures of human 11beta-
hydroxysteroid dehydrogenase type I provide insights into
glucocorticoid interconversion and enzyme regulation.";
J. Biol. Chem. 280:4639-4648(2005).
[13]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-284 IN COMPLEXES WITH
ADAMANTANE SULFONE AND SULFONAMIDE INHIBITORS, AND CATALYTIC ACTIVITY.
PubMed=17070044; DOI=10.1016/j.bmcl.2006.10.008;
Sorensen B., Winn M., Rohde J., Shuai Q., Wang J., Fung S., Monzon K.,
Chiou W., Stolarik D., Imade H., Pan L., Deng X., Chovan L.,
Longenecker K., Judge R., Qin W., Brune M., Camp H., Frevert E.U.,
Jacobson P., Link J.T.;
"Adamantane sulfone and sulfonamide 11-beta-HSD1 Inhibitors.";
Bioorg. Med. Chem. Lett. 17:527-532(2007).
[14]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-292 IN COMPLEX WITH NADP
AND INHIBITOR, SUBUNIT, AND CATALYTIC ACTIVITY.
PubMed=17919905; DOI=10.1016/j.bmcl.2007.09.070;
Yuan C., St Jean D.J. Jr., Liu Q., Cai L., Li A., Han N., Moniz G.,
Askew B., Hungate R.W., Johansson L., Tedenborg L., Pyring D.,
Williams M., Hale C., Chen M., Cupples R., Zhang J., Jordan S.,
Bartberger M.D., Sun Y., Emery M., Wang M., Fotsch C.;
"The discovery of 2-anilinothiazolones as 11beta-HSD1 inhibitors.";
Bioorg. Med. Chem. Lett. 17:6056-6061(2007).
[15]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP
AND INHIBITOR.
PubMed=18485702; DOI=10.1016/j.bmcl.2008.04.069;
Wang H., Ruan Z., Li J.J., Simpkins L.M., Smirk R.A., Wu S.C.,
Hutchins R.D., Nirschl D.S., Van Kirk K., Cooper C.B., Sutton J.C.,
Ma Z., Golla R., Seethala R., Salyan M.E.K., Nayeem A.,
Krystek S.R. Jr., Sheriff S., Camac D.M., Morin P.E., Carpenter B.,
Robl J.A., Zahler R., Gordon D.A., Hamann L.G.;
"Pyridine amides as potent and selective inhibitors of 11beta-
hydroxysteroid dehydrogenase type 1.";
Bioorg. Med. Chem. Lett. 18:3168-3172(2008).
[16]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP
AND INHIBITOR.
PubMed=18069989; DOI=10.1111/j.1747-0285.2007.00603.x;
Hale C., Veniant M., Wang Z., Chen M., McCormick J., Cupples R.,
Hickman D., Min X., Sudom A., Xu H., Matsumoto G., Fotsch C.,
St Jean D.J. Jr., Wang M.;
"Structural characterization and pharmacodynamic effects of an orally
active 11beta-hydroxysteroid dehydrogenase type 1 inhibitor.";
Chem. Biol. Drug Des. 71:36-44(2008).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP
AND INHIBITOR.
PubMed=18553955; DOI=10.1021/jm800310g;
Julian L.D., Wang Z., Bostick T., Caille S., Choi R.,
DeGraffenreid M., Di Y., He X., Hungate R.W., Jaen J.C., Liu J.,
Monshouwer M., McMinn D., Rew Y., Sudom A., Sun D., Tu H., Ursu S.,
Walker N., Yan X., Ye Q., Powers J.P.;
"Discovery of novel, potent benzamide inhibitors of 11beta-
hydroxysteroid dehydrogenase type 1 (11beta-HSD1) exhibiting oral
activity in an enzyme inhibition ex vivo model.";
J. Med. Chem. 51:3953-3960(2008).
[18]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP
AND INHIBITOR.
PubMed=19217779; DOI=10.1016/j.bmcl.2009.01.058;
Rew Y., McMinn D.L., Wang Z., He X., Hungate R.W., Jaen J.C.,
Sudom A., Sun D., Tu H., Ursu S., Villemure E., Walker N.P.C., Yan X.,
Ye Q., Powers J.P.;
"Discovery and optimization of piperidyl benzamide derivatives as a
novel class of 11beta-HSD1 inhibitors.";
Bioorg. Med. Chem. Lett. 19:1797-1801(2009).
[19]
VARIANT [LARGE SCALE ANALYSIS] GLU-148.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Catalyzes reversibly the conversion of cortisol to the
inactive metabolite cortisone. Catalyzes reversibly the conversion
of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact
cells, the reaction runs only in one direction, from 7-
ketocholesterol to 7-beta-hydroxycholesterol (By similarity).
{ECO:0007001}.
-!- CATALYTIC ACTIVITY: An 11-beta-hydroxysteroid + NADP(+) = an 11-
oxosteroid + NADPH. {ECO:0000269|PubMed:10497248,
ECO:0000269|PubMed:15152005, ECO:0000269|PubMed:17070044,
ECO:0000269|PubMed:17919905}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15513927,
ECO:0000269|PubMed:17919905, ECO:0000269|PubMed:18069989,
ECO:0000269|PubMed:18485702, ECO:0000269|PubMed:18553955,
ECO:0000269|PubMed:19217779}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10497248}; Single-pass type II membrane
protein {ECO:0000269|PubMed:10497248}.
-!- TISSUE SPECIFICITY: Widely expressed. Highest expression in liver.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:10497248,
ECO:0000269|PubMed:19159218}.
-!- DISEASE: Cortisone reductase deficiency (CRD) [MIM:604931]: In
CRD, activation of cortisone to cortisol does not occur, resulting
in adrenocorticotropin-mediated androgen excess and a phenotype
resembling polycystic ovary syndrome (PCOS).
{ECO:0000269|PubMed:12858176}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000320}.
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EMBL; M76665; AAC31757.1; -; Genomic_DNA.
EMBL; M76661; AAC31757.1; JOINED; Genomic_DNA.
EMBL; M76662; AAC31757.1; JOINED; Genomic_DNA.
EMBL; M76663; AAC31757.1; JOINED; Genomic_DNA.
EMBL; M76664; AAC31757.1; JOINED; Genomic_DNA.
EMBL; AY044084; AAK83653.1; -; Genomic_DNA.
EMBL; AY044083; AAK83653.1; JOINED; Genomic_DNA.
EMBL; AK313973; BAG36688.1; -; mRNA.
EMBL; AL022398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL031316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471100; EAW93445.1; -; Genomic_DNA.
EMBL; CH471100; EAW93446.1; -; Genomic_DNA.
EMBL; BC012593; AAH12593.1; -; mRNA.
CCDS; CCDS1489.1; -.
PIR; A41173; DXHUBH.
RefSeq; NP_001193670.1; NM_001206741.1.
RefSeq; NP_005516.1; NM_005525.3.
RefSeq; NP_861420.1; NM_181755.2.
UniGene; Hs.195040; -.
PDB; 1XU7; X-ray; 1.80 A; A/B/C/D=24-292.
PDB; 1XU9; X-ray; 1.55 A; A/B/C/D=24-292.
PDB; 2BEL; X-ray; 2.11 A; A/B/C/D=26-284.
PDB; 2ILT; X-ray; 2.30 A; A=24-285.
PDB; 2IRW; X-ray; 3.10 A; A/B/C/D/E/F/G/H=26-289.
PDB; 2RBE; X-ray; 1.90 A; A/B/C/D=25-292.
PDB; 3BYZ; X-ray; 2.69 A; A/B/C/D=25-292.
PDB; 3BZU; X-ray; 2.25 A; A/B/C/D=24-292.
PDB; 3CH6; X-ray; 2.35 A; A/B/D/E=24-292.
PDB; 3CZR; X-ray; 2.35 A; A/B=24-292.
PDB; 3D3E; X-ray; 2.60 A; A/B/C/D=24-292.
PDB; 3D4N; X-ray; 2.50 A; A/B/C/D=24-292.
PDB; 3D5Q; X-ray; 2.55 A; A/B/C/D=24-292.
PDB; 3EY4; X-ray; 3.00 A; A/B/C/D=25-292.
PDB; 3FCO; X-ray; 2.65 A; A/B=24-291.
PDB; 3FRJ; X-ray; 2.30 A; A/B=24-292.
PDB; 3H6K; X-ray; 2.19 A; A/B/C/D=24-292.
PDB; 3HFG; X-ray; 2.30 A; A/B/C/D=24-292.
PDB; 3OQ1; X-ray; 2.60 A; A/B/C/D=24-292.
PDB; 3PDJ; X-ray; 2.30 A; A/B=24-292.
PDB; 3QQP; X-ray; 2.72 A; A/B/C/D=24-292.
PDB; 3TFQ; X-ray; 1.80 A; A/B/D/E=24-292.
PDB; 4BB5; X-ray; 2.20 A; A/B/C/D=1-292.
PDB; 4BB6; X-ray; 2.55 A; A/B=1-292.
PDB; 4C7J; X-ray; 2.16 A; A/B/C/D=24-292.
PDB; 4C7K; X-ray; 1.91 A; A/B/C/D=24-292.
PDB; 4HFR; X-ray; 2.73 A; A/B=24-292.
PDB; 4HX5; X-ray; 2.19 A; A/B/C/D=24-292.
PDB; 4IJU; X-ray; 2.35 A; A/B/D/E=24-292.
PDB; 4IJV; X-ray; 2.35 A; A/B/D/E=24-292.
PDB; 4IJW; X-ray; 2.35 A; A/B/D/E=24-292.
PDB; 4K1L; X-ray; 1.96 A; A/B/C/D=24-292.
PDB; 4P38; X-ray; 2.80 A; A/B=26-290.
PDB; 4YYZ; X-ray; 3.20 A; A/B=26-284.
PDBsum; 1XU7; -.
PDBsum; 1XU9; -.
PDBsum; 2BEL; -.
PDBsum; 2ILT; -.
PDBsum; 2IRW; -.
PDBsum; 2RBE; -.
PDBsum; 3BYZ; -.
PDBsum; 3BZU; -.
PDBsum; 3CH6; -.
PDBsum; 3CZR; -.
PDBsum; 3D3E; -.
PDBsum; 3D4N; -.
PDBsum; 3D5Q; -.
PDBsum; 3EY4; -.
PDBsum; 3FCO; -.
PDBsum; 3FRJ; -.
PDBsum; 3H6K; -.
PDBsum; 3HFG; -.
PDBsum; 3OQ1; -.
PDBsum; 3PDJ; -.
PDBsum; 3QQP; -.
PDBsum; 3TFQ; -.
PDBsum; 4BB5; -.
PDBsum; 4BB6; -.
PDBsum; 4C7J; -.
PDBsum; 4C7K; -.
PDBsum; 4HFR; -.
PDBsum; 4HX5; -.
PDBsum; 4IJU; -.
PDBsum; 4IJV; -.
PDBsum; 4IJW; -.
PDBsum; 4K1L; -.
PDBsum; 4P38; -.
PDBsum; 4YYZ; -.
ProteinModelPortal; P28845; -.
SMR; P28845; -.
BioGrid; 109523; 16.
DIP; DIP-59618N; -.
IntAct; P28845; 1.
STRING; 9606.ENSP00000261465; -.
BindingDB; P28845; -.
ChEMBL; CHEMBL4235; -.
DrugBank; DB07049; (2R)-1-[(4-tert-butylphenyl)sulfonyl]-2-methyl-4-(4-nitrophenyl)piperazine.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB03814; 2-(N-Morpholino)-Ethanesulfonic Acid.
DrugBank; DB02329; Carbenoxolone.
DrugBank; DB05064; INCB13739.
DrugBank; DB00157; NADH.
DrugBank; DB00635; Prednisone.
GuidetoPHARMACOLOGY; 2763; -.
SwissLipids; SLP:000000809; -.
iPTMnet; P28845; -.
PhosphoSitePlus; P28845; -.
BioMuta; HSD11B1; -.
DMDM; 118569; -.
PaxDb; P28845; -.
PeptideAtlas; P28845; -.
PRIDE; P28845; -.
DNASU; 3290; -.
Ensembl; ENST00000367027; ENSP00000355994; ENSG00000117594.
Ensembl; ENST00000367028; ENSP00000355995; ENSG00000117594.
GeneID; 3290; -.
KEGG; hsa:3290; -.
CTD; 3290; -.
DisGeNET; 3290; -.
EuPathDB; HostDB:ENSG00000117594.9; -.
GeneCards; HSD11B1; -.
HGNC; HGNC:5208; HSD11B1.
HPA; HPA047729; -.
MalaCards; HSD11B1; -.
MIM; 600713; gene.
MIM; 604931; phenotype.
neXtProt; NX_P28845; -.
OpenTargets; ENSG00000117594; -.
Orphanet; 168588; Hyperandrogenism due to cortisone reductase deficiency.
PharmGKB; PA29476; -.
eggNOG; KOG1205; Eukaryota.
eggNOG; COG1028; LUCA.
GeneTree; ENSGT00880000138008; -.
HOGENOM; HOG000010276; -.
HOVERGEN; HBG005481; -.
InParanoid; P28845; -.
KO; K15680; -.
OMA; IGREMAY; -.
OrthoDB; EOG091G0H0R; -.
PhylomeDB; P28845; -.
TreeFam; TF329114; -.
BioCyc; MetaCyc:HS04154-MONOMER; -.
BRENDA; 1.1.1.146; 2681.
BRENDA; 1.1.1.B40; 2681.
Reactome; R-HSA-194002; Glucocorticoid biosynthesis.
SABIO-RK; P28845; -.
ChiTaRS; HSD11B1; human.
EvolutionaryTrace; P28845; -.
GeneWiki; 11%CE%B2-hydroxysteroid_dehydrogenase_type_1; -.
GenomeRNAi; 3290; -.
PRO; PR:P28845; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117594; -.
CleanEx; HS_HSD11B1; -.
ExpressionAtlas; P28845; baseline and differential.
Genevisible; P28845; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:Reactome.
GO; GO:0016021; C:integral component of membrane; RCA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HTP:UniProtKB.
GO; GO:0070524; F:11-beta-hydroxysteroid dehydrogenase (NADP+) activity; RCA:UniProtKB-EC.
GO; GO:0003845; F:11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity; IBA:Reactome.
GO; GO:0006704; P:glucocorticoid biosynthetic process; IBA:Reactome.
GO; GO:0030324; P:lung development; RCA:Ensembl.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Endoplasmic reticulum; Glycoprotein;
Lipid metabolism; Membrane; NADP; Oxidoreductase; Polymorphism;
Reference proteome; Signal-anchor; Steroid metabolism; Transmembrane;
Transmembrane helix.
CHAIN 1 292 Corticosteroid 11-beta-dehydrogenase
isozyme 1.
/FTId=PRO_0000054619.
TOPO_DOM 1 7 Cytoplasmic. {ECO:0000270}.
TRANSMEM 8 24 Helical; Signal-anchor for type II
membrane protein. {ECO:0000270}.
TOPO_DOM 25 292 Lumenal. {ECO:0000270}.
NP_BIND 41 67 NADP. {ECO:0000269|PubMed:15513927,
ECO:0000269|PubMed:17919905,
ECO:0000269|PubMed:18069989,
ECO:0000269|PubMed:18485702,
ECO:0000269|PubMed:18553955,
ECO:0000269|PubMed:19217779}.
NP_BIND 92 93 NADP. {ECO:0000269|PubMed:15513927,
ECO:0000269|PubMed:17919905,
ECO:0000269|PubMed:18069989,
ECO:0000269|PubMed:18485702,
ECO:0000269|PubMed:18553955,
ECO:0000269|PubMed:19217779}.
NP_BIND 119 121 NADP. {ECO:0000269|PubMed:15513927,
ECO:0000269|PubMed:17919905,
ECO:0000269|PubMed:18069989,
ECO:0000269|PubMed:18485702,
ECO:0000269|PubMed:18553955,
ECO:0000269|PubMed:19217779}.
NP_BIND 183 187 NADP. {ECO:0000269|PubMed:15513927,
ECO:0000269|PubMed:17919905,
ECO:0000269|PubMed:18069989,
ECO:0000269|PubMed:18485702,
ECO:0000269|PubMed:18553955,
ECO:0000269|PubMed:19217779}.
NP_BIND 218 222 NADP. {ECO:0000269|PubMed:15513927,
ECO:0000269|PubMed:17919905,
ECO:0000269|PubMed:18069989,
ECO:0000269|PubMed:18485702,
ECO:0000269|PubMed:18553955,
ECO:0000269|PubMed:19217779}.
ACT_SITE 183 183 Proton acceptor.
BINDING 170 170 Substrate.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 162 162 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000270}.
VARIANT 148 148 V -> E (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035845.
MUTAGEN 5 6 KK->RR: Predominantly inverted topology.
No effect on activity.
{ECO:0000269|PubMed:10497248,
ECO:0000269|PubMed:15152005}.
MUTAGEN 5 6 KK->SS: Inverted topology. Reduced Vmax.
{ECO:0000269|PubMed:10497248,
ECO:0000269|PubMed:15152005}.
MUTAGEN 5 5 K->R: Predominantly inverted topology. No
effect on activity.
{ECO:0000269|PubMed:10497248}.
MUTAGEN 5 5 K->S: Inverted topology. No effect on
activity. {ECO:0000269|PubMed:10497248}.
MUTAGEN 6 6 K->R: No effect on topology. Increased Km
for corticosterone.
{ECO:0000269|PubMed:10497248}.
MUTAGEN 6 6 K->S: No effect on topology or activity.
{ECO:0000269|PubMed:10497248}.
MUTAGEN 18 21 YYYY->AAAA: No effect on topology.
Reduced Vmax.
{ECO:0000269|PubMed:10497248}.
MUTAGEN 18 21 YYYY->FFFF: No effect on topology or
activity. {ECO:0000269|PubMed:10497248}.
MUTAGEN 19 21 YYY->AYA: No effect on topology. Reduced
Vmax. {ECO:0000269|PubMed:10497248}.
MUTAGEN 25 26 EE->KK: Inverted topology. Reduced Vmax.
{ECO:0000269|PubMed:15152005}.
MUTAGEN 25 26 EE->KQ: No effect on topology. Reduced
Vmax. {ECO:0000269|PubMed:15152005}.
MUTAGEN 25 26 EE->QQ: Reduced Vmax.
{ECO:0000269|PubMed:15152005}.
MUTAGEN 25 25 E->K,Q: No effect on activity.
{ECO:0000269|PubMed:15152005}.
MUTAGEN 26 26 E->K: No effect on activity.
{ECO:0000269|PubMed:15152005}.
MUTAGEN 35 36 KK->SS: Complete loss of activity.
{ECO:0000269|PubMed:15152005}.
HELIX 29 32 {ECO:0000307|PDB:1XU9}.
STRAND 36 41 {ECO:0000307|PDB:1XU9}.
HELIX 45 56 {ECO:0000307|PDB:1XU9}.
STRAND 60 66 {ECO:0000307|PDB:1XU9}.
HELIX 68 81 {ECO:0000307|PDB:1XU9}.
STRAND 84 90 {ECO:0000307|PDB:1XU9}.
STRAND 93 95 {ECO:0000307|PDB:4YYZ}.
HELIX 96 110 {ECO:0000307|PDB:1XU9}.
STRAND 114 118 {ECO:0000307|PDB:1XU9}.
HELIX 133 143 {ECO:0000307|PDB:1XU9}.
HELIX 145 161 {ECO:0000307|PDB:1XU9}.
STRAND 164 170 {ECO:0000307|PDB:1XU9}.
HELIX 171 173 {ECO:0000307|PDB:1XU9}.
HELIX 181 204 {ECO:0000307|PDB:1XU9}.
STRAND 209 215 {ECO:0000307|PDB:1XU9}.
HELIX 221 226 {ECO:0000307|PDB:1XU9}.
HELIX 229 234 {ECO:0000307|PDB:1XU9}.
HELIX 238 250 {ECO:0000307|PDB:1XU9}.
STRAND 254 258 {ECO:0000307|PDB:1XU9}.
HELIX 262 267 {ECO:0000307|PDB:1XU9}.
HELIX 271 280 {ECO:0000307|PDB:1XU9}.
HELIX 281 283 {ECO:0000307|PDB:1XU9}.
HELIX 287 290 {ECO:0000307|PDB:4C7J}.
SEQUENCE 292 AA; 32401 MW; 4632D0F3BBEFC474 CRC64;
MAFMKKYLLP ILGLFMAYYY YSANEEFRPE MLQGKKVIVT GASKGIGREM AYHLAKMGAH
VVVTARSKET LQKVVSHCLE LGAASAHYIA GTMEDMTFAE QFVAQAGKLM GGLDMLILNH
ITNTSLNLFH DDIHHVRKSM EVNFLSYVVL TVAALPMLKQ SNGSIVVVSS LAGKVAYPMV
AAYSASKFAL DGFFSSIRKE YSVSRVNVSI TLCVLGLIDT ETAMKAVSGI VHMQAAPKEE
CALEIIKGGA LRQEEVYYDS SLWTTLLIRN PCRKILEFLY STSYNMDRFI NK


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