ID C11B1_HUMAN Reviewed; 503 AA. AC P15538; Q14095; Q4VAQ8; Q4VAQ9; Q9UML2; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 5. DT 24-JAN-2024, entry version 225. DE RecName: Full=Cytochrome P450 11B1, mitochondrial; DE Short=CYP11B1; DE AltName: Full=CYPXIB1; DE AltName: Full=Cytochrome P-450c11; DE Short=Cytochrome P450C11; DE AltName: Full=Steroid 11-beta-hydroxylase, CYP11B1 {ECO:0000303|PubMed:2592361}; DE EC=1.14.15.4 {ECO:0000269|PubMed:18215163}; DE Flags: Precursor; GN Name=CYP11B1 {ECO:0000303|PubMed:18215163, GN ECO:0000312|HGNC:HGNC:2591}; Synonyms=S11BH; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT CYS-494. RX PubMed=2592361; DOI=10.1016/s0021-9258(19)30030-4; RA Mornet E., Dupont J., Vitek A., White P.C.; RT "Characterization of two genes encoding human steroid 11 beta-hydroxylase RT (P-450(11) beta)."; RL J. Biol. Chem. 264:20961-20967(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND RP VARIANTS GLN-43 AND VAL-386. RX PubMed=2401360; DOI=10.1016/0014-5793(90)81190-y; RA Kawamoto T., Mitsuuchi Y., Toda K., Miyahara K., Yokoyama Y., Nakao K., RA Hosoda K., Yamamoto Y., Imura H., Shizuta Y.; RT "Cloning of cDNA and genomic DNA for human cytochrome P-45011 beta."; RL FEBS Lett. 269:345-349(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-132. RC TISSUE=Peripheral blood; RX PubMed=7903314; DOI=10.1210/jcem.77.6.7903314; RA Naiki Y., Kawamoto T., Mitsuuchi Y., Miyahara K., Toda K., Orii T., RA Imura H., Shizuta Y.; RT "A nonsense mutation (TGG [Trp116]-->TAG [Stop]) in CYP11B1 causes steroid RT 11 beta-hydroxylase deficiency."; RL J. Clin. Endocrinol. Metab. 77:1677-1682(1993). RN [8] RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 216-466, AND VARIANT VAL-386. RX PubMed=3499608; DOI=10.1073/pnas.84.20.7193; RA Chua S.C., Szabo P., Vitek A., Grzeschik K.H., John M., White P.C.; RT "Cloning of cDNA encoding steroid 11 beta-hydroxylase (P450c11)."; RL Proc. Natl. Acad. Sci. U.S.A. 84:7193-7197(1987). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30. RX PubMed=1741400; DOI=10.1073/pnas.89.4.1458; RA Kawamoto T., Mitsuuchi Y., Toda K., Yokoyama Y., Miyahara K., Miura S., RA Ohnishi T., Icikawa Y., Nakao K., Imura H., Ulick S., Shuzuta Y.; RT "Role of steroid 11 beta-hydroxylase and steroid 18-hydroxylase in the RT biosynthesis of glucocorticoids and mineralocorticoids in humans."; RL Proc. Natl. Acad. Sci. U.S.A. 89:1458-1462(1992). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=1775135; DOI=10.1210/mend-5-10-1513; RA Curnow K.M., Tusie-Luna M.T., Pascoe L., Natarajan R., Gu J.L., RA Nadler J.L., White P.C.; RT "The product of the CYP11B2 gene is required for aldosterone biosynthesis RT in the human adrenal cortex."; RL Mol. Endocrinol. 5:1513-1522(1991). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=1518866; DOI=10.1073/pnas.89.17.8327; RA Pascoe L., Curnow K.M., Slutsker L., Connell J.M., Speiser P.W., New M.I., RA White P.C.; RT "Glucocorticoid-suppressible hyperaldosteronism results from hybrid genes RT created by unequal crossovers between CYP11B1 and CYP11B2."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8327-8331(1992). RN [12] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=12530636; DOI=10.1081/erc-120016808; RA Bureik M., Zeeh A., Bernhardt R.; RT "Modulation of steroid hydroxylase activity in stably transfected RT V79MZh11B1 and V79MZh11B2 cells by PKC and PKD inhibitors."; RL Endocr. Res. 28:351-355(2002). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RX PubMed=18215163; DOI=10.1111/j.1742-4658.2008.06253.x; RA Zoellner A., Kagawa N., Waterman M.R., Nonaka Y., Takio K., Shiro Y., RA Hannemann F., Bernhardt R.; RT "Purification and functional characterization of human 11beta hydroxylase RT expressed in Escherichia coli."; RL FEBS J. 275:799-810(2008). RN [14] RP TISSUE SPECIFICITY. RX PubMed=20200334; DOI=10.1210/jc.2009-2010; RA Nishimoto K., Nakagawa K., Li D., Kosaka T., Oya M., Mikami S., Shibata H., RA Itoh H., Mitani F., Yamazaki T., Ogishima T., Suematsu M., Mukai K.; RT "Adrenocortical zonation in humans under normal and pathological RT conditions."; RL J. Clin. Endocrinol. Metab. 95:2296-2305(2010). RN [15] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23322723; DOI=10.1210/me.2012-1287; RA Strushkevich N., Gilep A.A., Shen L., Arrowsmith C.H., Edwards A.M., RA Usanov S.A., Park H.W.; RT "Structural insights into aldosterone synthase substrate specificity and RT targeted inhibition."; RL Mol. Endocrinol. 27:315-324(2013). RN [16] RP VARIANT AH4 HIS-448. RX PubMed=2022736; DOI=10.1172/jci115182; RA White P.C., Dupont J., New M.I., Leiberman E., Hochberg Z., Roesler A.; RT "A mutation in CYP11B1 (Arg-448-->His) associated with steroid 11 beta- RT hydroxylase deficiency in Jews of Moroccan origin."; RL J. Clin. Invest. 87:1664-1667(1991). RN [17] RP VARIANTS AH4 SER-42; HIS-133 AND MET-319. RX PubMed=9302260; DOI=10.1093/hmg/6.11.1829; RA Joehrer K., Geley S., Strasser-Wozak E.M.C., Azziz R., Wollmann H.A., RA Schmitt K., Kofler R., White P.C.; RT "CYP11B1 mutations causing non-classic adrenal hyperplasia due to 11 beta- RT hydroxylase deficiency."; RL Hum. Mol. Genet. 6:1829-1834(1997). RN [18] RP VARIANT CYS-494. RX PubMed=10599751; DOI=10.1210/jcem.84.12.6272-6; RA Loidi L., Quinteiro C., Barros F., Dominguez F., Barreiro J., Pombo M.; RT "The C494F variant in the CYP11B1 gene is a sequence polymorphism in the RT Spanish population."; RL J. Clin. Endocrinol. Metab. 84:4749-4749(1999). RN [19] RP VARIANTS TYR-10; GLN-43; THR-348 AND VAL-386. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions of RT human genes."; RL Nat. Genet. 22:231-238(1999). RN [20] RP ERRATUM OF PUBMED:10391209. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). RN [21] RP VARIANTS GLN-43; ILE-160 AND VAL-293. RX PubMed=10391210; DOI=10.1038/10297; RA Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., RA Cooper R., Lipshutz R., Chakravarti A.; RT "Patterns of single-nucleotide polymorphisms in candidate genes for blood- RT pressure homeostasis."; RL Nat. Genet. 22:239-247(1999). RN [22] RP VARIANTS AH4 LEU-94; ARG-318 AND HIS-448. RX PubMed=16046588; DOI=10.1210/jc.2005-0379; RA Grigorescu Sido A., Weber M.M., Grigorescu Sido P., Clausmeyer S., RA Heinrich U., Schulze E.; RT "21-Hydroxylase and 11beta-hydroxylase mutations in Romanian patients with RT classic congenital adrenal hyperplasia."; RL J. Clin. Endocrinol. Metab. 90:5769-5773(2005). RN [23] RP VARIANT AH4 VAL-379. RX PubMed=20331679; DOI=10.1111/j.1399-0004.2010.01403.x; RA Kharrat M., Trabelsi S., Chaabouni M., Maazoul F., Kraoua L., Ben Jemaa L., RA Gandoura N., Barsaoui S., Morel Y., M'rad R., Chaabouni H.; RT "Only two mutations detected in 15 Tunisian patients with 11beta- RT hydroxylase deficiency: the p.Q356X and the novel p.G379V."; RL Clin. Genet. 78:398-401(2010). RN [24] RP VARIANTS AH4 SER-42; SER-83; ILE-88; LEU-94; CYS-116; GLY-116; ARG-125; RP MET-129; HIS-133; SER-135; LEU-139; PRO-158; LEU-159; VAL-161 DEL; ASP-165; RP ALA-196; 254-LYS--ALA-259 DEL; ASP-267; PRO-299; VAL-306; ARG-314; ARG-318; RP MET-318; PRO-318; MET-319; VAL-321; VAL-331; SER-341; CYS-366; ASP-368; RP GLY-371; GLN-374; GLN-384; GLY-384; VAL-386; ALA-401; HIS-427; PHE-438 DEL; RP GLY-441; ASP-444; CYS-448; HIS-448; GLN-453 AND SER-489, VARIANT GLN-43, RP CHARACTERIZATION OF VARIANTS AH4 SER-42; SER-83; ILE-88; LEU-94; CYS-116; RP GLY-116; ARG-125; MET-129; HIS-133; SER-135; LEU-139; PRO-158; LEU-159; RP ASP-165; ALA-196; 254-LYS--ALA-259 DEL; PRO-299; ARG-314; MET-318; MET-319; RP VAL-331; CYS-366; ASP-368; GLY-371; GLN-374; GLN-384; ALA-401; PHE-438 DEL; RP GLY-441; CYS-448; HIS-448 AND GLN-453, AND CHARACTERIZATION OF VARIANT RP GLN-43. RX PubMed=20089618; DOI=10.1210/jc.2009-0651; RA Parajes S., Loidi L., Reisch N., Dhir V., Rose I.T., Hampel R., RA Quinkler M., Conway G.S., Castro-Feijoo L., Araujo-Vilar D., Pombo M., RA Dominguez F., Williams E.L., Cole T.R., Kirk J.M., Kaminsky E., Rumsby G., RA Arlt W., Krone N.; RT "Functional consequences of seven novel mutations in the CYP11B1 gene: four RT mutations associated with nonclassic and three mutations causing classic RT 11{beta}-hydroxylase deficiency."; RL J. Clin. Endocrinol. Metab. 95:779-788(2010). RN [25] RP VARIANT AH4 CYS-454. RX PubMed=20947076; DOI=10.1016/j.fertnstert.2010.09.035; RA Wu C., Zhou Q., Wan L., Ni L., Zheng C., Qian Y., Jin J.; RT "Novel homozygous p.R454C mutation in the CYP11B1 gene leads to 11beta- RT hydroxylase deficiency in a Chinese patient."; RL Fertil. Steril. 95:1122-1122(2011). RN [26] RP VARIANT AH4 ILE-79, AND CHARACTERIZATION OF VARIANT AH4 ILE-79. RX PubMed=23940125; DOI=10.1210/jc.2013-1306; RA Reisch N., Hoegler W., Parajes S., Rose I.T., Dhir V., Goetzinger J., RA Arlt W., Krone N.; RT "A diagnosis not to be missed: nonclassic steroid 11beta-hydroxylase RT deficiency presenting with premature adrenarche and hirsutism."; RL J. Clin. Endocrinol. Metab. 98:E1620-E1625(2013). RN [27] RP VARIANTS AH4 LEU-150 AND LEU-463 INS, AND CHARACTERIZATION OF VARIANTS AH4 RP LEU-150 AND LEU-463 INS. RX PubMed=24536089; DOI=10.1530/eje-13-0737; RA Polat S., Kulle A., Karaca Z., Akkurt I., Kurtoglu S., Kelestimur F., RA Groetzinger J., Holterhus P.M., Riepe F.G.; RT "Characterisation of three novel CYP11B1 mutations in classic and non- RT classic 11beta-hydroxylase deficiency."; RL Eur. J. Endocrinol. 170:697-706(2014). RN [28] RP VARIANTS AH4 TRP-143; PRO-299; VAL-306; LYS-310 AND GLN-332, AND RP CHARACTERIZATION OF VARIANTS AH4 TRP-143; VAL-306; LYS-310 AND GLN-332. RX PubMed=24022297; DOI=10.1038/ejhg.2013.197; RA Menabo S., Polat S., Baldazzi L., Kulle A.E., Holterhus P.M., RA Groetzinger J., Fanelli F., Balsamo A., Riepe F.G.; RT "Congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency: RT functional consequences of four CYP11B1 mutations."; RL Eur. J. Hum. Genet. 22:610-616(2014). RN [29] RP VARIANTS AH4 GLN-141; ARG-318 AND HIS-448. RX PubMed=24987415; DOI=10.1155/2014/185974; RA Dumic K., Yuen T., Grubic Z., Kusec V., Barisic I., New M.I.; RT "Two novel CYP11B1 gene mutations in patients from two Croatian families RT with 11 beta-hydroxylase deficiency."; RL Int. J. Endocrinol. 2014:185974-185979(2014). RN [30] RP VARIANTS AH4 LEU-42 AND SER-42, AND CHARACTERIZATION OF VARIANTS AH4 LEU-42 RP AND SER-42. RX PubMed=26053152; DOI=10.1111/cen.12834; RA Mooij C.F., Parajes S., Rose I.T., Taylor A.E., Bayraktaroglu T., RA Wass J.A., Connell J.M., Ray D.W., Arlt W., Krone N.; RT "Characterization of the molecular genetic pathology in patients with RT 11beta-hydroxylase deficiency."; RL Clin. Endocrinol. (Oxf.) 83:629-635(2015). RN [31] RP VARIANTS AH4 ARG-318; GLY-332 AND HIS-448, AND CHARACTERIZATION OF VARIANT RP GLY-332. RX PubMed=26476331; DOI=10.1016/j.jsbmb.2015.10.011; RA Nguyen H.H., Eiden-Plach A., Hannemann F., Malunowicz E.M., Hartmann M.F., RA Wudy S.A., Bernhardt R.; RT "Phenotypic, metabolic, and molecular genetic characterization of six RT patients with congenital adrenal hyperplasia caused by novel mutations in RT the CYP11B1 gene."; RL J. Steroid Biochem. Mol. Biol. 155:126-134(2016). CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the biosynthesis CC of adrenal corticoids (PubMed:1775135, PubMed:1518866, PubMed:12530636, CC PubMed:18215163, PubMed:23322723). Catalyzes a variety of reactions CC that are essential for many species, including detoxification, defense, CC and the formation of endogenous chemicals like steroid hormones. CC Steroid 11beta, 18- and 19-hydroxylase with preferred regioselectivity CC at 11beta, then 18, and lastly 19 (By similarity). Catalyzes the CC hydroxylation of 11-deoxycortisol and 11-deoxycorticosterone (21- CC hydroxyprogesterone) at 11beta position, yielding cortisol or CC corticosterone, respectively, but cannot produce aldosterone CC (PubMed:18215163, PubMed:1518866, PubMed:1775135, PubMed:12530636, CC PubMed:23322723). Mechanistically, uses molecular oxygen inserting one CC oxygen atom into a substrate for hydroxylation and reducing the second CC into a water molecule. Two electrons are provided by NADPH via a two- CC protein mitochondrial transfer system comprising flavoprotein FDXR CC (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 CC or FDX2 (adrenodoxin/ferredoxin) (PubMed:18215163). Due to its lack of CC 18-oxidation activity, it is incapable of generating aldosterone CC (PubMed:23322723). Could also be involved in the androgen metabolic CC pathway (Probable). {ECO:0000250|UniProtKB:P15393, CC ECO:0000269|PubMed:12530636, ECO:0000269|PubMed:1518866, CC ECO:0000269|PubMed:1775135, ECO:0000269|PubMed:18215163, CC ECO:0000269|PubMed:23322723, ECO:0000305|PubMed:23322723}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a steroid + 2 H(+) + O2 + 2 reduced [adrenodoxin] = an 11beta- CC hydroxysteroid + H2O + 2 oxidized [adrenodoxin]; CC Xref=Rhea:RHEA:15629, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:35341, CC ChEBI:CHEBI:35346; EC=1.14.15.4; CC Evidence={ECO:0000269|PubMed:12530636, ECO:0000269|PubMed:1518866, CC ECO:0000269|PubMed:1775135, ECO:0000269|PubMed:18215163, CC ECO:0000269|PubMed:23322723}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15630; CC Evidence={ECO:0000305|PubMed:12530636, ECO:0000305|PubMed:1518866, CC ECO:0000305|PubMed:1775135, ECO:0000305|PubMed:18215163, CC ECO:0000305|PubMed:23322723}; CC -!- CATALYTIC ACTIVITY: CC Reaction=11-deoxycortisol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = CC cortisol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:46100, CC Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17650, CC ChEBI:CHEBI:28324, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; CC Evidence={ECO:0000269|PubMed:12530636, ECO:0000269|PubMed:1775135, CC ECO:0000269|PubMed:18215163, ECO:0000269|PubMed:23322723}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46101; CC Evidence={ECO:0000305|PubMed:12530636, ECO:0000305|PubMed:1775135, CC ECO:0000305|PubMed:18215163, ECO:0000305|PubMed:23322723}; CC -!- CATALYTIC ACTIVITY: CC Reaction=21-hydroxyprogesterone + 2 H(+) + O2 + 2 reduced [adrenodoxin] CC = corticosterone + H2O + 2 oxidized [adrenodoxin]; CC Xref=Rhea:RHEA:46104, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16827, ChEBI:CHEBI:16973, ChEBI:CHEBI:33737, CC ChEBI:CHEBI:33738; Evidence={ECO:0000269|PubMed:12530636, CC ECO:0000269|PubMed:1518866, ECO:0000269|PubMed:1775135, CC ECO:0000269|PubMed:18215163, ECO:0000269|PubMed:23322723}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46105; CC Evidence={ECO:0000305|PubMed:12530636, ECO:0000305|PubMed:1518866, CC ECO:0000305|PubMed:1775135, ECO:0000305|PubMed:18215163, CC ECO:0000305|PubMed:23322723}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000250|UniProtKB:P19099}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=338.4 uM for 11-deoxycortisol {ECO:0000269|PubMed:18215163}; CC KM=179.5 uM for 21-hydroxyprogesterone {ECO:0000269|PubMed:18215163}; CC Note=kcat is 1.67 sec(-1) with 11-deoxycortisol as substrate. kcat is CC 0.85 sec(-1) with 21-hydroxyprogesterone as substrate. CC {ECO:0000269|PubMed:18215163}; CC -!- PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis. CC {ECO:0000269|PubMed:18215163}. CC -!- PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:18215163}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P14137}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P15538-1; Sequence=Displayed; CC Name=2; CC IsoId=P15538-2; Sequence=VSP_043308; CC -!- TISSUE SPECIFICITY: Expressed in the zona fasciculata/reticularis of CC the adrenal cortex. {ECO:0000269|PubMed:20200334}. CC -!- DISEASE: Adrenal hyperplasia 4 (AH4) [MIM:202010]: A form of congenital CC adrenal hyperplasia, a common recessive disease due to defective CC synthesis of cortisol. Congenital adrenal hyperplasia is characterized CC by androgen excess leading to ambiguous genitalia in affected females, CC rapid somatic growth during childhood in both sexes with premature CC closure of the epiphyses and short adult stature. Four clinical types: CC 'salt wasting' (SW, the most severe type), 'simple virilizing' (SV, CC less severely affected patients), with normal aldosterone biosynthesis, CC 'non-classic form' or late-onset (NC or LOAH) and 'cryptic' CC (asymptomatic). {ECO:0000269|PubMed:16046588, CC ECO:0000269|PubMed:20089618, ECO:0000269|PubMed:2022736, CC ECO:0000269|PubMed:20331679, ECO:0000269|PubMed:20947076, CC ECO:0000269|PubMed:23940125, ECO:0000269|PubMed:24022297, CC ECO:0000269|PubMed:24536089, ECO:0000269|PubMed:24987415, CC ECO:0000269|PubMed:26053152, ECO:0000269|PubMed:26476331, CC ECO:0000269|PubMed:9302260}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Hyperaldosteronism, familial, 1 (HALD1) [MIM:103900]: A CC disorder characterized by hypertension, variable hyperaldosteronism, CC and abnormal adrenal steroid production, including 18-oxocortisol and CC 18-hydroxycortisol. There is significant phenotypic heterogeneity, and CC some individuals never develop hypertension. Note=The disease is caused CC by variants affecting the gene represented in this entry. The molecular CC defect causing hyperaldosteronism familial 1 is an anti-Lepore-type CC fusion of the CYP11B1 and CYP11B2 genes. The hybrid gene has the CC promoting part of CYP11B1, ACTH-sensitive, and the coding part of CC CYP11B2. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M32879; AAA52149.1; -; Genomic_DNA. DR EMBL; M32863; AAA52149.1; JOINED; Genomic_DNA. DR EMBL; M32878; AAA52149.1; JOINED; Genomic_DNA. DR EMBL; X55764; CAA39290.1; -; mRNA. DR EMBL; D16153; BAB71992.1; -; Genomic_DNA. DR EMBL; D16155; BAA03717.1; -; Genomic_DNA. DR EMBL; EU332839; ABY87528.1; -; Genomic_DNA. DR EMBL; AC083841; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471162; EAW82293.1; -; Genomic_DNA. DR EMBL; BC096286; AAH96286.1; -; mRNA. DR EMBL; BC096287; AAH96287.1; -; mRNA. DR EMBL; M24667; AAA52148.1; ALT_SEQ; mRNA. DR EMBL; D10169; BAA01039.1; -; Genomic_DNA. DR CCDS; CCDS34953.1; -. [P15538-2] DR CCDS; CCDS6392.1; -. [P15538-1] DR PIR; S11338; S11338. DR RefSeq; NP_000488.3; NM_000497.3. [P15538-1] DR RefSeq; NP_001021384.1; NM_001026213.1. [P15538-2] DR PDB; 6M7X; X-ray; 2.10 A; A/B=31-503. DR PDB; 7E7F; X-ray; 1.40 A; A=28-503. DR PDBsum; 6M7X; -. DR PDBsum; 7E7F; -. DR AlphaFoldDB; P15538; -. DR SMR; P15538; -. DR BioGRID; 107956; 3. DR IntAct; P15538; 1. DR STRING; 9606.ENSP00000292427; -. DR BindingDB; P15538; -. DR ChEMBL; CHEMBL1908; -. DR DrugBank; DB04630; Aldosterone. DR DrugBank; DB00501; Cimetidine. DR DrugBank; DB01234; Dexamethasone. DR DrugBank; DB14649; Dexamethasone acetate. DR DrugBank; DB00292; Etomidate. DR DrugBank; DB00741; Hydrocortisone. DR DrugBank; DB14539; Hydrocortisone acetate. DR DrugBank; DB14540; Hydrocortisone butyrate. DR DrugBank; DB14543; Hydrocortisone probutate. DR DrugBank; DB14545; Hydrocortisone succinate. DR DrugBank; DB14544; Hydrocortisone valerate. DR DrugBank; DB01026; Ketoconazole. DR DrugBank; DB05667; Levoketoconazole. DR DrugBank; DB01011; Metyrapone. DR DrugBank; DB01388; Mibefradil. DR DrugBank; DB01110; Miconazole. DR DrugBank; DB00648; Mitotane. DR DrugBank; DB11837; Osilodrostat. DR DrugBank; DB00252; Phenytoin. DR DrugBank; DB00421; Spironolactone. DR DrugCentral; P15538; -. DR GuidetoPHARMACOLOGY; 1359; -. DR SwissLipids; SLP:000001197; -. DR iPTMnet; P15538; -. DR PhosphoSitePlus; P15538; -. DR BioMuta; CYP11B1; -. DR DMDM; 215274267; -. DR MassIVE; P15538; -. DR PaxDb; 9606-ENSP00000292427; -. DR PeptideAtlas; P15538; -. DR ProteomicsDB; 53185; -. [P15538-1] DR ProteomicsDB; 53186; -. [P15538-2] DR Antibodypedia; 27799; 284 antibodies from 23 providers. DR DNASU; 1584; -. DR Ensembl; ENST00000292427.10; ENSP00000292427.5; ENSG00000160882.13. [P15538-1] DR Ensembl; ENST00000517471.5; ENSP00000428043.1; ENSG00000160882.13. [P15538-2] DR GeneID; 1584; -. DR KEGG; hsa:1584; -. DR MANE-Select; ENST00000292427.10; ENSP00000292427.5; NM_000497.4; NP_000488.3. DR UCSC; uc003yxi.4; human. [P15538-1] DR AGR; HGNC:2591; -. DR CTD; 1584; -. DR DisGeNET; 1584; -. DR GeneCards; CYP11B1; -. DR HGNC; HGNC:2591; CYP11B1. DR HPA; ENSG00000160882; Tissue enriched (adrenal). DR MalaCards; CYP11B1; -. DR MIM; 103900; phenotype. DR MIM; 202010; phenotype. DR MIM; 610613; gene. DR neXtProt; NX_P15538; -. DR OpenTargets; ENSG00000160882; -. DR Orphanet; 90795; Congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency. DR Orphanet; 403; Familial hyperaldosteronism type I. DR PharmGKB; PA133; -. DR VEuPathDB; HostDB:ENSG00000160882; -. DR eggNOG; KOG0159; Eukaryota. DR GeneTree; ENSGT00940000163354; -. DR HOGENOM; CLU_001570_28_4_1; -. DR InParanoid; P15538; -. DR OMA; RNHKCGV; -. DR OrthoDB; 2658719at2759; -. DR PhylomeDB; P15538; -. DR TreeFam; TF105094; -. DR BioCyc; MetaCyc:HS08547-MONOMER; -. DR BRENDA; 1.14.15.4; 2681. DR PathwayCommons; P15538; -. DR Reactome; R-HSA-194002; Glucocorticoid biosynthesis. DR Reactome; R-HSA-211976; Endogenous sterols. DR Reactome; R-HSA-5579017; Defective CYP11B1 causes AH4. DR SignaLink; P15538; -. DR SIGNOR; P15538; -. DR UniPathway; UPA00788; -. DR BioGRID-ORCS; 1584; 16 hits in 1149 CRISPR screens. DR ChiTaRS; CYP11B1; human. DR GeneWiki; Steroid_11-beta-hydroxylase; -. DR GenomeRNAi; 1584; -. DR Pharos; P15538; Tclin. DR PRO; PR:P15538; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P15538; Protein. DR Bgee; ENSG00000160882; Expressed in right adrenal gland cortex and 80 other cell types or tissues. DR ExpressionAtlas; P15538; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL. DR GO; GO:0047783; F:corticosterone 18-monooxygenase activity; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; IC:BHF-UCL. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004507; F:steroid 11-beta-monooxygenase activity; IDA:BHF-UCL. DR GO; GO:0032342; P:aldosterone biosynthetic process; IDA:BHF-UCL. DR GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IDA:BHF-UCL. DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB. DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IBA:GO_Central. DR GO; GO:0035865; P:cellular response to potassium ion; IEP:UniProtKB. DR GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central. DR GO; GO:0034651; P:cortisol biosynthetic process; IDA:BHF-UCL. DR GO; GO:0034650; P:cortisol metabolic process; IBA:GO_Central. DR GO; GO:0006704; P:glucocorticoid biosynthetic process; IBA:GO_Central. DR GO; GO:0042593; P:glucose homeostasis; TAS:BHF-UCL. DR GO; GO:0006955; P:immune response; TAS:BHF-UCL. DR GO; GO:0008217; P:regulation of blood pressure; IMP:BHF-UCL. DR GO; GO:0016125; P:sterol metabolic process; TAS:Reactome. DR CDD; cd20644; CYP11B; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002399; Cyt_P450_mitochondrial. DR InterPro; IPR036396; Cyt_P450_sf. DR PANTHER; PTHR24279; -; 1. DR PANTHER; PTHR24279:SF115; CYTOCHROME P450 11B1, MITOCHONDRIAL; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00408; MITP450. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. DR Genevisible; P15538; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Congenital adrenal hyperplasia; KW Direct protein sequencing; Disease variant; Heme; Iron; Lipid biosynthesis; KW Lipid metabolism; Membrane; Metal-binding; Mitochondrion; KW Mitochondrion inner membrane; Monooxygenase; Oxidoreductase; KW Reference proteome; Steroid biosynthesis; Steroidogenesis; Transit peptide. FT TRANSIT 1..24 FT /note="Mitochondrion" FT CHAIN 25..503 FT /note="Cytochrome P450 11B1, mitochondrial" FT /id="PRO_0000003596" FT BINDING 450 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P19099" FT VAR_SEQ 401..466 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043308" FT VARIANT 10 FT /note="C -> Y (in dbSNP:rs6405)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_014145" FT VARIANT 42 FT /note="P -> L (in AH4; classic; highly decreases steroid FT 11-beta-hydroxylase activity; dbSNP:rs193922538)" FT /evidence="ECO:0000269|PubMed:26053152" FT /id="VAR_074493" FT VARIANT 42 FT /note="P -> S (in AH4; non-classic; highly decreases FT steroid 11-beta-hydroxylase activity; dbSNP:rs104894069)" FT /evidence="ECO:0000269|PubMed:20089618, FT ECO:0000269|PubMed:26053152, ECO:0000269|PubMed:9302260" FT /id="VAR_001260" FT VARIANT 43 FT /note="R -> Q (decreases steroid 11-beta-hydroxylase FT activity; dbSNP:rs4534)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:10391210, ECO:0000269|PubMed:20089618, FT ECO:0000269|PubMed:2401360" FT /id="VAR_014146" FT VARIANT 63 FT /note="D -> H (in dbSNP:rs5282)" FT /id="VAR_014638" FT VARIANT 79 FT /note="F -> I (in AH4; non-classic; highly decreases FT steroid 11-beta-hydroxylase activity; dbSNP:rs1489638195)" FT /evidence="ECO:0000269|PubMed:23940125" FT /id="VAR_074494" FT VARIANT 83 FT /note="L -> S (in AH4; highly decreases steroid FT 11-beta-hydroxylase activity)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074495" FT VARIANT 88 FT /note="M -> I (in AH4; slightly decreases steroid FT 11-beta-hydroxylase activity; dbSNP:rs193922539)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074496" FT VARIANT 94 FT /note="P -> L (in AH4; almost abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs104894070)" FT /evidence="ECO:0000269|PubMed:16046588, FT ECO:0000269|PubMed:20089618" FT /id="VAR_065666" FT VARIANT 116 FT /note="W -> C (in AH4; almost abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs772003869)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074497" FT VARIANT 116 FT /note="W -> G (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs772733691)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074498" FT VARIANT 125 FT /note="H -> R (in AH4; slightly decreases steroid FT 11-beta-hydroxylase activity; dbSNP:rs757389720)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074499" FT VARIANT 129 FT /note="V -> M (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs377423817)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074500" FT VARIANT 133 FT /note="N -> H (in AH4; non-classic; highly decreases FT steroid 11-beta-hydroxylase activity; dbSNP:rs104894067)" FT /evidence="ECO:0000269|PubMed:20089618, FT ECO:0000269|PubMed:9302260" FT /id="VAR_001261" FT VARIANT 135 FT /note="P -> S (in AH4; highly decreases steroid FT 11-beta-hydroxylase activity)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074501" FT VARIANT 139 FT /note="F -> L (in AH4; decreases steroid FT 11-beta-hydroxylase activity)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074502" FT VARIANT 141 FT /note="R -> Q (in AH4; uncertain significance; FT dbSNP:rs267601810)" FT /evidence="ECO:0000269|PubMed:24987415" FT /id="VAR_075553" FT VARIANT 143 FT /note="R -> W (in AH4; non-classic; highly decreases FT steroid 11-beta-hydroxylase activity; dbSNP:rs140336749)" FT /evidence="ECO:0000269|PubMed:24022297" FT /id="VAR_074503" FT VARIANT 150 FT /note="S -> L (in AH4; non-classic; highly decreases FT steroid 11-beta-hydroxylase activity; dbSNP:rs142484434)" FT /evidence="ECO:0000269|PubMed:24536089" FT /id="VAR_074504" FT VARIANT 158 FT /note="L -> P (in AH4; highly decreases steroid FT 11-beta-hydroxylase activity; dbSNP:rs1554653191)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074505" FT VARIANT 159 FT /note="P -> L (in AH4; decreases steroid FT 11-beta-hydroxylase activity; dbSNP:rs370266763)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074506" FT VARIANT 160 FT /note="M -> I (in dbSNP:rs5287)" FT /evidence="ECO:0000269|PubMed:10391210" FT /id="VAR_014147" FT VARIANT 161 FT /note="Missing (in AH4)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074507" FT VARIANT 165 FT /note="A -> D (in AH4; almost abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs1554653185)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074508" FT VARIANT 173 FT /note="K -> R (in dbSNP:rs142163070)" FT /id="VAR_014639" FT VARIANT 196 FT /note="T -> A (in AH4; decreases steroid FT 11-beta-hydroxylase activity)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074509" FT VARIANT 248 FT /note="T -> I (in dbSNP:rs34620645)" FT /id="VAR_048462" FT VARIANT 254..259 FT /note="Missing (in AH4; abolishes steroid FT 11-beta-hydroxylase activity)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074510" FT VARIANT 257 FT /note="F -> L (in dbSNP:rs5288)" FT /id="VAR_014640" FT VARIANT 267 FT /note="G -> D (in AH4)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074511" FT VARIANT 281 FT /note="S -> N (in dbSNP:rs5291)" FT /id="VAR_014641" FT VARIANT 293 FT /note="L -> V (in dbSNP:rs5292)" FT /evidence="ECO:0000269|PubMed:10391210" FT /id="VAR_014148" FT VARIANT 299 FT /note="L -> P (in AH4; non-classic; almost abolishes FT steroid 11-beta-hydroxylase activity; dbSNP:rs387907573)" FT /evidence="ECO:0000269|PubMed:20089618, FT ECO:0000269|PubMed:24022297" FT /id="VAR_074512" FT VARIANT 306 FT /note="A -> V (in AH4; non-classic; almost abolishes FT steroid 11-beta-hydroxylase activity; dbSNP:rs387907572)" FT /evidence="ECO:0000269|PubMed:20089618, FT ECO:0000269|PubMed:24022297" FT /id="VAR_074513" FT VARIANT 310 FT /note="E -> K (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs387907574)" FT /evidence="ECO:0000269|PubMed:24022297" FT /id="VAR_074514" FT VARIANT 314 FT /note="G -> R (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs1336285846)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074515" FT VARIANT 318 FT /note="T -> M (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs104894061)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_001262" FT VARIANT 318 FT /note="T -> P (in AH4; dbSNP:rs1296969984)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074516" FT VARIANT 318 FT /note="T -> R (in AH4; dbSNP:rs104894061)" FT /evidence="ECO:0000269|PubMed:16046588, FT ECO:0000269|PubMed:20089618, ECO:0000269|PubMed:24987415, FT ECO:0000269|PubMed:26476331" FT /id="VAR_065667" FT VARIANT 319 FT /note="T -> M (in AH4; non-classic; decreases steroid FT 11-beta-hydroxylase activity; dbSNP:rs104894068)" FT /evidence="ECO:0000269|PubMed:20089618, FT ECO:0000269|PubMed:9302260" FT /id="VAR_001263" FT VARIANT 321 FT /note="F -> V (in AH4; dbSNP:rs1453371113)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074517" FT VARIANT 331 FT /note="A -> V (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs1326688256)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074518" FT VARIANT 332 FT /note="R -> G (in AH4; high reduction of steroid FT 11-beta-monooxygenase activity)" FT /evidence="ECO:0000269|PubMed:26476331" FT /id="VAR_075554" FT VARIANT 332 FT /note="R -> Q (in AH4; non-classic; highly decreases FT steroid 11-beta-hydroxylase activity; dbSNP:rs149881706)" FT /evidence="ECO:0000269|PubMed:24022297" FT /id="VAR_074519" FT VARIANT 341 FT /note="R -> S (in AH4; uncertain significance; FT dbSNP:rs372115638)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074520" FT VARIANT 348 FT /note="A -> T (in dbSNP:rs6407)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_014149" FT VARIANT 366 FT /note="R -> C (in AH4; decreases steroid FT 11-beta-hydroxylase activity; dbSNP:rs773245244)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074521" FT VARIANT 368 FT /note="A -> D (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs104894071)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074522" FT VARIANT 371 FT /note="E -> G (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs368944209)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074523" FT VARIANT 374 FT /note="R -> Q (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs104894062)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_001264" FT VARIANT 379 FT /note="G -> V (in AH4; dbSNP:rs1816901292)" FT /evidence="ECO:0000269|PubMed:20331679" FT /id="VAR_065196" FT VARIANT 384 FT /note="R -> G (in AH4)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074524" FT VARIANT 384 FT /note="R -> Q (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs764598023)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074525" FT VARIANT 386 FT /note="A -> V (in dbSNP:rs4541)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:20089618, ECO:0000269|PubMed:2401360, FT ECO:0000269|PubMed:3499608" FT /id="VAR_014150" FT VARIANT 401 FT /note="T -> A (in AH4; decreases steroid FT 11-beta-hydroxylase activity; dbSNP:rs201300785)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074526" FT VARIANT 404 FT /note="R -> H (in dbSNP:rs4998896)" FT /id="VAR_048463" FT VARIANT 427 FT /note="R -> H (in AH4; uncertain significance; FT dbSNP:rs754432887)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074527" FT VARIANT 438 FT /note="Missing (in AH4; abolishes steroid FT 11-beta-hydroxylase activity)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074528" FT VARIANT 439 FT /note="Y -> H (in dbSNP:rs5294)" FT /id="VAR_014642" FT VARIANT 441 FT /note="V -> G (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs772169059)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074529" FT VARIANT 444 FT /note="G -> D (in AH4; dbSNP:rs779103938)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074530" FT VARIANT 448 FT /note="R -> C (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs1221010438)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074531" FT VARIANT 448 FT /note="R -> H (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs28934586)" FT /evidence="ECO:0000269|PubMed:16046588, FT ECO:0000269|PubMed:20089618, ECO:0000269|PubMed:2022736, FT ECO:0000269|PubMed:24987415, ECO:0000269|PubMed:26476331" FT /id="VAR_001265" FT VARIANT 453 FT /note="R -> Q (in AH4; abolishes steroid FT 11-beta-hydroxylase activity; dbSNP:rs1447069098)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074532" FT VARIANT 454 FT /note="R -> C (in AH4; dbSNP:rs1563867899)" FT /evidence="ECO:0000269|PubMed:20947076" FT /id="VAR_065197" FT VARIANT 463 FT /note="L -> LL (in AH4; classic; abolishes steroid FT 11-beta-hydroxylase activity)" FT /evidence="ECO:0000269|PubMed:24536089" FT /id="VAR_074533" FT VARIANT 489 FT /note="L -> S (in AH4; dbSNP:rs750428278)" FT /evidence="ECO:0000269|PubMed:20089618" FT /id="VAR_074534" FT VARIANT 494 FT /note="F -> C" FT /evidence="ECO:0000269|PubMed:10599751, FT ECO:0000269|PubMed:2592361" FT /id="VAR_008687" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 52..59 FT /evidence="ECO:0007829|PDB:7E7F" FT TURN 60..63 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 64..75 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 77..83 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 86..91 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 94..102 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 114..123 FT /evidence="ECO:0007829|PDB:7E7F" FT TURN 129..131 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 134..148 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 151..178 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 182..186 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 189..205 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 218..238 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 242..244 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 245..280 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 289..296 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 301..313 FT /evidence="ECO:0007829|PDB:7E7F" FT TURN 314..317 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 320..332 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 334..353 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 355..357 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 358..361 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 363..375 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 378..385 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 390..392 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 395..397 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 402..406 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 407..411 FT /evidence="ECO:0007829|PDB:7E7F" FT TURN 414..416 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 417..419 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 426..430 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 436..438 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 446..448 FT /evidence="ECO:0007829|PDB:7E7F" FT HELIX 453..470 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 471..474 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 483..493 FT /evidence="ECO:0007829|PDB:7E7F" FT STRAND 497..501 FT /evidence="ECO:0007829|PDB:7E7F" SQ SEQUENCE 503 AA; 57573 MW; 0B36D82513960EE9 CRC64; MALRAKAEVC MAVPWLSLQR AQALGTRAAR VPRTVLPFEA MPRRPGNRWL RLLQIWREQG YEDLHLEVHQ TFQELGPIFR YDLGGAGMVC VMLPEDVEKL QQVDSLHPHR MSLEPWVAYR QHRGHKCGVF LLNGPEWRFN RLRLNPEVLS PNAVQRFLPM VDAVARDFSQ ALKKKVLQNA RGSLTLDVQP SIFHYTIEAS NLALFGERLG LVGHSPSSAS LNFLHALEVM FKSTVQLMFM PRSLSRWTSP KVWKEHFEAW DCIFQYGDNC IQKIYQELAF SRPQQYTSIV AELLLNAELS PDAIKANSME LTAGSVDTTV FPLLMTLFEL ARNPNVQQAL RQESLAAAAS ISEHPQKATT ELPLLRAALK ETLRLYPVGL FLERVASSDL VLQNYHIPAG TLVRVFLYSL GRNPALFPRP ERYNPQRWLD IRGSGRNFYH VPFGFGMRQC LGRRLAEAEM LLLLHHVLKH LQVETLTQED IKMVYSFILR PSMFPLLTFR AIN //