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Cytochrome P450 11B1, mitochondrial (CYPXIB1) (Cytochrome P-450c11) (Cytochrome P450C11) (Steroid 11-beta-hydroxylase) (EC 1.14.15.4)

 C11B1_HUMAN             Reviewed;         503 AA.
P15538; Q14095; Q4VAQ8; Q4VAQ9; Q9UML2;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 5.
27-SEP-2017, entry version 190.
RecName: Full=Cytochrome P450 11B1, mitochondrial;
AltName: Full=CYPXIB1;
AltName: Full=Cytochrome P-450c11;
Short=Cytochrome P450C11;
AltName: Full=Steroid 11-beta-hydroxylase;
EC=1.14.15.4;
Flags: Precursor;
Name=CYP11B1; Synonyms=S11BH;
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], AND VARIANT CYS-494.
PubMed=2592361;
Mornet E., Dupont J., Vitek A., White P.C.;
"Characterization of two genes encoding human steroid 11 beta-
hydroxylase (P-450(11) beta).";
J. Biol. Chem. 264:20961-20967(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
VARIANTS GLN-43 AND VAL-386.
PubMed=2401360; DOI=10.1016/0014-5793(90)81190-Y;
Kawamoto T., Mitsuuchi Y., Toda K., Miyahara K., Yokoyama Y.,
Nakao K., Hosoda K., Yamamoto Y., Imura H., Shizuta Y.;
"Cloning of cDNA and genomic DNA for human cytochrome P-45011 beta.";
FEBS Lett. 269:345-349(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(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] (ISOFORMS 1 AND 2).
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-132.
TISSUE=Peripheral blood;
PubMed=7903314; DOI=10.1210/jcem.77.6.7903314;
Naiki Y., Kawamoto T., Mitsuuchi Y., Miyahara K., Toda K., Orii T.,
Imura H., Shizuta Y.;
"A nonsense mutation (TGG [Trp116]-->TAG [Stop]) in CYP11B1 causes
steroid 11 beta-hydroxylase deficiency.";
J. Clin. Endocrinol. Metab. 77:1677-1682(1993).
[8]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 216-466, AND VARIANT
VAL-386.
PubMed=3499608; DOI=10.1073/pnas.84.20.7193;
Chua S.C., Szabo P., Vitek A., Grzeschik K.H., John M., White P.C.;
"Cloning of cDNA encoding steroid 11 beta-hydroxylase (P450c11).";
Proc. Natl. Acad. Sci. U.S.A. 84:7193-7197(1987).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
PubMed=1741400; DOI=10.1073/pnas.89.4.1458;
Kawamoto T., Mitsuuchi Y., Toda K., Yokoyama Y., Miyahara K.,
Miura S., Ohnishi T., Icikawa Y., Nakao K., Imura H., Ulick S.,
Shuzuta Y.;
"Role of steroid 11 beta-hydroxylase and steroid 18-hydroxylase in the
biosynthesis of glucocorticoids and mineralocorticoids in humans.";
Proc. Natl. Acad. Sci. U.S.A. 89:1458-1462(1992).
[10]
VARIANT AH4 HIS-448.
PubMed=2022736; DOI=10.1172/JCI115182;
White P.C., Dupont J., New M.I., Leiberman E., Hochberg Z.,
Roesler A.;
"A mutation in CYP11B1 (Arg-448-->His) associated with steroid 11
beta-hydroxylase deficiency in Jews of Moroccan origin.";
J. Clin. Invest. 87:1664-1667(1991).
[11]
VARIANTS AH4 SER-42; HIS-133 AND MET-319.
PubMed=9302260; DOI=10.1093/hmg/6.11.1829;
Joehrer K., Geley S., Strasser-Wozak E.M.C., Azziz R., Wollmann H.A.,
Schmitt K., Kofler R., White P.C.;
"CYP11B1 mutations causing non-classic adrenal hyperplasia due to 11
beta-hydroxylase deficiency.";
Hum. Mol. Genet. 6:1829-1834(1997).
[12]
VARIANT CYS-494.
PubMed=10599751; DOI=10.1210/jcem.84.12.6272-6;
Loidi L., Quinteiro C., Barros F., Dominguez F., Barreiro J.,
Pombo M.;
"The C494F variant in the CYP11B1 gene is a sequence polymorphism in
the Spanish population.";
J. Clin. Endocrinol. Metab. 84:4749-4749(1999).
[13]
VARIANTS TYR-10; GLN-43; THR-348 AND VAL-386.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[14]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[15]
VARIANTS GLN-43; ILE-160 AND VAL-293.
PubMed=10391210; DOI=10.1038/10297;
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
Cooper R., Lipshutz R., Chakravarti A.;
"Patterns of single-nucleotide polymorphisms in candidate genes for
blood-pressure homeostasis.";
Nat. Genet. 22:239-247(1999).
[16]
VARIANTS AH4 LEU-94; ARG-318 AND HIS-448.
PubMed=16046588; DOI=10.1210/jc.2005-0379;
Grigorescu Sido A., Weber M.M., Grigorescu Sido P., Clausmeyer S.,
Heinrich U., Schulze E.;
"21-Hydroxylase and 11beta-hydroxylase mutations in Romanian patients
with classic congenital adrenal hyperplasia.";
J. Clin. Endocrinol. Metab. 90:5769-5773(2005).
[17]
VARIANT AH4 VAL-379.
PubMed=20331679; DOI=10.1111/j.1399-0004.2010.01403.x;
Kharrat M., Trabelsi S., Chaabouni M., Maazoul F., Kraoua L.,
Ben Jemaa L., Gandoura N., Barsaoui S., Morel Y., M'rad R.,
Chaabouni H.;
"Only two mutations detected in 15 Tunisian patients with 11beta-
hydroxylase deficiency: the p.Q356X and the novel p.G379V.";
Clin. Genet. 78:398-401(2010).
[18]
VARIANTS AH4 SER-42; GLN-43; SER-83; ILE-88; LEU-94; CYS-116; GLY-116;
ARG-125; MET-129; HIS-133; SER-135; LEU-139; PRO-158; LEU-159; VAL-161
DEL; ASP-165; ALA-196; 254-LYS--ALA-259 DEL; ASP-267; PRO-299;
VAL-306; ARG-314; ARG-318; MET-318; PRO-318; MET-319; VAL-321;
VAL-331; SER-341; CYS-366; ASP-368; GLY-371; GLN-374; GLN-384;
GLY-384; VAL-386; ALA-401; HIS-427; PHE-438 DEL; GLY-441; ASP-444;
CYS-448; HIS-448; GLN-453 AND SER-489, AND CHARACTERIZATION OF
VARIANTS AH4 SER-42; GLN-43; SER-83; ILE-88; LEU-94; CYS-116; GLY-116;
ARG-125; MET-129; HIS-133; SER-135; LEU-139; PRO-158; LEU-159;
ASP-165; ALA-196; 254-LYS--ALA-259 DEL; PRO-299; ARG-314; MET-318;
MET-319; VAL-331; CYS-366; ASP-368; GLY-371; GLN-374; GLN-384;
ALA-401; PHE-438 DEL; GLY-441; CYS-448; HIS-448 AND GLN-453.
PubMed=20089618; DOI=10.1210/jc.2009-0651;
Parajes S., Loidi L., Reisch N., Dhir V., Rose I.T., Hampel R.,
Quinkler M., Conway G.S., Castro-Feijoo L., Araujo-Vilar D., Pombo M.,
Dominguez F., Williams E.L., Cole T.R., Kirk J.M., Kaminsky E.,
Rumsby G., Arlt W., Krone N.;
"Functional consequences of seven novel mutations in the CYP11B1 gene:
four mutations associated with nonclassic and three mutations causing
classic 11{beta}-hydroxylase deficiency.";
J. Clin. Endocrinol. Metab. 95:779-788(2010).
[19]
VARIANT AH4 CYS-454.
PubMed=20947076; DOI=10.1016/j.fertnstert.2010.09.035;
Wu C., Zhou Q., Wan L., Ni L., Zheng C., Qian Y., Jin J.;
"Novel homozygous p.R454C mutation in the CYP11B1 gene leads to
11beta-hydroxylase deficiency in a Chinese patient.";
Fertil. Steril. 95:1122-1122(2011).
[20]
VARIANT AH4 ILE-79, AND CHARACTERIZATION OF VARIANT AH4 ILE-79.
PubMed=23940125; DOI=10.1210/jc.2013-1306;
Reisch N., Hoegler W., Parajes S., Rose I.T., Dhir V., Goetzinger J.,
Arlt W., Krone N.;
"A diagnosis not to be missed: nonclassic steroid 11beta-hydroxylase
deficiency presenting with premature adrenarche and hirsutism.";
J. Clin. Endocrinol. Metab. 98:E1620-E1625(2013).
[21]
VARIANTS AH4 LEU-150 AND LEU-463 INS, AND CHARACTERIZATION OF VARIANTS
AH4 LEU-150 AND LEU-463 INS.
PubMed=24536089; DOI=10.1530/EJE-13-0737;
Polat S., Kulle A., Karaca Z., Akkurt I., Kurtoglu S., Kelestimur F.,
Groetzinger J., Holterhus P.M., Riepe F.G.;
"Characterisation of three novel CYP11B1 mutations in classic and non-
classic 11beta-hydroxylase deficiency.";
Eur. J. Endocrinol. 170:697-706(2014).
[22]
VARIANTS AH4 TRP-143; PRO-299; VAL-306; LYS-310 AND GLN-332, AND
CHARACTERIZATION OF VARIANTS AH4 TRP-143; VAL-306; LYS-310 AND
GLN-332.
PubMed=24022297; DOI=10.1038/ejhg.2013.197;
Menabo S., Polat S., Baldazzi L., Kulle A.E., Holterhus P.M.,
Groetzinger J., Fanelli F., Balsamo A., Riepe F.G.;
"Congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency:
functional consequences of four CYP11B1 mutations.";
Eur. J. Hum. Genet. 22:610-616(2014).
[23]
VARIANTS AH4 GLN-141; ARG-318 AND HIS-448.
PubMed=24987415; DOI=10.1155/2014/185974;
Dumic K., Yuen T., Grubic Z., Kusec V., Barisic I., New M.I.;
"Two novel CYP11B1 gene mutations in patients from two Croatian
families with 11 beta-hydroxylase deficiency.";
Int. J. Endocrinol. 2014:185974-185979(2014).
[24]
VARIANTS AH4 LEU-42 AND SER-42, AND CHARACTERIZATION OF VARIANTS AH4
LEU-42 AND SER-42.
PubMed=26053152; DOI=10.1111/cen.12834;
Mooij C.F., Parajes S., Rose I.T., Taylor A.E., Bayraktaroglu T.,
Wass J.A., Connell J.M., Ray D.W., Arlt W., Krone N.;
"Characterization of the molecular genetic pathology in patients with
11beta-hydroxylase deficiency.";
Clin. Endocrinol. (Oxf.) 83:629-635(2015).
[25]
VARIANTS AH4 ARG-318; GLY-332 AND HIS-448, AND CHARACTERIZATION OF
VARIANT GLY-332.
PubMed=26476331; DOI=10.1016/j.jsbmb.2015.10.011;
Nguyen H.H., Eiden-Plach A., Hannemann F., Malunowicz E.M.,
Hartmann M.F., Wudy S.A., Bernhardt R.;
"Phenotypic, metabolic, and molecular genetic characterization of six
patients with congenital adrenal hyperplasia caused by novel mutations
in the CYP11B1 gene.";
J. Steroid Biochem. Mol. Biol. 155:126-134(2016).
-!- FUNCTION: Has steroid 11-beta-hydroxylase activity. In addition to
this activity, the 18 or 19-hydroxylation of steroids and the
aromatization of androstendione to estrone have also been ascribed
to cytochrome P450 XIB.
-!- CATALYTIC ACTIVITY: A steroid + 2 reduced adrenodoxin + O(2) + 2
H(+) = an 11-beta- hydroxysteroid + 2 oxidized adrenodoxin +
H(2)O.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:P19099};
-!- SUBCELLULAR LOCATION: Mitochondrion membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P15538-1; Sequence=Displayed;
Name=2;
IsoId=P15538-2; Sequence=VSP_043308;
Note=No experimental confirmation available.;
-!- DISEASE: Adrenal hyperplasia 4 (AH4) [MIM:202010]: A form of
congenital adrenal hyperplasia, a common recessive disease due to
defective synthesis of cortisol. Congenital adrenal hyperplasia is
characterized by androgen excess leading to ambiguous genitalia in
affected females, rapid somatic growth during childhood in both
sexes with premature closure of the epiphyses and short adult
stature. Four clinical types: 'salt wasting' (SW, the most severe
type), 'simple virilizing' (SV, less severely affected patients),
with normal aldosterone biosynthesis, 'non-classic form' or late-
onset (NC or LOAH) and 'cryptic' (asymptomatic).
{ECO:0000269|PubMed:16046588, ECO:0000269|PubMed:20089618,
ECO:0000269|PubMed:2022736, ECO:0000269|PubMed:20331679,
ECO:0000269|PubMed:20947076, ECO:0000269|PubMed:23940125,
ECO:0000269|PubMed:24022297, ECO:0000269|PubMed:24536089,
ECO:0000269|PubMed:24987415, ECO:0000269|PubMed:26053152,
ECO:0000269|PubMed:26476331, ECO:0000269|PubMed:9302260}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Hyperaldosteronism, familial, 1 (HALD1) [MIM:103900]: A
disorder characterized by hypertension, variable
hyperaldosteronism, and abnormal adrenal steroid production,
including 18-oxocortisol and 18-hydroxycortisol. There is
significant phenotypic heterogeneity, and some individuals never
develop hypertension. Note=The disease is caused by mutations
affecting the gene represented in this entry. The molecular defect
causing hyperaldosteronism familial 1 is an anti-Lepore-type
fusion of the CYP11B1 and CYP11B2 genes. The hybrid gene has the
promoting part of CYP11B1, ACTH-sensitive, and the coding part of
CYP11B2.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; M32879; AAA52149.1; -; Genomic_DNA.
EMBL; M32863; AAA52149.1; JOINED; Genomic_DNA.
EMBL; M32878; AAA52149.1; JOINED; Genomic_DNA.
EMBL; X55764; CAA39290.1; -; mRNA.
EMBL; D16153; BAB71992.1; -; Genomic_DNA.
EMBL; D16155; BAA03717.1; -; Genomic_DNA.
EMBL; EU332839; ABY87528.1; -; Genomic_DNA.
EMBL; AC083841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471162; EAW82293.1; -; Genomic_DNA.
EMBL; BC096286; AAH96286.1; -; mRNA.
EMBL; BC096287; AAH96287.1; -; mRNA.
EMBL; M24667; AAA52148.1; ALT_SEQ; mRNA.
EMBL; D10169; BAA01039.1; -; Genomic_DNA.
CCDS; CCDS34953.1; -. [P15538-2]
CCDS; CCDS6392.1; -. [P15538-1]
PIR; S11338; S11338.
RefSeq; NP_000488.3; NM_000497.3. [P15538-1]
RefSeq; NP_001021384.1; NM_001026213.1. [P15538-2]
UniGene; Hs.184927; -.
ProteinModelPortal; P15538; -.
SMR; P15538; -.
BioGrid; 107956; 1.
STRING; 9606.ENSP00000292427; -.
BindingDB; P15538; -.
ChEMBL; CHEMBL1908; -.
DrugBank; DB04630; Aldosterone.
DrugBank; DB00501; Cimetidine.
DrugBank; DB00257; Clotrimazole.
DrugBank; DB00292; Etomidate.
DrugBank; DB00196; Fluconazole.
DrugBank; DB00741; Hydrocortisone.
DrugBank; DB01026; Ketoconazole.
DrugBank; DB01233; Metoclopramide.
DrugBank; DB01011; Metyrapone.
DrugBank; DB01388; Mibefradil.
DrugBank; DB01110; Miconazole.
DrugBank; DB00648; Mitotane.
DrugBank; DB00252; Phenytoin.
DrugBank; DB00421; Spironolactone.
GuidetoPHARMACOLOGY; 1359; -.
SwissLipids; SLP:000001197; -.
iPTMnet; P15538; -.
PhosphoSitePlus; P15538; -.
BioMuta; CYP11B1; -.
DMDM; 215274267; -.
PaxDb; P15538; -.
PeptideAtlas; P15538; -.
PRIDE; P15538; -.
Ensembl; ENST00000292427; ENSP00000292427; ENSG00000160882. [P15538-1]
Ensembl; ENST00000517471; ENSP00000428043; ENSG00000160882. [P15538-2]
GeneID; 1584; -.
KEGG; hsa:1584; -.
UCSC; uc003yxi.4; human. [P15538-1]
CTD; 1584; -.
DisGeNET; 1584; -.
EuPathDB; HostDB:ENSG00000160882.11; -.
GeneCards; CYP11B1; -.
HGNC; HGNC:2591; CYP11B1.
HPA; HPA049171; -.
HPA; HPA056348; -.
HPA; HPA057752; -.
MalaCards; CYP11B1; -.
MIM; 103900; phenotype.
MIM; 202010; phenotype.
MIM; 610613; gene.
neXtProt; NX_P15538; -.
OpenTargets; ENSG00000160882; -.
Orphanet; 90795; Congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency.
Orphanet; 403; Familial hyperaldosteronism type I.
PharmGKB; PA133; -.
eggNOG; KOG0159; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00760000119243; -.
HOGENOM; HOG000013161; -.
HOVERGEN; HBG051098; -.
InParanoid; P15538; -.
KO; K00497; -.
PhylomeDB; P15538; -.
TreeFam; TF105094; -.
BioCyc; MetaCyc:HS08547-MONOMER; -.
BRENDA; 1.14.15.4; 2681.
Reactome; R-HSA-194002; Glucocorticoid biosynthesis.
Reactome; R-HSA-211976; Endogenous sterols.
ChiTaRS; CYP11B1; human.
GeneWiki; Steroid_11-beta-hydroxylase; -.
GenomeRNAi; 1584; -.
PRO; PR:P15538; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000160882; -.
CleanEx; HS_CYP11B1; -.
ExpressionAtlas; P15538; baseline and differential.
Genevisible; P15538; HS.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
GO; GO:0047783; F:corticosterone 18-monooxygenase activity; IBA:GO_Central.
GO; GO:0020037; F:heme binding; IC:BHF-UCL.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004507; F:steroid 11-beta-monooxygenase activity; IDA:BHF-UCL.
GO; GO:0032342; P:aldosterone biosynthetic process; IDA:BHF-UCL.
GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IDA:BHF-UCL.
GO; GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB.
GO; GO:0035865; P:cellular response to potassium ion; IEP:UniProtKB.
GO; GO:0034651; P:cortisol biosynthetic process; IDA:BHF-UCL.
GO; GO:0006704; P:glucocorticoid biosynthetic process; TAS:Reactome.
GO; GO:0042593; P:glucose homeostasis; TAS:BHF-UCL.
GO; GO:0006955; P:immune response; TAS:BHF-UCL.
GO; GO:0008217; P:regulation of blood pressure; IMP:BHF-UCL.
GO; GO:0016125; P:sterol metabolic process; TAS:Reactome.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002399; Cyt_P450_mitochondrial.
Pfam; PF00067; p450; 1.
PRINTS; PR00408; MITP450.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome;
Congenital adrenal hyperplasia; Direct protein sequencing;
Disease mutation; Heme; Iron; Lipid metabolism; Membrane;
Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase;
Polymorphism; Reference proteome; Steroid metabolism; Steroidogenesis;
Transit peptide.
TRANSIT 1 24 Mitochondrion.
CHAIN 25 503 Cytochrome P450 11B1, mitochondrial.
/FTId=PRO_0000003596.
METAL 450 450 Iron (heme axial ligand). {ECO:0000250}.
VAR_SEQ 401 466 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043308.
VARIANT 10 10 C -> Y (in dbSNP:rs6405).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014145.
VARIANT 42 42 P -> L (in AH4; classic; highly decreases
steroid 11-beta-hydroxylase activity;
dbSNP:rs193922538).
{ECO:0000269|PubMed:26053152}.
/FTId=VAR_074493.
VARIANT 42 42 P -> S (in AH4; non-classic; highly
decreases steroid 11-beta-hydroxylase
activity; dbSNP:rs104894069).
{ECO:0000269|PubMed:20089618,
ECO:0000269|PubMed:26053152,
ECO:0000269|PubMed:9302260}.
/FTId=VAR_001260.
VARIANT 43 43 R -> Q (in AH4; decreases steroid 11-
beta-hydroxylase activity; dbSNP:rs4534).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10391210,
ECO:0000269|PubMed:20089618,
ECO:0000269|PubMed:2401360}.
/FTId=VAR_014146.
VARIANT 63 63 D -> H (in dbSNP:rs5282).
/FTId=VAR_014638.
VARIANT 79 79 F -> I (in AH4; non-classic; highly
decreases steroid 11-beta-hydroxylase
activity). {ECO:0000269|PubMed:23940125}.
/FTId=VAR_074494.
VARIANT 83 83 L -> S (in AH4; highly decreases steroid
11-beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074495.
VARIANT 88 88 M -> I (in AH4; slightly decreases
steroid 11-beta-hydroxylase activity;
dbSNP:rs193922539).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074496.
VARIANT 94 94 P -> L (in AH4; almost abolishes steroid
11-beta-hydroxylase activity;
dbSNP:rs104894070).
{ECO:0000269|PubMed:16046588,
ECO:0000269|PubMed:20089618}.
/FTId=VAR_065666.
VARIANT 116 116 W -> C (in AH4; almost abolishes steroid
11-beta-hydroxylase activity;
dbSNP:rs772003869).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074497.
VARIANT 116 116 W -> G (in AH4; abolishes steroid 11-
beta-hydroxylase activity;
dbSNP:rs772733691).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074498.
VARIANT 125 125 H -> R (in AH4; slightly decreases
steroid 11-beta-hydroxylase activity;
dbSNP:rs757389720).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074499.
VARIANT 129 129 V -> M (in AH4; abolishes steroid 11-
beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074500.
VARIANT 133 133 N -> H (in AH4; non-classic; highly
decreases steroid 11-beta-hydroxylase
activity; dbSNP:rs104894067).
{ECO:0000269|PubMed:20089618,
ECO:0000269|PubMed:9302260}.
/FTId=VAR_001261.
VARIANT 135 135 P -> S (in AH4; highly decreases steroid
11-beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074501.
VARIANT 139 139 F -> L (in AH4; decreases steroid 11-
beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074502.
VARIANT 141 141 R -> Q (in AH4; unknown pathological
significance; dbSNP:rs267601810).
{ECO:0000269|PubMed:24987415}.
/FTId=VAR_075553.
VARIANT 143 143 R -> W (in AH4; non-classic; highly
decreases steroid 11-beta-hydroxylase
activity; dbSNP:rs140336749).
{ECO:0000269|PubMed:24022297}.
/FTId=VAR_074503.
VARIANT 150 150 S -> L (in AH4; non-classic; highly
decreases steroid 11-beta-hydroxylase
activity; dbSNP:rs142484434).
{ECO:0000269|PubMed:24536089}.
/FTId=VAR_074504.
VARIANT 158 158 L -> P (in AH4; highly decreases steroid
11-beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074505.
VARIANT 159 159 P -> L (in AH4; decreases steroid 11-
beta-hydroxylase activity;
dbSNP:rs370266763).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074506.
VARIANT 160 160 M -> I (in dbSNP:rs5287).
{ECO:0000269|PubMed:10391210}.
/FTId=VAR_014147.
VARIANT 161 161 Missing (in AH4).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074507.
VARIANT 165 165 A -> D (in AH4; almost abolishes steroid
11-beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074508.
VARIANT 173 173 K -> R (in dbSNP:rs4539).
/FTId=VAR_014639.
VARIANT 196 196 T -> A (in AH4; decreases steroid 11-
beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074509.
VARIANT 248 248 T -> I (in dbSNP:rs34620645).
/FTId=VAR_048462.
VARIANT 254 259 Missing (in AH4; abolishes steroid 11-
beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074510.
VARIANT 257 257 F -> L (in dbSNP:rs5288).
/FTId=VAR_014640.
VARIANT 267 267 G -> D (in AH4).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074511.
VARIANT 281 281 S -> N (in dbSNP:rs5291).
/FTId=VAR_014641.
VARIANT 293 293 L -> V (in dbSNP:rs5292).
{ECO:0000269|PubMed:10391210}.
/FTId=VAR_014148.
VARIANT 299 299 L -> P (in AH4; non-classic; almost
abolishes steroid 11-beta-hydroxylase
activity; dbSNP:rs387907573).
{ECO:0000269|PubMed:20089618,
ECO:0000269|PubMed:24022297}.
/FTId=VAR_074512.
VARIANT 306 306 A -> V (in AH4; non-classic; almost
abolishes steroid 11-beta-hydroxylase
activity; dbSNP:rs387907572).
{ECO:0000269|PubMed:20089618,
ECO:0000269|PubMed:24022297}.
/FTId=VAR_074513.
VARIANT 310 310 E -> K (in AH4; abolishes steroid 11-
beta-hydroxylase activity;
dbSNP:rs387907574).
{ECO:0000269|PubMed:24022297}.
/FTId=VAR_074514.
VARIANT 314 314 G -> R (in AH4; abolishes steroid 11-
beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074515.
VARIANT 318 318 T -> M (in AH4; abolishes steroid 11-
beta-hydroxylase activity;
dbSNP:rs104894061).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_001262.
VARIANT 318 318 T -> P (in AH4).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074516.
VARIANT 318 318 T -> R (in AH4).
{ECO:0000269|PubMed:16046588,
ECO:0000269|PubMed:20089618,
ECO:0000269|PubMed:24987415,
ECO:0000269|PubMed:26476331}.
/FTId=VAR_065667.
VARIANT 319 319 T -> M (in AH4; non-classic; decreases
steroid 11-beta-hydroxylase activity;
dbSNP:rs104894068).
{ECO:0000269|PubMed:20089618,
ECO:0000269|PubMed:9302260}.
/FTId=VAR_001263.
VARIANT 321 321 F -> V (in AH4).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074517.
VARIANT 331 331 A -> V (in AH4; abolishes steroid 11-
beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074518.
VARIANT 332 332 R -> G (in AH4; high reduction of steroid
11-beta-monooxygenase activity).
{ECO:0000269|PubMed:26476331}.
/FTId=VAR_075554.
VARIANT 332 332 R -> Q (in AH4; non-classic; highly
decreases steroid 11-beta-hydroxylase
activity; dbSNP:rs149881706).
{ECO:0000269|PubMed:24022297}.
/FTId=VAR_074519.
VARIANT 341 341 R -> S (in AH4; dbSNP:rs372115638).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074520.
VARIANT 348 348 A -> T (in dbSNP:rs6407).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014149.
VARIANT 366 366 R -> C (in AH4; decreases steroid 11-
beta-hydroxylase activity;
dbSNP:rs773245244).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074521.
VARIANT 368 368 A -> D (in AH4; abolishes steroid 11-
beta-hydroxylase activity;
dbSNP:rs104894071).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074522.
VARIANT 371 371 E -> G (in AH4; abolishes steroid 11-
beta-hydroxylase activity;
dbSNP:rs368944209).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074523.
VARIANT 374 374 R -> Q (in AH4; abolishes steroid 11-
beta-hydroxylase activity;
dbSNP:rs104894062).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_001264.
VARIANT 379 379 G -> V (in AH4).
{ECO:0000269|PubMed:20331679}.
/FTId=VAR_065196.
VARIANT 384 384 R -> G (in AH4).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074524.
VARIANT 384 384 R -> Q (in AH4; abolishes steroid 11-
beta-hydroxylase activity;
dbSNP:rs764598023).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074525.
VARIANT 386 386 A -> V (in dbSNP:rs4541).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:20089618,
ECO:0000269|PubMed:2401360,
ECO:0000269|PubMed:3499608}.
/FTId=VAR_014150.
VARIANT 401 401 T -> A (in AH4; decreases steroid 11-
beta-hydroxylase activity;
dbSNP:rs201300785).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074526.
VARIANT 404 404 R -> H (in dbSNP:rs4998896).
/FTId=VAR_048463.
VARIANT 427 427 R -> H (in AH4; dbSNP:rs754432887).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074527.
VARIANT 438 438 Missing (in AH4; abolishes steroid 11-
beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074528.
VARIANT 439 439 Y -> H (in dbSNP:rs5294).
/FTId=VAR_014642.
VARIANT 441 441 V -> G (in AH4; abolishes steroid 11-
beta-hydroxylase activity;
dbSNP:rs772169059).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074529.
VARIANT 444 444 G -> D (in AH4; dbSNP:rs779103938).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074530.
VARIANT 448 448 R -> C (in AH4; abolishes steroid 11-
beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074531.
VARIANT 448 448 R -> H (in AH4; abolishes steroid 11-
beta-hydroxylase activity;
dbSNP:rs28934586).
{ECO:0000269|PubMed:16046588,
ECO:0000269|PubMed:20089618,
ECO:0000269|PubMed:2022736,
ECO:0000269|PubMed:24987415,
ECO:0000269|PubMed:26476331}.
/FTId=VAR_001265.
VARIANT 453 453 R -> Q (in AH4; abolishes steroid 11-
beta-hydroxylase activity).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074532.
VARIANT 454 454 R -> C (in AH4).
{ECO:0000269|PubMed:20947076}.
/FTId=VAR_065197.
VARIANT 463 463 L -> LL (in AH4; classic; abolishes
steroid 11-beta-hydroxylase activity).
{ECO:0000269|PubMed:24536089}.
/FTId=VAR_074533.
VARIANT 489 489 L -> S (in AH4; dbSNP:rs750428278).
{ECO:0000269|PubMed:20089618}.
/FTId=VAR_074534.
VARIANT 494 494 F -> C. {ECO:0000269|PubMed:10599751,
ECO:0000269|PubMed:2592361}.
/FTId=VAR_008687.
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


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