[1]	NUCLEOTIDE SEQUENCE, AND VARIANTS ARG-43 AND ALA-386. PubMed=2592361 [NCBI, ExPASy, EBI, Israel, Japan] 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], AND PARTIAL PROTEIN SEQUENCE. DOI=10.1016/0014-5793(90)81190-Y; PubMed=2401360 [NCBI, ExPASy, EBI, Israel, Japan] 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] OF 1-132. TISSUE=Peripheral blood; DOI=10.1210/jc.77.6.1677; PubMed=7903314 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[4]	PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 216-466. PubMed=3499608 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[5]	NUCLEOTIDE SEQUENCE OF 1-30. PubMed=1741400 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	VARIANT AH4 HIS-448. PubMed=2022736 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[7]	VARIANTS AH4 SER-42; HIS-133 AND MET-319. DOI=10.1093/hmg/6.11.1829; PubMed=9302260 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	VARIANT PHE-494. DOI=10.1210/jc.84.12.4749; PubMed=10599751 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[9]	VARIANTS TYR-10; ARG-43; THR-348 AND ALA-386. DOI=10.1038/10290; PubMed=10391209 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[10]	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).
[11]	VARIANTS ARG-43; ILE-160 AND VAL-293. DOI=10.1038/10297; PubMed=10391210 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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 + reduced adrenal ferredoxin + O₂ = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H₂O.
COFACTOR: Heme group (By similarity).
SUBCELLULAR LOCATION: Mitochondrion membrane.
DISEASE: Defects in CYP11B1 are the cause of adrenal hyperplasia type 4 (AH4) [MIM:202010]. AH4 is 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). AH4 patients usually have hypertension.
DISEASE: An anti-Lepore-type fusion of the CYP11B1 and CYP11B2 genes is a cause of glucocorticoid-remediable aldosteronism (GRA) [MIM:103900].
SIMILARITY: Belongs to the cytochrome P450 family.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=CYP11B1";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M32879; AAA52149.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32863; AAA52149.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32878; AAA52149.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X55764; CAA39290.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D16153; BAB71992.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D16155; BAA03717.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M24667; AAA52148.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10169; BAA01039.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S11338; S11338.

UniGene

Hs.184927

3D structure databases

HSSP

P00189; 1SCC. [HSSP ENTRY / PDB]

ModBase

P15538.

Enzyme and pathway databases

Reactome

REACT_602; Lipid and lipoprotein metabolism.

Organism-specific databases

HGNC:2591; CYP11B1.

103900; phenotype. [NCBI / EBI]
202010; phenotype. [NCBI / EBI]
610613; gene. [NCBI / EBI]

Orphanet

418; Adrenal hyperplasia, congenital.
85142; Conn's syndrome.
403; Hyperaldosteronism, familial, type 1.
404; Hyperaldosteronism, familial, type 2.
427; Hypoaldosteronism, familial.

PharmGKB

PA133; -.

GeneCards

P15538.

Gene expression databases

ArrayExpress

P15538; -.

CleanEx

HS_CYP11B1; -.

GermOnline

ENSG00000160882; Homo sapiens.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (traceable author statement from UniProtKB).
GO:0020037;	Molecular function: heme binding (inferred by curator from UniProtKB).
GO:0004507;	Molecular function: steroid 11-beta-monooxygenase activity (inferred from direct assay from UniProtKB).
GO:0005496;	Molecular function: steroid binding (inferred by curator from UniProtKB).
GO:0032342;	Biological process: aldosterone biosynthetic process (inferred from direct assay from UniProtKB).
GO:0006700;	Biological process: C21-steroid hormone biosynthetic process (inferred from direct assay from UniProtKB).
GO:0006704;	Biological process: glucocorticoid biosynthetic process (inferred from direct assay from UniProtKB).
GO:0042593;	Biological process: glucose homeostasis (traceable author statement from UniProtKB).
GO:0006955;	Biological process: immune response (traceable author statement from UniProtKB).
GO:0008217;	Biological process: regulation of blood pressure (inferred from mutant phenotype from UniProtKB).
GO:0006950;	Biological process: response to stress (traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002399; Cyt_P450_mit.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00408; MITP450.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

Genome annotation databases

Ensembl

ENSG00000160882; Homo sapiens. [Contig view]

Phylogenomic databases

HOVERGEN

P15538; -.

Other

DrugBank

DB00648; Mitotane.

SOURCE

CYP11B1; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Congenital adrenal hyperplasia; Direct protein sequencing; Disease mutation; Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase; Polymorphism; Steroid metabolism; Steroidogenesis; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 24`	`24`	`Mitochondrion.`
`CHAIN`	`25 503`	`479`	`Cytochrome P450 11B1, mitochondrial.`	`PRO_0000003596`
`METAL`	`450 450`		`Iron (heme axial ligand) (By similarity).`
`VARIANT`	`10 10`	`1`	`C -> Y (in dbSNP:rs6405 [NCBI]).`	`VAR_014145`
`VARIANT`	`42 42`	`1`	`P -> S (in AH4; non-classic).`	`VAR_001260`
`VARIANT`	`43 43`	`1`	`Q -> R (in dbSNP:rs4534 [NCBI]).`	`VAR_014146`
`VARIANT`	`63 63`	`1`	`D -> H (in dbSNP:rs5282 [NCBI]).`	`VAR_014638`
`VARIANT`	`133 133`	`1`	`N -> H (in AH4; non-classic).`	`VAR_001261`
`VARIANT`	`160 160`	`1`	`M -> I (in dbSNP:rs5287 [NCBI]).`	`VAR_014147`
`VARIANT`	`173 173`	`1`	`K -> R (in dbSNP:rs4539 [NCBI]).`	`VAR_014639`
`VARIANT`	`257 257`	`1`	`F -> L (in dbSNP:rs5288 [NCBI]).`	`VAR_014640`
`VARIANT`	`281 281`	`1`	`S -> N (in dbSNP:rs5291 [NCBI]).`	`VAR_014641`
`VARIANT`	`293 293`	`1`	`L -> V (in dbSNP:rs5292 [NCBI]).`	`VAR_014148`
`VARIANT`	`318 318`	`1`	`T -> M (in AH4).`	`VAR_001262`
`VARIANT`	`319 319`	`1`	`T -> M (in AH4; non-classic).`	`VAR_001263`
`VARIANT`	`348 348`	`1`	`A -> T (in dbSNP:rs6407 [NCBI]).`	`VAR_014149`
`VARIANT`	`374 374`	`1`	`R -> Q (in AH4).`	`VAR_001264`
`VARIANT`	`386 386`	`1`	`V -> A (in dbSNP:rs4541 [NCBI]).`	`VAR_014150`
`VARIANT`	`439 439`	`1`	`Y -> H (in dbSNP:rs5294 [NCBI]).`	`VAR_014642`
`VARIANT`	`448 448`	`1`	`R -> H (in AH4).`	`VAR_001265`
`VARIANT`	`494 494`	`1`	`C -> F.`	`VAR_008687`

Sequence information

Length: 503 AA [This is the length of the unprocessed precursor]

Molecular weight: 57529 Da [This is the MW of the unprocessed precursor]

CRC64: 36FF57802115BB9C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALRAKAEVC MAVPWLSLQR AQALGTRAAR VPRTVLPFEA MPQRPGNRWL RLLQIWREQG 

        70         80         90        100        110        120 
YEDLHLEVHQ TFQELGPIFR YDLGGAGMVC VMLPEDVEKL QQVDSLHPHR MSLEPWVAYR 

       130        140        150        160        170        180 
QHRGHKCGVF LLNGPEWRFN RLRLNPEVLS PNAVQRFLPM VDAVARDFSQ ALKKKVLQNA 

       190        200        210        220        230        240 
RGSLTLDVQP SIFHYTIEAS NLALFGERLG LVGHSPSSAS LNFLHALEVM FKSTVQLMFM 

       250        260        270        280        290        300 
PRSLSRWTSP KVWKEHFEAW DCIFQYGDNC IQKIYQELAF SRPQQYTSIV AELLLNAELS 

       310        320        330        340        350        360 
PDAIKANSME LTAGSVDTTV FPLLMTLFEL ARNPNVQQAL RQESLAAAAS ISEHPQKATT 

       370        380        390        400        410        420 
ELPLLRAALK ETLRLYPVGL FLERVVSSDL VLQNYHIPAG TLVRVFLYSL GRNPALFPRP 

       430        440        450        460        470        480 
ERYNPQRWLD IRGSGRNFYH VPFGFGMRQC LGRRLAEAEM LLLLHHVLKH LQVETLTQED 

       490        500 
IKMVYSFILR PSMCPLLTFR AIN

P15538 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools