[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Adrenal gland; DOI=10.1016/0006-291X(90)91460-A; PubMed=2350348 [NCBI, ExPASy, EBI, Israel, Japan] Matsukawa N., Nonaka Y., Ying Z., Higaki J., Ogihara T., Okamoto M.; "Molecular cloning and expression of cDNAS encoding rat aldosterone synthase: variants of cytochrome P-450(11 beta)."; Biochem. Biophys. Res. Commun. 169:245-252(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0960-0760(92)90367-R; PubMed=1562515 [NCBI, ExPASy, EBI, Israel, Japan] Okamoto M., Nonaka Y.; "Molecular biology of rat steroid 11 beta-hydroxylase [P450(11 beta)] and aldosterone synthase [P450(11 beta, aldo)]."; J. Steroid Biochem. Mol. Biol. 41:415-419(1992).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Adrenal gland; DOI=10.1006/bbrc.1993.1792; PubMed=8333830 [NCBI, ExPASy, EBI, Israel, Japan] Zhou M., Gomez-Sanchez C.E.; "Cloning and expression of a rat cytochrome P-450 11 beta-hydroxylase/aldosterone synthase (CYP11B2) cDNA variant."; Biochem. Biophys. Res. Commun. 194:112-117(1993).
[4]	NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND VARIANT GLY-84. PubMed=8468320 [NCBI, ExPASy, EBI, Israel, Japan] Nomura M., Morohashi K., Kirita S., Nonaka Y., Okamoto M., Nawata H., Omura T.; "Three forms of rat CYP11B genes: 11 beta-hydroxylase gene, aldosterone synthase gene, and a novel gene."; J. Biochem. 113:144-152(1993).
[5]	PROTEIN SEQUENCE OF 35-54. TISSUE=Adrenal cortex; PubMed=2738055 [NCBI, ExPASy, EBI, Israel, Japan] Ogishima T., Mitani F., Ishimura Y.; "Isolation of aldosterone synthase cytochrome P-450 from zona glomerulosa mitochondria of rat adrenal cortex."; J. Biol. Chem. 264:10935-10938(1989).

Comments

FUNCTION: Converts 11-deoxycorticosterone into corticosterone, 18-hydroxycorticosterone, and aldosterone. Also can catalyze the conversion of 11-deoxycortisol to cortisol, 18-hydroxycortisol and cortisone.
CATALYTIC ACTIVITY: A steroid + reduced adrenal ferredoxin + O₂ = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H₂O.
CATALYTIC ACTIVITY: Corticosterone + reduced adrenal ferredoxin + O₂ = 18-hydroxycorticosterone + oxidized adrenal ferredoxin + H₂O.
COFACTOR: Heme group (By similarity).
SUBCELLULAR LOCATION: Mitochondrion membrane.
TISSUE SPECIFICITY: Adrenal cortex.
INDUCTION: A 12-fold increase was seen in the presence of a low sodium-high potassium diet.
SIMILARITY: Belongs to the cytochrome P450 family.

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

D00567; BAA00444.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U14908; AAB60457.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35342; A35342.
JN0615; JN0615.

UniGene

Rn.144549

3D structure databases

HSSP

P00189; 1SCC. [HSSP ENTRY / PDB]

ModBase

P30099.

Organism-specific databases

RGD

2454; Cyp11b2.

Gene expression databases

ArrayExpress

P30099; -.

GermOnline

ENSRNOG00000030111; Rattus norvegicus.

Ontologies

GO:0031966;	Cellular component: mitochondrial membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0047783;	Molecular function: corticosterone 18-monooxygenase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0004507;	Molecular function: steroid 11-beta-monooxygenase activity (inferred from electronic annotation from EC).
GO:0006700;	Biological process: C21-steroid hormone biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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

ENSRNOG00000030111; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P30099; -.

Other

UniRef

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

Keywords

Direct protein sequencing; Heme; Iron; Membrane; Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase; Steroidogenesis; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 34`	`34`	`Mitochondrion.`
`CHAIN`	`35 510`	`476`	`Cytochrome P450 11B2, mitochondrial.`	`PRO_0000003604`
`METAL`	`457 457`		`Iron (heme axial ligand) (By similarity).`
`VARIANT`	`84 84`	`1`	`E -> G.`
`VARIANT`	`146 146`	`1`	`E -> D.`
`VARIANT`	`261 261`	`1`	`Q -> R.`
`VARIANT`	`509 509`	`1`	`I -> V.`
`CONFLICT`	`1 13`		`MGACDNDFIELHS -> MNKAPAKAL (in Ref. 3).`

Sequence information

Length: 510 AA [This is the length of the unprocessed precursor]

Molecular weight: 58241 Da [This is the MW of the unprocessed precursor]

CRC64: 2E5129EE513DEA9E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGACDNDFIE LHSRVTADVW LARPWQCLHR TRALGTTATL APKTLKPFEA IPQYSRNKWL 

        70         80         90        100        110        120 
KMIQILREQG QENLHLEMHQ AFQELGPIFR HSAGGAQIVS VMLPEDAEKL HQVESILPRR 

       130        140        150        160        170        180 
MHLEPWVAHR ELRGLRRGVF LLNGAEWRFN RLKLNPNVLS PKAVQNFVPM VDEVARDFLE 

       190        200        210        220        230        240 
ALKKKVRQNA RGSLTMDVQQ SLFNYTIEAS NFALFGERLG LLGHDLNPGS LKFIHALHSM 

       250        260        270        280        290        300 
FKSTTQLLFL PRSLTRWTST QVWKEHFDAW DVISEYANRC IWKVHQELRL GSSQTYSGIV 

       310        320        330        340        350        360 
AALITQGALP LDAIKANSME LTAGSVDTTA IPLVMTLFEL ARNPDVQQAL RQETLAAEAS 

       370        380        390        400        410        420 
IAANPQKAMS DLPLLRAALK ETLRLYPVGG FLERILNSDL VLQNYHVPAG TLVLLYLYSM 

       430        440        450        460        470        480 
GRNPAVFPRP ERYMPQRWLE RKRSFQHLAF GFGVRQCLGR RLAEVEMLLL LHHMLKTFQV 

       490        500        510 
ETLRQEDVQM AYRFVLMPSS SPVLTFRPIS

P30099 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