[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. 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]. TISSUE=Adrenal gland; DOI=10.1016/0014-5793(90)81398-8; PubMed=2129527 [NCBI, ExPASy, EBI, Israel, Japan] Imai M., Shimada H., Okada Y., Matsushima-Hibiya Y., Ogishima T., Ishimura Y.; "Molecular cloning of a cDNA encoding aldosterone synthase cytochrome P-450 in rat adrenal cortex."; FEBS Lett. 263:299-302(1990).
[4]	NUCLEOTIDE SEQUENCE. PubMed=8473352 [NCBI, ExPASy, EBI, Israel, Japan] Mukai K., Imai M., Shimada H., Ishimura Y.; "Isolation and characterization of rat CYP11B genes involved in late steps of mineralo- and glucocorticoid syntheses."; J. Biol. Chem. 268:9130-9137(1993).
[5]	NUCLEOTIDE SEQUENCE. 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).
[6]	PROTEIN SEQUENCE OF 25-44. STRAIN=Sprague-Dawley; TISSUE=Adrenal gland; 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.
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

D00568; BAA00445.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X52766; CAA36978.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D14097; BAA03172.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JX0252; JX0252.

NP_036670.1; -.

3D structure databases

HSSP

P00189; 1SCC. [HSSP ENTRY / PDB]

ModBase

P30100.

Organism-specific databases

RGD

727886; Cyp11b3.

Gene expression databases

ArrayExpress

P30100; -.

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]

GeneID

24294; -.

KEGG

rno:24294; -.

Phylogenomic databases

HOVERGEN

P30100; -.

Other

NextBio

602896; -.

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 24`	`24`	`Mitochondrion.`
`CHAIN`	`25 500`	`476`	`Cytochrome P450 11B3, mitochondrial.`	`PRO_0000003605`
`METAL`	`447 447`		`Iron (heme axial ligand) (By similarity).`
`CONFLICT`	`310 310`		`K -> E (in Ref. 3 and 4).`

Sequence information

Length: 500 AA [This is the length of the unprocessed precursor]

Molecular weight: 57122 Da [This is the MW of the unprocessed precursor]

CRC64: 040F6ECCA84CDEAD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALRVTADVW LARPWQCLHR TRALGTTATL APKTLKPFEA IPQYSRNKWL KMIQILREQG 

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

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

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

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

       310        320        330        340        350        360 
LDAIKANSMK LTAGSVDTTA IPLVMTLFEL ARNPDVQQAL RQETLAAEAS IAANPQKAMS 

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

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

       490        500 
AYRFVLMPSS SPVLTFRPIS

P30100 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