[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Adrenal glomerulosa; DOI=10.1016/0960-0760(94)90003-5; PubMed=8031709 [NCBI, ExPASy, EBI, Israel, Japan] Lehoux J.-G., Mason J.I., Bernard H., Ducharme L., Lehoux J., Veronneau S., Lefebvre A.; "The presence of two cytochrome P450 aldosterone synthase mRNAs in the hamster adrenal."; J. Steroid Biochem. Mol. Biol. 49:131-137(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=9303441 [NCBI, ExPASy, EBI, Israel, Japan] Coulombe N., Lefebvre A., Lehoux J.-G.; "Characterization of the hamster CYP11B2 gene encoding adrenal cytochrome P450 aldosterone synthase."; DNA Cell Biol. 16:993-1002(1997).

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 (By similarity).
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 gland.
INDUCTION: By low sodium intake.
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

S73810; AAB31349.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U71280; AAB16805.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00189; 1SCC. [HSSP ENTRY / PDB]

ModBase

Q64658.

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:0004507;	Molecular function: steroid 11-beta-monooxygenase activity (inferred from electronic annotation from EC).
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.

BLOCKS

Q64658.

Phylogenomic databases

HOVERGEN

Q64658; -.

Other

ProtoNet

Q64658.

UniRef

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

Keywords

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 (By similarity).`
`CHAIN`	`25 500`	`476`	`Cytochrome P450 11B2, mitochondrial.`	`PRO_0000003599`
`METAL`	`447 447`		`Iron (heme axial ligand) (By similarity).`

Sequence information

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

Molecular weight: 57332 Da [This is the MW of the unprocessed precursor]

CRC64: 38251EDAD2085DE8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALRAKADVW LARPWQCLPR TRALGTTAAL APNTLRPFEA IPQYSRNRWL KMLQILREEG 

        70         80         90        100        110        120 
QEGLHLEMHE AFRELGPIFR YSMGRTQVVS VMLPEDAEKL HQVESMHPRR MHLEPWVAHR 

       130        140        150        160        170        180 
EHRGLSRGVF LLNGPEWRFN RLRLNPHVLS PKAVQKFVPM VDMVARDFLE SLKKKVFQNA 

       190        200        210        220        230        240 
RGSLTMDVQQ SLFNYSIEAS NFVLFGERLG LLGHDLSPAS LTFIHALHSV FKTTPQLMFL 

       250        260        270        280        290        300 
PRSLTRWTST RVWKEHFEAW DVISEYVNRC IRKVHQELRL GSPHTYSGIV AELMSQGALP 

       310        320        330        340        350        360 
LDAIRANSIE LTAGSVDTTT FPLVMALFEL ARNPDVQQAV RQESLAAEAS VAANPQRAMS 

       370        380        390        400        410        420 
DLPLLRAVLK ETLRLYPVGG FLERILSSDL VLQNYHVPAG TLVLLYLYSM GRNPAVFPRP 

       430        440        450        460        470        480 
EHYLPQRWLE RNGSFQHLTF GFGVRQCLGK RLAQVEMLLL LHHVLKSFRV ETQEREDVRM 

       490        500 
VYRFVLAPSS SPLLTFRPVS

Q64658 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