NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Syrian;
TISSUE=Adrenal gland;
DOI=10.1016/0960-0760(95)00249-9; PubMed=8645611 [NCBI, ExPASy, EBI, Israel, Japan]
Veronneau S., Bernard H., Cloutier M., Courtemanche J., Ducharme L., Lefebvre A., Mason J.I., Lehoux J.-G.;
"The hamster adrenal cytochrome P450C11 has equipotent 11beta-hydroxylase and 19-hydroxylase activities, but no aldosterone synthase activity.";
J. Steroid Biochem. Mol. Biol. 57:125-139(1996).

Comments

FUNCTION: Forms corticosterone from 11-deoxycorticosterone. Possesses high and nearly equal 11-beta-hydroxylase and 19-hydroxylase activities and a lower 18-hydroxylase activity. Involved in the formation of the precursor of 19-nor-deoxycorticosterone, a very potent mineralocorticoid involved in the development of essential hypertension.
CATALYTIC ACTIVITY: A steroid + reduced adrenal ferredoxin + O₂ = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H₂O.
COFACTOR: Heme group (By similarity).
PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis .
SUBCELLULAR LOCATION: Mitochondrion membrane.
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

S82228; AAB47144.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00189; 1SCC. [HSSP ENTRY / PDB]

ModBase

P97720.

Ontologies

GO:0031966;	Cellular component: mitochondrial membrane (inferred from electronic annotation from UniProtKB-SubCell).
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.

ProtoNet

P97720.

Phylogenomic databases

HOVERGEN

P97720; -.

Other

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`	`25 499`	`475`	`Cytochrome P450 11B1, mitochondrial.`	`PRO_0000003598`
`METAL`	`446 446`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 499 AA [This is the length of the unprocessed precursor]

Molecular weight: 56821 Da [This is the MW of the unprocessed precursor]

CRC64: C798467266D741BD [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 YSMGRTQVVY VMLPEVAEKV FQADSTQPSR TLLEPWVAHR 

       130        140        150        160        170        180 
EHRGLSRGVF LLNGPEWRFN RLRINPHMLS PKAVQKFVPM VDMVARDFLE FLKKKVLANA 

       190        200        210        220        230        240 
HGSLSMNFYS SMFNYTIEAS HFVLFGERLG LLGDDLNSGS LKFVNALNSI MKTTPQLMLL 

       250        260        270        280        290        300 
PSGLTRWIST RVWKENFDSW DFVSEYVTKN VKNVYQEVQS GGPQSWSVIS QLVAEGALTM 

       310        320        330        340        350        360 
DAILANSLEL TAGSVDTTSV PLVMTLFELA RNPDVQQAVR QESLAAEASV AANPQRAMSD 

       370        380        390        400        410        420 
LPLLRAVLKE TLRLYPVAVF LERILSSDLV LQNYHVPAGT ILHMSLYSMG RNPAVFPRPE 

       430        440        450        460        470        480 
HYLPQRWLER NGSFQHLTFG FGVRQCLGKR LAQVEMLLLL HHVLKSFRVE TQEREDVRMV 

       490 
YRFVLAPSSS PLLTFRPVS

P97720 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