[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Merino; TISSUE=Adrenal cortex; DOI=10.1016/0167-4781(94)00190-E; PubMed=7999785 [NCBI, ExPASy, EBI, Israel, Japan] Boon W.C., Roche P.J., Hammond V.E., Jeyaseelan K., Crawford R.J., Coghlan J.P.; "Cloning and expression analysis of a cytochrome P-450(11 beta) cDNA in sheep."; Biochim. Biophys. Acta 1260:109-112(1995).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. TISSUE=Adrenal gland, and Liver; PubMed=10728821 [NCBI, ExPASy, EBI, Israel, Japan] Anwar A., Coghlan J.P., Jeyaseelan K.; "Structure of an ovine CYP11B1 gene."; DNA Seq. 8:357-374(1998).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77. PubMed=7804143 [NCBI, ExPASy, EBI, Israel, Japan] Anwar A., Jeyaseelan K., Coghlan J.P.; "Molecular cloning and characterization of the ovine CYP11B1 promoter."; Biochem. Mol. Biol. Int. 33:1169-1178(1994).

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.
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

L34337; AAA62308.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L47569; AAA81576.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U78478; AAB64249.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U78477; AAB64248.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L28716; AAA83384.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S52085; S52085.

NP_001068568.1; -.

3D structure databases

HSSP

P00189; 1SCC. [HSSP ENTRY / PDB]

ModBase

P51663.

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.
IPR002401; Cyt_P450_E_grp-I.
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

PR00463; EP450I.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

Genome annotation databases

GeneID

767576; -.

Phylogenomic databases

HOVERGEN

P51663; -.

Other

ProtoNet

P51663.

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.`
`CHAIN`	`25 503`	`479`	`Cytochrome P450 11B1, mitochondrial.`	`PRO_0000003606`
`METAL`	`450 450`		`Iron (heme axial ligand) (By similarity).`
`CONFLICT`	`99 99`		`R -> S (in Ref. 2; AAB64248/AAB64249).`
`CONFLICT`	`189 189`		`A -> G (in Ref. 1; AAA62308).`
`CONFLICT`	`439 439`		`P -> R (in Ref. 1; AAA62308).`
`CONFLICT`	`500 500`		`R -> G (in Ref. 2; AAB64248/AAB64249).`

Sequence information

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

Molecular weight: 57784 Da [This is the MW of the unprocessed precursor]

CRC64: 968F2DF6EE7D595B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALWAKARVW MAGPWLSLHR ARPLGTRASA APKAVLPFEA MPRCPGNKWM RVLQIWKEQG 

        70         80         90        100        110        120 
SENMHLDMHQ TFQELGPIFR YDVGGRHMVF VMLPEDVERL QQAESLHPQR MLLEPWLAYR 

       130        140        150        160        170        180 
QARGHKCGVF LLNGPQWRLD RLRLNPDVLS LPALQKYTPL VDGVARDFSQ TLKARVLQNA 

       190        200        210        220        230        240 
RGSLTLDIAP SVFRYTIEAS TLVLYGERLG LLTQQPNPDS LNFIHALEAM FKSTVQLMFV 

       250        260        270        280        290        300 
PRRLSRWTSS SMWREHFEAW DYIFQYANRA IQRIYQELAL GHPWHYSGIV AELLMRADMT 

       310        320        330        340        350        360 
LDTIKANTID LTAGSVDTTA FPLLMTLFEL ARNPEVQQAL RQESLVAEAR ISENPQRATT 

       370        380        390        400        410        420 
ELPLLRAALK ETLRLYPVGI TLERQVSSDL VLQNYHIPAG TLVKVLLYSL GRNPAVFARP 

       430        440        450        460        470        480 
ESYHPQRWLD RQGSGSRFPH LAFGFGMRQC LGRRVAEVEM LLLLHHVLKN FLVETLAQED 

       490        500 
IKMVYRFILM PSTLPLFTFR AIQ

P51663 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