[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME-2), AND PARTIAL PROTEIN SEQUENCE. PubMed=3429448 [NCBI, ExPASy, EBI, Israel, Japan] Morohashi K., Yoshioka H., Gotoh O., Okada Y., Yamamoto K., Miyata T., Sogawa K., Fujii-Kuriyama Y., Omura T.; "Molecular cloning and nucleotide sequence of DNA of mitochondrial cytochrome P-450(11 beta) of bovine adrenal cortex."; J. Biochem. 102:559-568(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME-3). TISSUE=Adrenal cortex; PubMed=3266212 [NCBI, ExPASy, EBI, Israel, Japan] Kirita S., Morohashi K., Hashimoto T., Yoshioka H., Fujii-Kuriyama Y., Omura T.; "Expression of two kinds of cytochrome P-450(11 beta) mRNA in bovine adrenal cortex."; J. Biochem. 104:683-686(1988).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3499608 [NCBI, ExPASy, EBI, Israel, Japan] Chua S.C., Szabo P., Vitek A., Grzeschik K.H., John M., White P.C.; "Cloning of cDNA encoding steroid 11 beta-hydroxylase (P450c11)."; Proc. Natl. Acad. Sci. U.S.A. 84:7193-7197(1987).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2753866 [NCBI, ExPASy, EBI, Israel, Japan] Hashimoto T., Morohashi K., Omura T.; "Cloning and characterization of bovine cytochrome P-450(11 beta) genes."; J. Biochem. 105:676-679(1989).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1965187 [NCBI, ExPASy, EBI, Israel, Japan] Kirita S., Hashimoto T., Kitajima M., Honda S., Morohashi K., Omura T.; "Structural analysis of multiple bovine P-450(11 beta) genes and their promoter activities."; J. Biochem. 108:1030-1041(1990).

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.
MISCELLANEOUS: The sequence shown is that of isozyme 11-beta-2.
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

D00185; BAA00127.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D00361; BAA00268.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17843; AAA83383.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D00455; BAA00347.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A28415; A28415.
JX0071; JX0071.
JX0151; JX0151.

RefSeq

NP_777063.2; -.

UniGene

Bt.4297

3D structure databases

HSSP

P00189; 1SCC. [HSSP ENTRY / PDB]

ModBase

P15150.

Ontologies

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

BLOCKS

P15150.

Genome annotation databases

Ensembl

ENSBTAG00000026342; Bos taurus. [Contig view]

GeneID

282422; -.

KEGG

bta:282422; -.

Phylogenomic databases

HOVERGEN

P15150; -.

Other

ProtoNet

P15150.

UniRef

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

Keywords

Direct protein sequencing; Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase; Steroid metabolism; 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_0000003594`
`METAL`	`450 450`		`Iron (heme axial ligand).`
`VARIANT`	`30 30`	`1`	`A -> V (in 11-beta-3).`
`VARIANT`	`60 60`	`1`	`S -> G (in 11-beta-3).`
`VARIANT`	`106 106`	`1`	`H -> R (in 11-beta-3).`
`CONFLICT`	`191 192`		`SV -> RL (in Ref. 3; AAA83383).`
`CONFLICT`	`337 337`		`Q -> T (in Ref. 4 and 5).`
`CONFLICT`	`347 347`		`A -> P (in Ref. 3; AAA83383).`
`CONFLICT`	`502 502`		`I -> Y (in Ref. 4; BAA00347).`

Sequence information

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

Molecular weight: 57847 Da [This is the MW of the unprocessed precursor]

CRC64: 9FBEEC132975FD72 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALWAKARVR MAGPWLSLHE ARLLGTRGAA APKAVLPFEA MPRCPGNKWM RMLQIWKEQS 

        70         80         90        100        110        120 
SENMHLDMHQ TFQELGPIFR YDVGGRHMVF VMLPEDVERL QQADSHHPQR MILEPWLAYR 

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

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

       250        260        270        280        290        300 
PRRLSRWMST NMWREHFEAW DYIFQYANRA IQRIYQELAL GHPWHYSGIV AELLMRADMT 

       310        320        330        340        350        360 
LDTIKANTID LTAGSVDTTA FPLLMTLFEL ARNPEVQQAV RQESLVAEAR ISENPQRAIT 

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

       430        440        450        460        470        480 
ESYHPQRWLD RQGSGSRFPH LAFGFGVRQC LGRRVAEVEM LLLLHHVLKN FLVETLEQED 

       490        500 
IKMVYRFILM PSTLPLFTFR AIQ

P15150 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