[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; DOI=10.1016/0014-5793(89)81053-1; PubMed=2551730 [NCBI, ExPASy, EBI, Israel, Japan] Nonaka Y., Matsukawa N., Morohashi K., Omura T., Ogihara T., Teraoka H., Okamoto M.; "Molecular cloning and sequence analysis of cDNA encoding rat adrenal cytochrome P-450(11)beta."; FEBS Lett. 255:21-26(1989).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Dahl salt-resistant; TISSUE=Adrenal gland; PubMed=8473350 [NCBI, ExPASy, EBI, Israel, Japan] Matsukawa N., Nonaka Y., Higaki J., Nagano M., Mikami H., Ogihara T., Okamoto M.; "Dahl's salt-resistant normotensive rat has mutations in cytochrome P450(11 beta), but the salt-sensitive hypertensive rat does not."; J. Biol. Chem. 268:9117-9121(1993).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Sprague-Dawley; TISSUE=Testis; 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).
[4]	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).
[5]	NUCLEOTIDE SEQUENCE. STRAIN=Dahl salt-resistant; DOI=10.1016/0960-0760(95)00025-U; PubMed=7626522 [NCBI, ExPASy, EBI, Israel, Japan] Okamoto M., Nonaka Y., Ohta M., Takemori H., Halder S.K., Zhi-Nong W., Sun T., Hatano O., Takakusa A., Murakami T.; "Cytochrome P450(11 beta): structure-function relationship of the enzyme and its involvement in blood pressure regulation."; J. Steroid Biochem. Mol. Biol. 53:89-94(1995).
[6]	PROTEIN SEQUENCE OF 25-44. TISSUE=Adrenal cortex; 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: Forms corticosterone from 11-deoxycorticosterone.
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.
TISSUE SPECIFICITY: Adrenal zona fasciculata/reticularis.
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

D11354; BAA01957.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D14091; BAA03171.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15431; CAA33472.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10107; BAA00988.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A46039; A46039.

NP_036669.2; -.

3D structure databases

HSSP

P00189; 1SCC. [HSSP ENTRY / PDB]

ModBase

P15393.

Organism-specific databases

RGD

2453; Cyp11b1.

Gene expression databases

ArrayExpress

P15393; -.

GermOnline

ENSRNOG00000032450; Rattus norvegicus.

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

P15393.

Genome annotation databases

Ensembl

ENSRNOG00000032450; Rattus norvegicus. [Contig view]

GeneID

500892; -.

KEGG

rno:500892; -.

Phylogenomic databases

HOVERGEN

P15393; -.

Other

NextBio

707547; -.

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`	`25 499`	`475`	`Cytochrome P450 11B1, mitochondrial.`	`PRO_0000003603`
`METAL`	`446 446`		`Iron (heme axial ligand) (By similarity).`
`VARIANT`	`127 127`	`1`	`R -> C (in strain: Dahl salt-resistant).`
`VARIANT`	`351 351`	`1`	`V -> A (in strain: Dahl salt-resistant).`
`VARIANT`	`381 381`	`1`	`V -> L (in strain: Dahl salt-resistant).`
`VARIANT`	`384 384`	`1`	`I -> L (in strain: Dahl salt-resistant).`
`VARIANT`	`443 443`	`1`	`V -> M (in strain: Dahl salt-resistant).`

Sequence information

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

Molecular weight: 57459 Da [This is the MW of the unprocessed precursor]

CRC64: 19C041F96A673C7E [This is a checksum on the sequence]

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

        70         80         90        100        110        120 
QENLHLEMHQ AFQELGPIFR HSAGGAQIVS VMLPEDAEKL HQVESILPHR MPLEPWVAHR 

       130        140        150        160        170        180 
ELRGLRRGVF LLNGADWRFN RLQLNPNMLS PKAIQSFVPF VDVVARDFVE NLKKRMLENV 

       190        200        210        220        230        240 
HGSMSINIQS NMFNYTMEAS HFVISGERLG LTGHDLKPES VTFTHALHSM FKSTTQLMFL 

       250        260        270        280        290        300 
PKSLTRWTST RVWKEHFDSW DIISEYVTKC IKNVYRELAE GRQQSWSVIS EMVAQSTLSM 

       310        320        330        340        350        360 
DAIHANSMEL IAGSVDTTAI SLVMTLFELA RNPDVQQALR QESLAAEASI VANPQKAMSD 

       370        380        390        400        410        420 
LPLLRAALKE TLRLYPVGSF VERIVHSDLV LQNYHVPAGT FVIIYLYSMG RNPAVFPRPE 

       430        440        450        460        470        480 
RYMPQRWLER KRSFQHLAFG FGVRQCLGRR LAEVEMLLLL HHMLKTFQVE TLRQEDMQMV 

       490 
FRFLLMPSSS PFLTFRPVS

P15393 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