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Reviewed, UniProtKB/Swiss-Prot P30099 (C11B2_RAT)

Last modified September 2, 2008. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cytochrome P450 11B2, mitochondrial
    EC=1.14.15.4
    EC=1.14.15.5
Alternative name(s):
    CYPXIB2
    P450-Aldo-1
    Aldosterone synthase
Gene names
Name: Cyp11b2
Synonyms: Cyp11b-2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (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.

Catalytic activity

A steroid + reduced adrenal ferredoxin + O(2) = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H(2)O.

Corticosterone + reduced adrenal ferredoxin + O(2) = 18-hydroxycorticosterone + oxidized adrenal ferredoxin + H(2)O.

Cofactor

Heme group By similarity.

Subcellular location

Mitochondrion membrane.

Tissue specificity

Adrenal cortex.

Induction

A 12-fold increase was seen in the presence of a low sodium-high potassium diet.

Sequence similarities

Belongs to the cytochrome P450 family.

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Ontologies

Keywords

   Biological processSteroidogenesis
   Cellular componentMembrane
Mitochondrion
   DomainTransit peptide
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Cellular componentmitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – 3434Mitochondrion
Chain35 – 510476Cytochrome P450 11B2, mitochondrial

Sites

Metal binding4571Iron (heme axial ligand) By similarity

Natural variations

Natural variant841E → G
Natural variant1461E → D
Natural variant2611Q → R
Natural variant5091I → V

Experimental info

Sequence conflict1 – 1313MGACD…IELHS → MNKAPAKAL Ref.3

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Sequences

Sequence LengthMass (Da)Tools
P30099-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 2E5129EE513DEA9E

FASTA51058,241
        10         20         30         40         50         60 
MGACDNDFIE LHSRVTADVW LARPWQCLHR TRALGTTATL APKTLKPFEA IPQYSRNKWL 

        70         80         90        100        110        120 
KMIQILREQG QENLHLEMHQ AFQELGPIFR HSAGGAQIVS VMLPEDAEKL HQVESILPRR 

       130        140        150        160        170        180 
MHLEPWVAHR ELRGLRRGVF LLNGAEWRFN RLKLNPNVLS PKAVQNFVPM VDEVARDFLE 

       190        200        210        220        230        240 
ALKKKVRQNA RGSLTMDVQQ SLFNYTIEAS NFALFGERLG LLGHDLNPGS LKFIHALHSM 

       250        260        270        280        290        300 
FKSTTQLLFL PRSLTRWTST QVWKEHFDAW DVISEYANRC IWKVHQELRL GSSQTYSGIV 

       310        320        330        340        350        360 
AALITQGALP LDAIKANSME LTAGSVDTTA IPLVMTLFEL ARNPDVQQAL RQETLAAEAS 

       370        380        390        400        410        420 
IAANPQKAMS DLPLLRAALK ETLRLYPVGG FLERILNSDL VLQNYHVPAG TLVLLYLYSM 

       430        440        450        460        470        480 
GRNPAVFPRP ERYMPQRWLE RKRSFQHLAF GFGVRQCLGR RLAEVEMLLL LHHMLKTFQV 

       490        500        510 
ETLRQEDVQM AYRFVLMPSS SPVLTFRPIS

« Hide

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References

[1]"Molecular cloning and expression of cDNAS encoding rat aldosterone synthase: variants of cytochrome P-450(11 beta)."
Matsukawa N., Nonaka Y., Ying Z., Higaki J., Ogihara T., Okamoto M.
Biochem. Biophys. Res. Commun. 169:245-252(1990) [PubMed: 2350348] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal gland.
[2]"Molecular biology of rat steroid 11 beta-hydroxylase [P450(11 beta)] and aldosterone synthase [P450(11 beta, aldo)]."
Okamoto M., Nonaka Y.
J. Steroid Biochem. Mol. Biol. 41:415-419(1992) [PubMed: 1562515] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning and expression of a rat cytochrome P-450 11 beta-hydroxylase/aldosterone synthase (CYP11B2) cDNA variant."
Zhou M., Gomez-Sanchez C.E.
Biochem. Biophys. Res. Commun. 194:112-117(1993) [PubMed: 8333830] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Adrenal gland.
[4]"Three forms of rat CYP11B genes: 11 beta-hydroxylase gene, aldosterone synthase gene, and a novel gene."
Nomura M., Morohashi K., Kirita S., Nonaka Y., Okamoto M., Nawata H., Omura T.
J. Biochem. 113:144-152(1993) [PubMed: 8468320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, VARIANT GLY-84.
[5]"Isolation of aldosterone synthase cytochrome P-450 from zona glomerulosa mitochondria of rat adrenal cortex."
Ogishima T., Mitani F., Ishimura Y.
J. Biol. Chem. 264:10935-10938(1989) [PubMed: 2738055] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-54.
Tissue: Adrenal cortex.

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Cross-references

Sequence databases

D00567 mRNA. Translation: BAA00444.1.
U14908 mRNA. Translation: AAB60457.1.
PIRA35342.
JN0615.
UniGeneRn.144549

3D structure databases

HSSPHSSP built from PDB template 1SCC based on UniProtKB P00189.
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000030111. Rattus norvegicus. [Contig view]

Organism-specific databases

RGD2454. Cyp11b2.

Phylogenomic databases

HOVERGENP30099.

Gene expression databases

ArrayExpressP30099.
GermOnlineENSRNOG00000030111. Rattus norvegicus.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR002399. Cyt_P450_mit.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00408. MITP450.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProDomP30099.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameC11B2_RAT
AccessionPrimary (citable) accession number: P30099
Secondary accession number(s): Q64540
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: September 2, 2008
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents