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Reviewed, UniProtKB/Swiss-Prot P15539 (C11B2_MOUSE)

Last modified July 22, 2008. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
    Cytochrome P450 11B2, mitochondrial
    EC=1.14.15.4
    EC=1.14.15.5
Alternative name(s):
    CYPXIB2
    P450C11
    Steroid 11-beta-hydroxylase
    Aldosterone synthase
Gene names
Name: Cyp11b2
Synonyms: Cyp11b-2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Forms corticosterone from 11-deoxycorticosterone.

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.

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – 2424Mitochondrion
Chain25 – 500476Cytochrome P450 11B2, mitochondrial

Sites

Metal binding4471Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict3661K → R in AAB21517. Ref.1
Sequence conflict3831G → E in AAB21517. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15539-1 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: 9381313CED5AB7A3

FASTA50057,315
        10         20         30         40         50         60 
MALRVTADVW LARPWQCLHR TRALGTTATL APKTLQPFEA IPQYSRNKWL KMIQILREQG 

        70         80         90        100        110        120 
QENLHLEMHQ VFRELGPIFR HSVGKTQIVS VMLPEDAEKL HQVESMLPRR MHLEPWVAHR 

       130        140        150        160        170        180 
ELRGLRRGVF LLNGPEWRLN RLRLNRNVLS PKAVQKFVPM VDMVARDFLE TLKEKVLQNA 

       190        200        210        220        230        240 
RGSLTMDVQQ SLFNYTIEAS NFALFGERLG LLGHDLSPGS LKFIHALHSM FKSTSQLLFL 

       250        260        270        280        290        300 
PKSLTRWTST RVWKEHFDAW DVISEYANRC IWKVHQELRL GSSQTYSGIV AELISQGSLP 

       310        320        330        340        350        360 
LDAIKANSME LTAGSVDTTA IPLVMTLFEL ARNPDVQKAL RQESLAAEAS IAANPQKAMS 

       370        380        390        400        410        420 
DLPLLKAALK ETLRLYPVGG FLGRILSSDL VLQNYHVPAG TLVLLYLYSM GRNPAVFPRP 

       430        440        450        460        470        480 
ERYMPQRWLE RKRSFQHLAF GFGVRQCLGR RLAEVEMMLL LHHILKTFQV ETLRQEDVQM 

       490        500 
AYRFVLMPSS EPVLTFRPVS 

« Hide

References

[1]"Different isozymes of mouse 11 beta-hydroxylase produce mineralocorticoids and glucocorticoids."
Domalik L.J., Chaplin D.D., Kirkman M.S., Wu R.C., Liu W., Howard T.A., Seldin M.F., Parker K.L.
Mol. Endocrinol. 5:1853-1861(1991) [PubMed: 1686470] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural and functional analysis of the promoter region of the gene encoding mouse steroid 11 beta-hydroxylase."
Mouw A.R., Rice D.A., Meade J.C., Chua S.C., White P.C., Schimmer B.P., Parker K.L.
J. Biol. Chem. 264:1305-1309(1989) [PubMed: 2783417] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
+Additional computationally mapped references.

Cross-references

Sequence databases

S85260 Genomic DNA. Translation: AAB21517.2.
J04451 Genomic DNA. Translation: AAA50299.1.
PIRA41552.
UniGeneMm.377079

3D structure databases

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

Genome annotation databases

EnsemblENSMUSG00000022589. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:88584. Cyp11b2.

Phylogenomic databases

HOGENOMP15539.
HOVERGENP15539.

Gene expression databases

ArrayExpressP15539.
GermOnlineENSMUSG00000022589. Mus musculus.

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]
ProDomP15539.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

SOURCESearch...
ProtoNetSearch...

Entry information

Entry nameC11B2_MOUSE
AccessionPrimary (citable) accession number: P15539
Secondary accession number(s): Q64661
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1993
Last modified: July 22, 2008
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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