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P15539 (C11B2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

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 adrenodoxin + O2 = an 11-beta-hydroxysteroid + oxidized adrenodoxin + H2O.

Corticosterone + reduced adrenodoxin + O2 = 18-hydroxycorticosterone + oxidized adrenodoxin + H2O.

Cofactor

Heme group By similarity.

Subcellular location

Mitochondrion membrane.

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion
Chain25 – 500476Cytochrome P450 11B2, mitochondrial
PRO_0000003600

Sites

Metal binding4471Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict4911S → E in AAB21517. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15539 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: DCAFFF3EF2663195

FASTA50057,373
        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 
DLPLLRAALK ETLRLYPVGG FLERILSSDL VLQNYHVPAG TLVLLYLYSM GRNPAVFPRP 

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

       490        500 
AYRFVLMPSS SPVLTFRPVS 

« Hide

References

« Hide 'large scale' 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S85260 Genomic DNA. Translation: AAB21517.2.
BC116908 mRNA. Translation: AAI16909.1.
BC119321 mRNA. Translation: AAI19322.1.
J04451 Genomic DNA. Translation: AAA50299.1.
PIRA41552.
RefSeqNP_034121.3. NM_009991.3.
UniGeneMm.377079.

3D structure databases

ProteinModelPortalP15539.
SMRP15539. Positions 34-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000023253.

Proteomic databases

PRIDEP15539.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13072.
KEGGmmu:13072.

Organism-specific databases

CTD1585.
MGIMGI:88584. Cyp11b2.

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000013161.
HOVERGENHBG051098.
InParanoidQ14AB5.
KOK00497.
PhylomeDBP15539.

Gene expression databases

BgeeP15539.
GenevestigatorP15539.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002399. Cyt_P450_mitochondrial.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00408. MITP450.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio283008.
PROP15539.
SOURCESearch...

Entry information

Entry nameC11B2_MOUSE
AccessionPrimary (citable) accession number: P15539
Secondary accession number(s): Q14AB5, Q64661
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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