Cytochrome P450 11B2, mitochondrial precursor

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P15539 (C11B2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 118. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Forms corticosterone from 11-deoxycorticosterone.
Catalytic activity	A steroid + reduced adrenal ferredoxin + O₂ = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H₂O. Corticosterone + reduced adrenal ferredoxin + O₂ = 18-hydroxycorticosterone + oxidized adrenal ferredoxin + H₂O.
Cofactor	Heme group By similarity.
Subcellular location	Mitochondrion membrane.
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Biological process	Steroidogenesis
Cellular component	Membrane Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aldosterone biosynthetic process Inferred from direct assay Ref.1 PubMed 8645611. Source: MGI drinking behavior Inferred from mutant phenotype PubMed 16118390. Source: MGI ion homeostasis Inferred from mutant phenotype PubMed 16118390. Source: MGI regulation of blood volume by renal aldosterone Inferred from mutant phenotype PubMed 16118390. Source: MGI regulation of systemic arterial blood pressure by circulatory renin-angiotensin Inferred from mutant phenotype PubMed 16118390. Source: MGI
Cellular_component	mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 14651853 PubMed 18614015. Source: MGI
Molecular_function	corticosterone 18-monooxygenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro steroid 11-beta-monooxygenase activity Inferred from direct assay Ref.1 PubMed 8645611. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 24

Mitochondrion

Chain

25 – 500

476

Cytochrome P450 11B2, mitochondrial

PRO_0000003600

Sites

Metal binding

447

Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict

491

S → E in AAB21517. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P15539 [UniParc].

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

FASTA

500

57,373

        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' referencesShow '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.
IPI	IPI00323713.
PIR	A41552.
RefSeq	NP_034121.3. NM_009991.3.
UniGene	Mm.377079.
3D structure databases
ProteinModelPortal	P15539.
SMR	P15539. Positions 36-498.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000023253.
Proteomic databases
PRIDE	P15539.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	13072.
KEGG	mmu:13072.
Organism-specific databases
CTD	1585.
MGI	MGI:88584. Cyp11b2.
Phylogenomic databases
eggNOG	COG2124.
HOGENOM	HOG000013161.
HOVERGEN	HBG051098.
InParanoid	Q14AB5.
KO	K00497.
OrthoDB	EOG4B2SWV.
Gene expression databases
ArrayExpress	P15539.
Bgee	P15539.
Genevestigator	P15539.
GermOnline	ENSMUSG00000022589. Mus musculus.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002399. Cyt_P450_mitochondrial. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00408. MITP450. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	283008.
SOURCE	Search...

Entry information

Entry name

C11B2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents