Cytochrome P450 11B2, mitochondrial precursor

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P30099 (C11B2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 107. History...

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

Documents (1) |

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 P450-Aldo-1
Steroid 11-beta-hydroxylase
EC=1.14.15.4
EC=1.14.15.5

Gene names

Name:	Cyp11b2
Synonyms:	Cyp11b-2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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 + 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.
Tissue specificity	Adrenal cortex.
Induction	A 12-fold increase was seen in the presence of a low sodium-high potassium diet. Ref.4
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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aldosterone biosynthetic process Inferred from direct assay PubMed 11832364. Source: RGD cellular response to mechanical stimulus Inferred from expression pattern PubMed 19478813. Source: RGD cellular response to nutrient Inferred from expression pattern PubMed 16876110. Source: RGD cellular response to peptide hormone stimulus Inferred from expression pattern PubMed 20685870. Source: RGD cellular response to potassium ion starvation Inferred from expression pattern PubMed 20685870. Source: RGD glucocorticoid biosynthetic process Inferred from direct assay PubMed 11832364. Source: RGD positive regulation of blood pressure Inferred from mutant phenotype PubMed 18495825. Source: RGD response to drug Inferred from expression pattern PubMed 16043663 PubMed 18154949. Source: RGD response to insulin stimulus Inferred from expression pattern PubMed 16043663. Source: RGD response to salt stress Inferred from expression pattern PubMed 19118098. Source: RGD
Cellular_component	dendrite Inferred from direct assay PubMed 12459034. Source: RGD mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	corticosterone 18-monooxygenase activity Inferred from direct assay PubMed 11832364 Ref.1. Source: RGD 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.3. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 34

Mitochondrion Ref.5

Chain

35 – 510

476

Cytochrome P450 11B2, mitochondrial

PRO_0000003604

Sites

Metal binding

457

Iron (heme axial ligand) By similarity

Natural variations

Natural variant

E → G. Ref.4

Natural variant

146

E → D.

Natural variant

261

Q → R.

Natural variant

509

I → V.

Experimental info

Sequence conflict

1 – 13

MGACD…IELHS → MNKAPAKAL in AAB60457. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P30099 [UniParc].

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

FASTA

510

58,241

        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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-54. Tissue: Adrenal cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D00567 mRNA. Translation: BAA00444.1. U14908 mRNA. Translation: AAB60457.1.
IPI	IPI00205063.
PIR	A35342. JN0615.
UniGene	Rn.144549.
3D structure databases
ProteinModelPortal	P30099.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000049722.
Proteomic databases
PaxDb	P30099.
PRIDE	P30099.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	RGD:2454. rat.
Organism-specific databases
RGD	2454. Cyp11b2.
Phylogenomic databases
eggNOG	COG2124.
HOGENOM	HOG000013161.
HOVERGEN	HBG051098.
InParanoid	P30099.
OrthoDB	EOG4B2SWV.
Gene expression databases
ArrayExpress	P30099.
Genevestigator	P30099.
GermOnline	ENSRNOG00000030111. Rattus norvegicus.
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
ChEMBL	CHEMBL3237.

Entry information

Entry name

C11B2_RAT

Accession

Primary (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:	April 3, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

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

Natural variations

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