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Q92104 (CP11B_LITCT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 11B, mitochondrial
Alternative name(s):
CYPXIB
Cytochrome P450C11
P-450(11 beta,aldo)
Steroid 11-beta-hydroxylase
EC=1.14.15.4
Gene names
Name:CYP11B
OrganismLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifier8400 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Has 11 beta-hydroxylation, 18-hydroxylation activities and aldosterone synthetic activity. Catalyzes the final steps of glucocorticoid and mineralocorticoid biosynthesis.

Catalytic activity

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

Cofactor

Heme group By similarity.

Subcellular location

Mitochondrion membrane.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Biological processSteroidogenesis
   Cellular componentMembrane
Mitochondrion
   DomainTransit peptide
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
Gene Ontology (GO)
   Biological_processsteroid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionheme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

steroid 11-beta-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4545Mitochondrion Potential
Chain46 – 517472Cytochrome P450 11B, mitochondrial
PRO_0000003607

Sites

Metal binding4651Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92104 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8F94DCD66BA6370B

FASTA51759,539
        10         20         30         40         50         60 
MLEKTAARQI GSCLMRCRTL DTTSPLWTGF SRLSTAPLIH EAREDGSLAS QTLPYEAIPT 

        70         80         90        100        110        120 
TGRSAWFNLF QFWRKNSFQH MHLAMEENFQ NLGPIYREKL GTHNSVNIML PQDVARLFQS 

       130        140        150        160        170        180 
EGIFPRRMTM EAWSKHRELR NHKQGVFLLN GEAWRSDRII LNKEVLSLAG VKKFLPFLDE 

       190        200        210        220        230        240 
AAADFVTFMK KRMSKNTRGS LTVDLYADLF RFTLEASSYV LYGQRLGLLE EHPNADTLRF 

       250        260        270        280        290        300 
ISAVETVLKT TLPLLYYPHQ ILQLFQTRLW NEHMHAWDVI FEQADRCIQN IYQEYCLGQE 

       310        320        330        340        350        360 
RGYSGIMAEL LLQAELPLDS IKANITELMA GGVDTTAMPL LFTLFELARN PSVQRELREE 

       370        380        390        400        410        420 
IRKAEAQNPN DLNQLLNSLP LLKGAIKETL RLYPVGITVQ RHLIKDIVLH NYHIPAGTLV 

       430        440        450        460        470        480 
QVGLYPMGRS PLLFQDALRY DPARWLKRED TNFKALAFGF GSRQCIGRRI AETEITLFLM 

       490        500        510 
HMLKNFQIDT VSKDDIKTVF GFILMPEKPP LLTFRPI 

« Hide

References

[1]"Frog cytochrome P-450 (11 beta,aldo), a single enzyme involved in the final steps of glucocorticoid and mineralocorticoid biosynthesis."
Nonaka Y., Takemori H., Halder S.K., Sun T., Ohta M., Hatano O., Takakusu A., Okamoto M.
Eur. J. Biochem. 229:249-256(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10984 mRNA. Translation: BAA01756.1.
PIRS69347.

3D structure databases

ProteinModelPortalQ92104.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG051098.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCP11B_LITCT
AccessionPrimary (citable) accession number: Q92104
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: December 11, 2013
This is version 77 of the entry and version 1 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