P15150 (C11B1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 108.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cytochrome P450 11B1, mitochondrial | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 503 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 | Has steroid 11-beta-hydroxylase activity. In addition to this activity, the 18 or 19-hydroxylation of steroids and the aromatization of androstendione to estrone have also been ascribed to cytochrome P450 XIB. |
| Catalytic activity | A steroid + reduced adrenal ferredoxin + O2 = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H2O. |
| Cofactor | Heme group By similarity. |
| Subcellular location | |
| Miscellaneous | The sequence shown is that of isozyme 11-beta-2. |
| Sequence similarities | Belongs to the cytochrome P450 family. |
| Sequence caution | The sequence BAA00127.1 differs from that shown. Reason: Frameshift at positions 186 and 192. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid metabolism Steroid metabolism 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 | steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | electron carrier activity Inferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: InterPro steroid 11-beta-monooxygenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 24 | 24 | Mitochondrion | ||||||
| Chain | 25 – 503 | 479 | Cytochrome P450 11B1, mitochondrial | PRO_0000003594 | |||||
Sites | |||||||||
| Metal binding | 450 | 1 | Iron (heme axial ligand) | ||||||
Natural variations | |||||||||
| Natural variant | 30 | 1 | A → V in 11-beta-3. | ||||||
| Natural variant | 60 | 1 | S → G in 11-beta-3. | ||||||
| Natural variant | 106 | 1 | H → R in 11-beta-3. | ||||||
Experimental info | |||||||||
| Sequence conflict | 191 – 192 | 2 | SV → RL in AAA83383. Ref.3 | ||||||
| Sequence conflict | 337 | 1 | Q → T in BAA00347. Ref.4 | ||||||
| Sequence conflict | 337 | 1 | Q → T no nucleotide entry Ref.5 | ||||||
| Sequence conflict | 347 | 1 | A → P in AAA83383. Ref.3 | ||||||
| Sequence conflict | 502 | 1 | I → Y in BAA00347. Ref.4 | ||||||
Sequences
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References
| [1] | "Molecular cloning and nucleotide sequence of DNA of mitochondrial cytochrome P-450(11 beta) of bovine adrenal cortex." Morohashi K., Yoshioka H., Gotoh O., Okada Y., Yamamoto K., Miyata T., Sogawa K., Fujii-Kuriyama Y., Omura T. J. Biochem. 102:559-568(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME-2), PARTIAL PROTEIN SEQUENCE. |
| [2] | "Expression of two kinds of cytochrome P-450(11 beta) mRNA in bovine adrenal cortex." Kirita S., Morohashi K., Hashimoto T., Yoshioka H., Fujii-Kuriyama Y., Omura T. J. Biochem. 104:683-686(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME-3). Tissue: Adrenal cortex. |
| [3] | "Cloning of cDNA encoding steroid 11 beta-hydroxylase (P450c11)." Chua S.C., Szabo P., Vitek A., Grzeschik K.H., John M., White P.C. Proc. Natl. Acad. Sci. U.S.A. 84:7193-7197(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [4] | "Cloning and characterization of bovine cytochrome P-450(11 beta) genes." Hashimoto T., Morohashi K., Omura T. J. Biochem. 105:676-679(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [5] | "Structural analysis of multiple bovine P-450(11 beta) genes and their promoter activities." Kirita S., Hashimoto T., Kitajima M., Honda S., Morohashi K., Omura T. J. Biochem. 108:1030-1041(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D00185 mRNA. Translation: BAA00127.1. Frameshift. D00361 mRNA. Translation: BAA00268.1. M17843 mRNA. Translation: AAA83383.1. D00455 Genomic DNA. Translation: BAA00347.1. |
| IPI | IPI00696443. |
| PIR | A28415. JX0071. JX0151. |
| RefSeq | NP_777063.2. NM_174638.3. |
| UniGene | Bt.4297. |
3D structure databases | |
| ProteinModelPortal | P15150. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9913.ENSBTAP00000037225. |
Proteomic databases | |
| PRIDE | P15150. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 282422. |
| KEGG | bta:282422. |
Organism-specific databases | |
| CTD | 1584. |
Phylogenomic databases | |
| eggNOG | COG2124. |
| HOGENOM | HOG000013161. |
| HOVERGEN | HBG051098. |
| InParanoid | P15150. |
| KO | K00497. |
| OrthoDB | EOG4B2SWV. |
Family and domain databases | |
| Gene3D | 1.10.630.10. 1 hit. |
| InterPro | IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view] |
| Pfam | PF00067. p450. 1 hit. [Graphical view] |
| PRINTS | PR00463. EP450I. PR00385. P450. |
| SUPFAM | SSF48264. Cytochrome_P450. 1 hit. |
| PROSITE | PS00086. CYTOCHROME_P450. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| BindingDB | P15150. |
| ChEMBL | CHEMBL2927. |
| NextBio | 20806202. |
Entry information
| Entry name | C11B1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P15150 Secondary accession number(s): Q29457 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
