P15393 (C11B1_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 115.
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 Alternative name(s): CYPXIB1 Cytochrome P450(11 beta)-DS Cytochrome P450C11 Steroid 11-beta-hydroxylase EC=1.14.15.4 | ||||
| Gene names |
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| 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 | 499 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 | Forms corticosterone from 11-deoxycorticosterone. |
| Catalytic activity | A steroid + reduced adrenal ferredoxin + O2 = an 11-beta-hydroxysteroid + oxidized adrenal ferredoxin + H2O. |
| Cofactor | Heme group By similarity. |
| Subcellular location | |
| Tissue specificity | Adrenal zona fasciculata/reticularis. |
| Sequence similarities | Belongs to the cytochrome P450 family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 24 | 24 | Mitochondrion Ref.6 | ||||||
| Chain | 25 – 499 | 475 | Cytochrome P450 11B1, mitochondrial | PRO_0000003603 | |||||
Sites | |||||||||
| Metal binding | 446 | 1 | Iron (heme axial ligand) By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 127 | 1 | R → C in strain: Dahl salt-resistant. | ||||||
| Natural variant | 351 | 1 | V → A in strain: Dahl salt-resistant. | ||||||
| Natural variant | 381 | 1 | V → L in strain: Dahl salt-resistant. | ||||||
| Natural variant | 384 | 1 | I → L in strain: Dahl salt-resistant. | ||||||
| Natural variant | 443 | 1 | V → M in strain: Dahl salt-resistant. | ||||||
Sequences
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References
| [1] | "Molecular cloning and sequence analysis of cDNA encoding rat adrenal cytochrome P-450(11)beta." Nonaka Y., Matsukawa N., Morohashi K., Omura T., Ogihara T., Teraoka H., Okamoto M. FEBS Lett. 255:21-26(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. |
| [2] | "Dahl's salt-resistant normotensive rat has mutations in cytochrome P450(11 beta), but the salt-sensitive hypertensive rat does not." Matsukawa N., Nonaka Y., Higaki J., Nagano M., Mikami H., Ogihara T., Okamoto M. J. Biol. Chem. 268:9117-9121(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Dahl salt-resistant. Tissue: Adrenal gland. |
| [3] | "Isolation and characterization of rat CYP11B genes involved in late steps of mineralo- and glucocorticoid syntheses." Mukai K., Imai M., Shimada H., Ishimura Y. J. Biol. Chem. 268:9130-9137(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sprague-Dawley. Tissue: Testis. |
| [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. |
| [5] | "Cytochrome P450(11 beta): structure-function relationship of the enzyme and its involvement in blood pressure regulation." Okamoto M., Nonaka Y., Ohta M., Takemori H., Halder S.K., Zhi-Nong W., Sun T., Hatano O., Takakusa A., Murakami T. J. Steroid Biochem. Mol. Biol. 53:89-94(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: Dahl salt-resistant. |
| [6] | "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 25-44. Tissue: Adrenal cortex. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D11354 mRNA. Translation: BAA01957.1. D14091 Genomic DNA. Translation: BAA03171.1. X15431 mRNA. Translation: CAA33472.1. D10107 mRNA. Translation: BAA00988.1. |
| IPI | IPI00734638. |
| PIR | A46039. |
| UniGene | Rn.198235. |
3D structure databases | |
| ProteinModelPortal | P15393. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000039857. |
Proteomic databases | |
| PaxDb | P15393. |
| PRIDE | P15393. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| UCSC | RGD:2453. rat. |
Organism-specific databases | |
| RGD | 2453. Cyp11b1. |
Phylogenomic databases | |
| eggNOG | COG2124. |
| HOGENOM | HOG000013161. |
| HOVERGEN | HBG051098. |
| InParanoid | P15393. |
| OrthoDB | EOG4B2SWV. |
Enzyme and pathway databases | |
| SABIO-RK | P15393. |
Gene expression databases | |
| ArrayExpress | P15393. |
| Genevestigator | P15393. |
| GermOnline | ENSRNOG00000032450. 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 | |
| BindingDB | P15393. |
| ChEMBL | CHEMBL4970. |
| NextBio | 21682341. |
Entry information
| Entry name | C11B1_RAT | ||||||||
| Accession | Primary (citable) accession number: P15393 Secondary accession number(s): Q64655 | ||||||||
| 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
