Q05556 (CP2AB_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 90.
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 2A11 EC=1.14.14.1 Alternative name(s): CYPIIA11 Cytochrome P450-IIA11 | ||
| Gene names |
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| Organism | Oryctolagus cuniculus (Rabbit) [Reference proteome] | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus![]() |
Protein attributes
| Sequence length | 494 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the oxygenation of a variety of substrates, including ethanol and procarcinogens such as N-nitrosodiethylamine and phenacetin. Has no or little activity as a coumarin 7-hydroxylase and in the formation of androstenedione from testosterone. |
| Catalytic activity | RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O. |
| Cofactor | Heme group By similarity. |
| Subcellular location | Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. |
| Tissue specificity | Expressed in liver and lung as well as in nasal tissues. |
| Sequence similarities | Belongs to the cytochrome P450 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Membrane Microsome |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | aromatase activity Inferred from electronic annotation. Source: EC electron carrier activityInferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 494 | 494 | Cytochrome P450 2A11 | PRO_0000051674 | |||||
Sites | |||||||||
| Metal binding | 439 | 1 | Iron (heme axial ligand) By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 62 – 63 | 2 | RD → SE: No effect. Almost as active as CYP2A10 in coumarin hydroxylation and approximately half as active as CYP2A10 in androstenedione formation; when associated with L-104; V-117 and S-120. | ||||||
| Mutagenesis | 104 | 1 | Q → L: No effect. Almost as active as CYP2A10 in coumarin hydroxylation and approximately half as active as CYP2A10 in androstenedione formation; when associated with 62-SE-63; V-117 and S-120. Ref.2 | ||||||
| Mutagenesis | 117 | 1 | A → V: No effect. Almost as active as CYP2A10 in coumarin hydroxylation and approximately half as active as CYP2A10 in androstenedione formation; when associated with 62-SE-63; L-104 and S-120. Ref.2 | ||||||
| Mutagenesis | 120 | 1 | T → S: No effect. Almost as active as CYP2A10 in coumarin hydroxylation and approximately half as active as CYP2A10 in androstenedione formation; when associated with 62-SE-63; L-104 and V-117. Ref.2 | ||||||
| Mutagenesis | 372 | 1 | R → H: Significant increase in the rate of hydroxylation of testosterone, but not of coumarin. Ref.2 | ||||||
Sequences
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References
| [1] | "Isolation and heterologous expression of cloned cDNAs for two rabbit nasal microsomal proteins, CYP2A10 and CYP2A11, that are related to nasal microsomal cytochrome P450 form a." Peng H.-M., Ding X., Coon M.J. J. Biol. Chem. 268:17253-17260(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: New Zealand white. Tissue: Nasal mucosa. |
| [2] | "Structure-function analysis of CYP2A10 and CYP2A11, P450 cytochromes that differ in only eight amino acids but have strikingly different activities toward testosterone and coumarin." Ding X., Peng H.-M., Coon M.J. Biochem. Biophys. Res. Commun. 203:373-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF 62-ARG-ASP-63; GLN-104; ALA-117; THR-120 AND ARG-372. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L10237 mRNA. Translation: AAA31372.1. |
| PIR | B47494. |
| RefSeq | NP_001164519.1. NM_001171048.1. |
| UniGene | Ocu.1915. |
3D structure databases | |
| ProteinModelPortal | Q05556. |
| SMR | Q05556. Positions 31-494. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100328596. |
Organism-specific databases | |
| CTD | 100328596. |
Phylogenomic databases | |
| HOVERGEN | HBG015789. |
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. IPR008067. Cyt_P450_E_grp-I_CYP2A-like. [Graphical view] |
| Pfam | PF00067. p450. 1 hit. [Graphical view] |
| PRINTS | PR00463. EP450I. PR01684. EP450ICYP2A. PR00385. P450. |
| SUPFAM | SSF48264. Cytochrome_P450. 1 hit. |
| PROSITE | PS00086. CYTOCHROME_P450. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CP2AB_RABIT | ||||||||
| Accession | Primary (citable) accession number: Q05556 | ||||||||
| 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
