Q05556 (CP2AB_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified December 11, 2013. Version 92. History...
Names and origin
|Protein names||Recommended name:|
Cytochrome P450 2A11
|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|
|Sequence length||494 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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.
RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.
Heme group By similarity.
Expressed in liver and lung as well as in nasal tissues.
Belongs to the cytochrome P450 family.
|Cellular component||Endoplasmic reticulum|
|Technical term||Complete proteome|
|Gene Ontology (GO)|
|Cellular_component||endoplasmic reticulum membrane|
Inferred from electronic annotation. Source: UniProtKB-SubCell
Inferred from electronic annotation. Source: UniProtKB-ECheme binding
Inferred from electronic annotation. Source: InterProiron ion binding
Inferred from electronic annotation. Source: InterPro
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 494||494||Cytochrome P450 2A11||PRO_0000051674|
|Metal binding||439||1||Iron (heme axial ligand) By similarity|
|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|
|||"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.
|||"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.
|L10237 mRNA. Translation: AAA31372.1.|
|RefSeq||NP_001164519.1. NM_001171048.1. |
3D structure databases
|SMR||Q05556. Positions 31-494. |
Protocols and materials databases
Genome annotation databases
Family and domain databases
|Gene3D||1.10.630.10. 1 hit. |
|InterPro||IPR001128. Cyt_P450. |
|Pfam||PF00067. p450. 1 hit. |
|PRINTS||PR00463. EP450I. |
|SUPFAM||SSF48264. SSF48264. 1 hit. |
|PROSITE||PS00086. CYTOCHROME_P450. 1 hit. |
|Accession||Primary (citable) accession number: Q05556|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families