P10611 (CP4A4_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 96.
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 4A4 EC=1.14.14.1 Alternative name(s): CYPIVA4 Cytochrome P450-P-2 Prostaglandin omega-hydroxylase | ||
| 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 | 510 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 | Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Catalyzes the omega- and (omega-1)-hydroxylation of fatty acids. Ref.3 |
| Catalytic activity | RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O. |
| Cofactor | Heme group By similarity. |
| Subcellular location | Endoplasmic reticulum membrane; Single-pass membrane protein. Microsome membrane; Single-pass membrane protein. |
| Induction | P450 can be induced to high levels in liver and other tissues by various foreign compounds, including drugs, pesticides, and carcinogens. |
| Sequence similarities | Belongs to the cytochrome P450 family. |
| Sequence caution | The sequence AAA31228.1 differs from that shown. Reason: Frameshift at position 23. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Membrane Microsome |
| Domain | Transmembrane Transmembrane helix |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Propeptide | 1 – 4 | 4 | Probable | PRO_0000003571 | |||||
| Chain | 5 – 510 | 506 | Cytochrome P450 4A4 | PRO_0000003572 | |||||
Regions | |||||||||
| Transmembrane | 11 – 31 | 21 | Helical; Potential | ||||||
Sites | |||||||||
| Metal binding | 457 | 1 | Iron (heme axial ligand) | ||||||
| Binding site | 321 | 1 | Heme (covalent; via 1 link) By similarity | ||||||
Sequences
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References
| [1] | "Rabbit prostaglandin omega-hydroxylase (CYP4A4): gene structure and expression." Palmer C.N., Griffin K.J., Johnson E.F. Arch. Biochem. Biophys. 300:670-676(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65. Strain: III/J. |
| [2] | "cDNA cloning and inducible expression during pregnancy of the mRNA for rabbit pulmonary prostaglandin omega-hydroxylase (cytochrome P-450p-2)." Matsubara S., Yamamoto S., Sogawa K., Yokotani N., Fujii-Kuriyama Y., Haniu M., Shively J.E., Gotoh O., Kusunose E., Kusunose M. J. Biol. Chem. 262:13366-13371(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-510, PROTEIN SEQUENCE OF 5-29. |
| [3] | "Purification and characterization of two forms of fatty acid omega-hydroxylase cytochrome P-450 from rabbit kidney cortex microsomes." Yoshimura R., Kusunose E., Yokotani N., Yamamoto S., Kubota I., Kusunose M. J. Biochem. 108:544-548(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L04758 Genomic DNA. Translation: AAA31228.1. Frameshift. J02818 mRNA. Translation: AAA31232.1. |
| PIR | A29368. S32315. |
3D structure databases | |
| ProteinModelPortal | P10611. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9986.ENSOCUP00000001485. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | COG2124. |
| HOGENOM | HOG000233833. |
| HOVERGEN | HBG000182. |
| OrthoDB | EOG4ZS93G. |
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 | P10611. |
| ChEMBL | CHEMBL4743. |
Entry information
| Entry name | CP4A4_RABIT | ||||||||
| Accession | Primary (citable) accession number: P10611 Secondary accession number(s): Q02927 | ||||||||
| 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
