Reviewed,
UniProtKB/Swiss-Prot P05176 (CP1A1_RABIT)
Last modified
October 13, 2009.
Version 75.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cytochrome P450 1A1 EC=1.14.14.1 Alternative name(s): CYPIA1 P450 isozyme 6 P-450 PHPAH1 P450 LM6 | ||
| Gene names |
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| Organism | Oryctolagus cuniculus (Rabbit) | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 518 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript 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. |
| 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. |
| Induction | By 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and by 3-methylcholanthrene (3MC). |
| 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 |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membraneInferred from electronic annotation. Source: UniProtKB-SubCell microsomeInferred 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 |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 518 | 518 | Cytochrome P450 1A1 | PRO_0000051632 | |||||
Sites | |||||||||
| Metal binding | 461 | 1 | Iron (heme axial ligand) | ||||||
Amino acid modifications | |||||||||
| Modified residue | 364 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 69 | 1 | R → L Ref.2 | ||||||
| Sequence conflict | 146 | 1 | L → R in AAA31431. Ref.2 | ||||||
| Sequence conflict | 176 – 177 | 2 | SK → GR in AAA31431. Ref.2 | ||||||
| Sequence conflict | 341 – 345 | 5 | PRIQR → RQHTRE in AAA31431. Ref.2 | ||||||
| Sequence conflict | 422 | 1 | P → R in AAA31431. Ref.2 | ||||||
| Sequence conflict | 429 – 430 | 2 | EA → RS Ref.2 | ||||||
| Sequence conflict | 442 – 443 | 2 | AV → TL Ref.2 | ||||||
| Sequence conflict | 446 – 449 | 4 | ALTE → GPDD Ref.2 | ||||||
| Sequence conflict | 463 | 1 | G → A in AAA31431. Ref.2 | ||||||
Sequences
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References
| [1] | "Structural analysis of cloned cDNAs for polycyclic hydrocarbon-inducible forms of rabbit liver microsomal cytochrome P-450." Kagawa N., Mihara K., Sato R. J. Biochem. 101:1471-1479(1987) [PubMed: 3667560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "Cloning and characterization of cDNAs encoding 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible rabbit mRNAs for cytochrome P-450 isozymes 4 and 6." Okino S.T., Quattrochi L.C., Barnes H.J., Osanto S., Griffin K.J., Johnson E.F., Tukey R.H. Proc. Natl. Acad. Sci. U.S.A. 82:5310-5314(1985) [PubMed: 2991917] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 56-518. |
Cross-references
Sequence databases | |
|---|---|
| M11727 mRNA. Translation: AAA31431.1. Sequence problems. X05685 mRNA. Translation: CAA29170.1. | |
| PIR | A27821. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1DT6 based on UniProtKB P00179. |
| SMR | P05176. Positions 36-516. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P05176. |
Genome annotation databases | |
| Ensembl | ENSOCUT00000017743; ENSOCUP00000015239; ENSOCUG00000017744; Oryctolagus cuniculus. [Genome view] |
Phylogenomic databases | |
| HOVERGEN | P05176. |
Enzyme and pathway databases | |
| BRENDA | 1.14.14.1. 255. |
Family and domain databases | |
| InterPro | IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. IPR008066. Cyt_P450_E_grp-I_CYP1. [Graphical view] |
| Gene3D | G3DSA:1.10.630.10. Cyt_P450. 1 hit. |
| PANTHER | PTHR19383. Cyt_P450. 1 hit. PTHR19383:SF63. Cyt_P450_E_grp-I_CYP1. 1 hit. |
| Pfam | PF00067. p450. 1 hit. [Graphical view] |
| PRINTS | PR00463. EP450I. PR01683. EP450ICYP1A. PR00385. P450. |
| PROSITE | PS00086. CYTOCHROME_P450. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CP1A1_RABIT | ||||||||
| Accession | Primary (citable) accession number: P05176 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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