Reviewed,
UniProtKB/Swiss-Prot P22443 (CP19A_RAT)
Last modified
June 16, 2009.
Version 73.
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 19A1 EC=1.14.14.1 Alternative name(s): CYPXIX Aromatase Estrogen synthetase P-450AROM | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||||
| 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 | 508 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Catalyzes the formation of aromatic C18 estrogens from C19 androgens. |
| Catalytic activity | RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O. |
| Cofactor | Heme group By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the cytochrome P450 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Monooxygenase Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | estrogen biosynthetic process Traceable author statement. Source: RGD oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW regulation of synapse structure and activityInferred from mutant phenotype. Source: RGD |
| Cellular component | dendritic spine Inferred from direct assay. Source: RGD endoplasmic reticulumInferred from direct assay. Source: RGD membraneInferred from electronic annotation. Source: UniProtKB-SubCell nerve terminalInferred from direct assay. Source: RGD synaptic vesicleInferred from direct assay. Source: RGD |
| 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 – 508 | 508 | Cytochrome P450 19A1 | PRO_0000051962 | |||||
Sites | |||||||||
| Metal binding | 437 | 1 | Iron (heme axial ligand) | ||||||
Experimental info | |||||||||
| Sequence conflict | 3 – 4 | 2 | LE → FQ Ref.2 | ||||||
| Sequence conflict | 10 | 1 | H → Q Ref.2 | ||||||
| Sequence conflict | 88 | 1 | W → C Ref.2 | ||||||
| Sequence conflict | 101 | 1 | S → L Ref.2 | ||||||
| Sequence conflict | 123 – 129 | 7 | QCIGMHE → VVHGHAR Ref.2 | ||||||
| Sequence conflict | 188 | 1 | V → L Ref.2 | ||||||
| Sequence conflict | 210 | 1 | E → G Ref.2 | ||||||
| Sequence conflict | 328 – 331 | 4 | VETA → WKQ Ref.2 | ||||||
| Sequence conflict | 342 | 1 | D → A Ref.2 | ||||||
| Sequence conflict | 364 – 369 | 6 | LRYQPV → CGISPF Ref.2 | ||||||
| Sequence conflict | 422 | 1 | V → L Ref.2 | ||||||
| Sequence conflict | 425 | 1 | R → T Ref.2 | ||||||
| Sequence conflict | 449 | 1 | V → I Ref.2 | ||||||
| Sequence conflict | 466 | 1 | R → K Ref.2 | ||||||
| Sequence conflict | 493 – 497 | 5 | RHIFN → SPRNS Ref.2 | ||||||
Sequences
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References
| [1] | "Aromatase cytochrome P450 in rat ovarian granulosa cells before and after luteinization: adenosine 3',5'-monophosphate-dependent and independent regulation. Cloning and sequencing of rat aromatase cDNA and 5' genomic DNA." Hickey G.J., Krasnow J.S., Beattie W.G., Richards J.S. Mol. Endocrinol. 4:3-12(1990) [PubMed: 2157976] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary. |
| [2] | "The structure of cDNA clones encoding the aromatase P-450 isolated from a rat Leydig cell tumor line demonstrates differential processing of aromatase mRNA in rat ovary and a neoplastic cell line." Lephart E.D., Peterson K.G., Noble J.F., George F.W., McPhaul M.J. Mol. Cell. Endocrinol. 70:31-40(1990) [PubMed: 2340950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| M33986 mRNA. Translation: AAA41044.1. | |
| IPI | IPI00207135. |
| PIR | A36121. |
| UniGene | Rn.21402 |
3D structure databases | |
| ModBase | Search... |
Organism-specific databases | |
| RGD | 2457. Cyp19a1. |
Phylogenomic databases | |
| HOVERGEN | P22443. |
Enzyme and pathway databases | |
| BRENDA | 1.14.14.1. 248. |
Gene expression databases | |
| ArrayExpress | P22443. |
Family and domain databases | |
| InterPro | IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view] |
| Gene3D | G3DSA:1.10.630.10. Cyt_P450. 1 hit. |
| PANTHER | PTHR19383. Cyt_P450. 1 hit. |
| Pfam | PF00067. p450. 1 hit. [Graphical view] |
| PRINTS | PR00463. EP450I. PR00385. P450. |
| PROSITE | PS00086. CYTOCHROME_P450. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CP19A_RAT | ||||||||
| Accession | Primary (citable) accession number: P22443 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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