Q5RBQ1
Gene name |
CYP1A2 |
Protein name |
Cytochrome P450 1A2 |
Names |
CYPIA2, Cholesterol 25-hydroxylase, Hydroperoxy icosatetraenoate dehydratase |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100172368 |
EC number |
1.14.14.1: With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5RBQ1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5RBQ1-F1 | Predicted | AlphaFoldDB |
No variants for Q5RBQ1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5RBQ1 | |||||
No associated diseases with Q5RBQ1
1 regional properties for Q5RBQ1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Cytochrome P450, conserved site | 451 - 460 | IPR017972 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.14.1 | With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| aromatase activity | Catalysis of the reduction of an aliphatic ring to yield an aromatic ring. |
| estrogen 16-alpha-hydroxylase activity | Catalysis of the reaction: estrogen + donor-H2 + O2 = 16-alpha-hydroxyestrogen + H2O. |
| estrogen 2-hydroxylase activity | Catalysis of the reaction: estrogen + donor-H2 + O2 = 2-hydroxyestrogen + H2O. |
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| hydroperoxy icosatetraenoate dehydratase activity | A hydroperoxy icosatetraenoate <=> an oxoicosatetraenoate + H(2)O. |
| iron ion binding | Binding to an iron (Fe) ion. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| arachidonic acid metabolic process | The chemical reactions and pathways involving arachidonic acid, a straight chain fatty acid with 20 carbon atoms and four double bonds per molecule. Arachidonic acid is the all-Z-(5,8,11,14)-isomer. |
| cholesterol metabolic process | The chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. It is a component of the plasma membrane lipid bilayer and of plasma lipoproteins and can be found in all animal tissues. |
| estrogen metabolic process | The chemical reactions and pathways involving estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants. |
| retinol metabolic process | The chemical reactions and pathways involving retinol, one of the three compounds that makes up vitamin A. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALSQSVPFS | ATELLLASAI | FCLVFWVLKG | LRPRVPKGLK | SPPEPWGWPL | LGHVLTLRKN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PHLALSRMSQ | RYGDVLQIRI | GSTPVLVLSG | LDTIRQALVR | QGDDFKGRPD | LYSSTLITDG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QSLTFSPDSG | PVWAARRHLA | QNALNTFSIA | SDPASSYSCY | LEEHVSKEAE | ALISRLQELM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AGPGHFDPYN | QVVVSVVNVI | GAMCFGQHFP | ESSDEMLSLV | KNTHEFVETA | SSGNPVDFFP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ILRYLPNPAL | QRFKAFNQRF | LRFLRKTVQE | HYQDFDKNSV | QDIMGALFKY | SKKGPRASGN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LIPQEKIVNL | VNDIFGAGFD | TVTTAISWSL | MYLVTKPEIQ | RKIQKELDTM | IGRGRRPRLS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DRPQLPYLKA | FILETFRHSS | FLPFTIPHST | TRDTTLNGFY | IPKECCVFVN | QWQVNHDPEL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| WEDPSEFWPE | RFLTTDGTAI | NKPLSEKVML | FGMGKRRCIG | EVLANWEVFL | FLAILLQQLE |
| 490 | 500 | 510 | |||
| FSVPPGVKVD | LTPIYGLTMK | HARCEHVQAR | LRFSIK |