Q2LA59
Gene name |
CYP21 |
Protein name |
Steroid 21-hydroxylase |
Names |
21-OHase, Cytochrome P-450c21, Cytochrome P450 21, Cytochrome P450 XXI, Cytochrome P450-C21 |
Species |
Lynx lynx (Eurasian lynx) (Felis lynx) |
KEGG Pathway |
|
EC number |
1.14.14.16: 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 Q2LA59
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2LA59-F1 | Predicted | AlphaFoldDB |
No variants for Q2LA59
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2LA59 | |||||
No associated diseases with Q2LA59
1 regional properties for Q2LA59
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Cytochrome P450, conserved site | 419 - 428 | IPR017972 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.14.16 | 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 |
|---|---|
| 17-hydroxyprogesterone 21-hydroxylase activity | Catalysis of the reaction: 17alpha-hydroxyprogesterone + O2 + reduced = 11-deoxycortisol + H(+) + H2O + oxidized |
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| iron ion binding | Binding to an iron (Fe) ion. |
| progesterone 21-hydroxylase activity | Catalysis of the reaction: O2 + progesterone + reduced = 21-hydroxyprogesterone + H(+) + H2O + oxidized |
| steroid binding | Binding to a steroid, any of a large group of substances that have in common a ring system based on 1,2-cyclopentanoperhydrophenanthrene. |
| steroid hydroxylase activity | Catalysis of the formation of a hydroxyl group on a steroid by incorporation of oxygen from O2. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| steroid biosynthetic process | The chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus; includes de novo formation and steroid interconversion by modification. |
| steroid metabolic process | The chemical reactions and pathways involving steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLLLGLLLLT | ALAGARLLWN | KWKYRSLHLP | PLAPGFLHLL | QPDLPIYLLG | LTQKLGPVYR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LRLGLQDVVV | LNSKRTIEEA | MIRRWVDFAG | RPQMPSYKLV | SQPYQDLSLG | DYSLLWKAHK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KLTRSALLLG | IRNSMEPLVE | QLTQEFCERM | RAQAGTPVAI | QKEFSFLTCS | VICCLTFGDK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EDTLVHAFHD | CVQDLMKSWE | HWSIQVLDIV | PFLRFFPNPG | LQRLKQALEN | RDRIVEKQLR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QHKDSMVAGQ | WRDMTDYMLQ | GMGKPRAEKG | HGRLLEGHVH | MSVVDLFIGG | TETTATTLSW |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AVAFLLHHPE | IQQRLQEELD | CELGPGASGS | RVPLKDPSRL | PLLTATIAEV | LRLRPVVPLA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LPHRTTRHSS | ILGYDIPEGT | VVIPNLQGAH | LDDTVWEQPH | EFRPDRFLVP | GASPRVLAFG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| CGARVCLGEP | LARLELFVVL | ARLLHAFTLL | PPTGPLPSLR | PRSHCGINLT | MQPFQVQLQP |
| 490 | |||||
| RGAVAPGPSQ | HQ |