Q3B7D0
Gene name |
Cpox |
Protein name |
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial |
Names |
COX, Coprogen oxidase, Coproporphyrinogenase |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:304024 |
EC number |
1.3.3.3: With oxygen as acceptor |
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 Q3B7D0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3B7D0-F1 | Predicted | AlphaFoldDB |
No variants for Q3B7D0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q3B7D0 | |||||
No associated diseases with Q3B7D0
1 regional properties for Q3B7D0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Coproporphyrinogen III oxidase, conserved site | 305 - 329 | IPR018375 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.3.3.3 | With oxygen as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| mitochondrial inner membrane | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. |
| mitochondrial intermembrane space | The region between the inner and outer lipid bilayers of the mitochondrial envelope. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| coproporphyrinogen oxidase activity | Catalysis of the reaction: coproporphyrinogen III + 2 H(+) + O(2) = 2 CO(2) + 2 H(2)O + protoporphyrinogen IX. |
| identical protein binding | Binding to an identical protein or proteins. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| structural constituent of eye lens | The action of a molecule that contributes to the structural integrity of the lens of an eye. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| heme biosynthetic process | The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors. |
| protoporphyrinogen IX biosynthetic process | The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX. |
| response to arsenic-containing substance | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an arsenic stimulus from compounds containing arsenic, including arsenates, arsenites, and arsenides. |
| response to inorganic substance | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an inorganic substance stimulus. |
| response to insecticide | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insecticide stimulus. Insecticides are chemicals used to kill insects. |
| response to iron ion | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an iron ion stimulus. |
| response to lead ion | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lead ion stimulus. |
| response to methylmercury | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a methylmercury stimulus. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9V3D2 | Coprox | Oxygen-dependent coproporphyrinogen-III oxidase | Drosophila melanogaster (Fruit fly) | PR |
| P36551 | CPOX | Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial | Homo sapiens (Human) | PR |
| P36552 | Cpox | Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALRLGQLGS | GPWWRAVRGD | YAQLRAPSPR | SASACVCRLP | GTAGTQPRRG | LGHGSSAGGG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SRLGTGLAAA | LAGMAGLAAA | VLGHVQRAEM | VPKSSGARSP | SPGRLEEDGD | ELARRCSTFM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SSPVTELREL | GRRPDDMKTK | MELMIMETQA | QVCRALAQVD | GVADFSVDRW | ERKEGGGGIT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CVLQDGRVFE | KAGVNISVVH | GNLSEEAANQ | MRSRGKALKK | KDGKLPFTAM | GISSVIHPKN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PYAPTMHFNY | RYFEVEEADG | KMHWWFGGGC | DLTPTYLNRE | DAVHFHRTLK | EACDQHGPDI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YPKFKKWCDD | YFFIAHRGER | RGIGGIFFDD | LDSPSKEEAF | RFVKTCAEAV | VPSYVPIVKK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HCDDSYTPQD | KLWQQLRRGR | YVEFNLVYDR | GTKFGLFTPG | SRIESILMSL | PLTARWEYMH |
| 430 | 440 | ||||
| SPPENSKEAE | ILEVLRHPKD | WVH |