Q0P483
Gene name |
slc25a42 (zgc:153304) |
Protein name |
Mitochondrial coenzyme A transporter SLC25A42 |
Names |
Solute carrier family 25 member 42 |
Species |
Danio rerio (Zebrafish) (Brachydanio rerio) |
KEGG Pathway |
dre:751743 |
EC number |
|
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 Q0P483
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q0P483-F1 | Predicted | AlphaFoldDB |
No variants for Q0P483
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q0P483 | |||||
No associated diseases with Q0P483
3 regional properties for Q0P483
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Mitochondrial substrate/solute carrier | 33 - 123 | IPR018108-1 |
| repeat | Mitochondrial substrate/solute carrier | 131 - 217 | IPR018108-2 |
| repeat | Mitochondrial substrate/solute carrier | 226 - 317 | IPR018108-3 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| mitochondrial inner membrane | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. |
| 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. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ADP phosphatase activity | Catalysis of the reaction: ADP + H2O = AMP + phosphate. |
| ADP transmembrane transporter activity | Enables the transfer of ADP, adenosine diphosphate, from one side of a membrane to the other. |
| AMP transmembrane transporter activity | Enables the transfer of AMP, adenosine monophosphate, from one side of a membrane to the other. |
| ATP transmembrane transporter activity | Enables the transfer of ATP, adenosine triphosphate, from one side of a membrane to the other. |
| coenzyme A transmembrane transporter activity | Enables the transfer of coenzyme A from one side of a membrane to the other. Coenzyme A, 3'-phosphoadenosine-(5')diphospho(4')pantatheine, is an acyl carrier in many acylation and acyl-transfer reactions in which the intermediate is a thiol ester. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| ADP transport | The directed movement of ADP, adenosine diphosphate, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| AMP transport | The directed movement of AMP, adenosine monophosphate, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| ATP transport | The directed movement of ATP, adenosine triphosphate, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| coenzyme A transmembrane transport | The process in which coenzyme A is transported across a membrane. Coenzyme A, 3'-phosphoadenosine-(5')diphospho(4')pantatheine, is an acyl carrier in many acylation and acyl-transfer reactions in which the intermediate is a thiol ester. |
| mitochondrial membrane organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrial membrane, either of the lipid bilayer surrounding a mitochondrion. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGNVVQERQG | ALAQGEVLPR | PAASQSEGFK | QGRSVLNSLV | SGAFAGAVAK | TAVAPLDRTK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IIFQVSSNRF | SAKEAYRLIY | RTYLKDGFFS | LWRGNSATMV | RVIPYAAIQF | CAHEQYKGIL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GKYYGFQGKA | LPPVPRLLAG | SLAGTTAAII | TYPLDMVRAR | MAVTPKEMYS | NIMDVFVRIS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| REEGLKTLYR | GFTPTILGVV | PYAGLSFFTY | ETLKKTHAEK | TGRAHPFPYE | RLVFGACAGL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IGQSASYPLD | VVRRRMQTAG | VTGHTYSTVL | GTMREIVAEE | GIVRGLYKGL | SMNWVKGPIA |
| 310 | 320 | ||||
| VGISFMTFDL | TQILLRKFQL | L |