Q58EK4
Gene name |
parl |
Protein name |
Presenilins-associated rhomboid-like protein, mitochondrial |
Names |
|
Species |
Danio rerio (Zebrafish) (Brachydanio rerio) |
KEGG Pathway |
dre:541485 |
EC number |
3.4.21.105: Serine endopeptidases |
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 Q58EK4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q58EK4-F1 | Predicted | AlphaFoldDB |
No variants for Q58EK4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q58EK4 | |||||
No associated diseases with Q58EK4
1 regional properties for Q58EK4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase S54, rhomboid domain | 207 - 350 | IPR022764 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.21.105 | Serine endopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 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. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| serine-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| signal peptide processing | The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9H300 | PARL | Presenilins-associated rhomboid-like protein, mitochondrial | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAWRSCFMKW | TQINSINASS | LCPKSTRLNI | HPQQRCGFRK | TERPSESKKG | VQETEAEAGG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HNRAVPPKPV | PPLPPRRPHQ | LFRPLVFTVG | FTGCSFGAAA | ILQYESVKSR | VQLAIEEAKE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EKRDTLLEGH | DTTYWHNWWN | QLSNFQKQVI | LLISAVDDFW | SGLSEGQKTV | TGIIALNTVV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LCCWRVPAMQ | RFLVKYFTSN | PASKTRCLPM | VLSSFSHYSV | IHMVVNMYVL | WTFSSSIVSL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LGREQFLALY | LSGGVISTFV | SYVFKTATGR | LGPSLGASGS | IMTVLAAVCT | KIPEAKLGIV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLPVISFSAG | NALKALVALD | IAGLVLGWRF | FDHAAHLGGA | LFGVWYIGYG | HELIWRKREP |
| 370 | 380 | ||||
| LIKFWHELRN | MSPGRPGPGG | GGG |