Q5WA72
Gene name |
PDIL1-5 (PDIL3-1) |
Protein name |
Protein disulfide isomerase-like 1-5 |
Names |
OsPDIL1-5, Protein disulfide isomerase-like 3-1, OsPDIL3-1 |
Species |
Oryza sativa subsp japonica (Rice) |
KEGG Pathway |
osa:4340223 |
EC number |
5.3.4.1: Transposing S-S bonds |
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 Q5WA72
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5WA72-F1 | Predicted | AlphaFoldDB |
No variants for Q5WA72
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5WA72 | |||||
No associated diseases with Q5WA72
2 regional properties for Q5WA72
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Thioredoxin domain | 51 - 196 | IPR013766-1 |
| domain | Thioredoxin domain | 387 - 516 | IPR013766-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.3.4.1 | Transposing S-S bonds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| endoplasmic reticulum lumen | The volume enclosed by the membranes of the endoplasmic reticulum. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| protein disulfide isomerase activity | Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| response to endoplasmic reticulum stress | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q29RV1 | PDIA4 | Protein disulfide-isomerase A4 | Bos taurus (Bovine) | PR |
| Q8N807 | PDILT | Protein disulfide-isomerase-like protein of the testis | Homo sapiens (Human) | PR |
| Q13087 | PDIA2 | Protein disulfide-isomerase A2 | Homo sapiens (Human) | PR |
| Q17770 | pdi-2 | Protein disulfide-isomerase 2 | Caenorhabditis elegans | PR |
| A3KPF5 | PDIL1-5 | Protein disulfide isomerase-like 1-5 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q66GQ3 | PDIL1-6 | Protein disulfide isomerase-like 1-6 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRARRVVAAA | AVLLLFAVVA | VARLDLDDDG | DDSEVLDELL | AVDEEEERGE | LGGGGEAAAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EAVRRAQSMV | LVLDNDNARR | AVEENAEVLL | LGYAPWCERS | AQLMPRFAEA | AAALRAMGSA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VAFAKLDGER | YPKAASAVGV | KGFPTVLLFV | NGTEHQFTGL | HTKDAIVTWV | RKKTGAPASR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IQSKDSAEEF | LKKDQTFAVG | LFKNFEGAEY | EEFVKAATSE | NEVQFVETND | RNVAKILFPG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IASEEQFLGL | VKSEPEKFEK | FNGAFEEKEI | IQFVELNKFP | LITVFTDLNS | GKVYGSPIKL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QVFTFAEAYD | FEDLESMIQE | VARGFKTKIM | LIYVDTAEEK | LAKPFLTLYG | LEPEKPTVTA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FDTSKGTKYL | MEAEINAKNL | QDFCLSLLEG | TLPPYFRSEP | VPEEKGPIEK | VVGRTFDSSV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LESPQNVFLE | VHAPWCVDCE | AISKNVEKLA | KHFNDLGQTN | LKFARIDASV | NEHPKLQINN |
| 490 | 500 | 510 | 520 | 530 | |
| YPTLLLYPAQ | DKSNPIKLSK | KSNLKDMAKF | VKEKLQIADV | ETVAAGDIVK | DEL |