Q5R5G2
Gene name |
SEC23B |
Protein name |
Protein transport protein Sec23B |
Names |
SEC23-related protein B |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100173777 |
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 Q5R5G2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5R5G2-F1 | Predicted | AlphaFoldDB |
No variants for Q5R5G2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5R5G2 | |||||
No associated diseases with Q5R5G2
6 regional properties for Q5R5G2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Zinc finger, Sec23/Sec24-type | 58 - 98 | IPR006895 |
| domain | Sec23/Sec24, trunk domain | 127 - 392 | IPR006896 |
| domain | Sec23/Sec24, helical domain | 520 - 617 | IPR006900 |
| domain | Gelsolin-like domain | 633 - 719 | IPR007123 |
| domain | Sec23/Sec24 beta-sandwich | 403 - 506 | IPR012990 |
| domain | Sec23, C-terminal | 611 - 731 | IPR037550 |
Functions
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| COPII vesicle coat | One of two multimeric complexes that forms a membrane vesicle coat. COPII is best characterized in S. cerevisiae, where the subunits are called Sar1p, Sec13p, Sec31p, Sec23p, and Sec24p. Vesicles with COPII coats are found associated with endoplasmic reticulum (ER) membranes at steady state. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| 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 membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| COPII-coated vesicle budding | The evagination of an endoplasmic reticulum membrane, resulting in formation of a COPII-coated vesicle. |
| intracellular protein transport | The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATYLEFIQQ | NEERDGVRFS | WNVWPSSRLE | ATRMVVPLAC | LLTPLKERPD | LPPVQYEPVL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| CSRPTCKAVL | NPLCQVDYRA | KLWACNFCFQ | RNQFPPAYGG | ISEVNQPAEL | MPQFSTIEYV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IQRGAQSPLI | FLYVVDTCLE | EDDLQALKES | LQMSLSLLPP | DALVGLITFG | RMVQVHELSC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EGISKSYVFR | GTKDLTAKQI | QDMLGLTKPA | MPMQQARPAQ | PQEHPFASSR | FLQPVHKIDM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NLTDLLGELQ | RDPWPVTQGK | RPLRSTGVAL | SIAVGLLEGT | FPNTGARIML | FTGGPPTQGP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GMVVGDELKI | PIRSWHDIEK | DNARFMKKAT | KHYEMLANRT | AANGHCIDIY | ACALDQTGLL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EMKCCANLTG | GYMVMGDSFN | TSLFKQTFQR | IFTKDFNGDF | RMAFGATLDV | KTSRELKIAG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AIGPCVSLNV | KGPCVSENEL | GVGGTSQWKI | CGLDPTSTLG | IYFEVVNQHN | TPIPQGGRGA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IQFVTHYQHS | STQRRIRVTT | IARNWADVQS | QLRHIEAAFD | QEAAAVLMAR | LGVFRAESEE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GPDVLRWLDR | QLIRLCQKFG | QYNKEDPTSF | RLSDSFSLYP | QFMFHLRRSP | FLQVFNNSPD |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SSYYRHHFAR | QDLTQSLIMI | QPILYSYSFH | GPPEPVLLDS | SSILADRILL | MDTFFQIVIY |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LGETIAQWRK | AGYQDMPEYE | NFKHLLQAPL | DDAQEILQAR | FPMPRYINTE | HGGSQARFLL |
| 730 | 740 | 750 | 760 | ||
| SKVNPSQTHN | NLYAWGQETG | APILTDDVSL | QVFMDHLKKL | AVSSAC |