Q9D662
Gene name |
Sec23b |
Protein name |
Protein transport protein Sec23B |
Names |
SEC23-related protein B |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:27054 |
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 Q9D662
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9D662-F1 | Predicted | AlphaFoldDB |
29 variants for Q9D662
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3392351019 | 9 | Q>L | No | EVA | |
| rs3392357472 | 10 | Q>L | No | EVA | |
| rs3388592701 | 53 | P>H | No | EVA | |
| rs3388594990 | 58 | P>T | No | EVA | |
| rs3392329582 | 59 | V>E | No | EVA | |
| rs3388600854 | 64 | P>S | No | EVA | |
| rs13465661 | 108 | A>G | No | EVA | |
| rs3388600900 | 113 | Q>E | No | EVA | |
| rs3388600888 | 212 | P>S | No | EVA | |
| rs259771810 | 216 | A>S | No | EVA | |
| rs3392184004 | 239 | D>G | No | EVA | |
| rs3388594961 | 244 | D>E | No | EVA | |
| rs3388596531 | 310 | T>I | No | EVA | |
| rs13465664 | 315 | W>C | No | EVA | |
| rs13465662 | 319 | E>Q | No | EVA | |
| rs3388592808 | 320 | K>R | No | EVA | |
| rs3392328293 | 355 | D>V | No | EVA | |
| rs3388598495 | 364 | C>* | No | EVA | |
| rs3388592862 | 396 | F>I | No | EVA | |
| rs3388600838 | 412 | T>A | No | EVA | |
| rs3392351051 | 450 | I>N | No | EVA | |
| rs3388599477 | 451 | C>Y | No | EVA | |
| rs3388583992 | 482 | Q>H | No | EVA | |
| rs3388589142 | 503 | R>H | No | EVA | |
| rs3388596344 | 590 | P>Q | No | EVA | |
| rs3388592852 | 650 | L>P | No | EVA | |
| rs3388596273 | 669 | W>R | No | EVA | |
| rs3388596489 | 705 | P>A | No | EVA | |
| rs3388589453 | 765 | S>R | No | EVA |
No associated diseases with Q9D662
6 regional properties for Q9D662
| 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 - 618 | IPR006900 |
| domain | Gelsolin-like domain | 634 - 720 | IPR007123 |
| domain | Sec23/Sec24 beta-sandwich | 403 - 506 | IPR012990 |
| domain | Sec23, C-terminal | 612 - 732 | IPR037550 |
Functions
7 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. |
| endomembrane system | A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles. |
| 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 exit site | An endoplasmic reticulum part at which COPII-coated vesicles are produced. |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTPase activator activity | Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| COPII-coated vesicle cargo loading | The formation of a macromolecular complex between the COPII coat proteins and proteins and/or lipoproteins that are going to be transported by the COPII vesicle to the Golgi. |
| 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. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q3SZN2 | SEC23B | Protein transport protein Sec23B | Bos taurus (Bovine) | PR |
| Q5ZK03 | SEC23A | Protein transport protein Sec23A | Gallus gallus (Chicken) | PR |
| Q15436 | SEC23A | Protein transport protein Sec23A | Homo sapiens (Human) | PR |
| Q15437 | SEC23B | Protein transport protein Sec23B | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATYLEFIQQ | NEERDGVRFS | WNVWPSSRLE | ATRMVVPLAC | LLTPLKERPD | LPPVQYEPVL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| CSRPTCKAIL | NPLCQVDYRA | KLWACNFCFQ | RNQFPPAYAG | ISEVNQPAEL | MPQFSTIEYM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IQRGARSPLI | FLYVVDTCLE | EDDLQALKES | LQMSLSLLPP | DALVGLITFG | RMVQVHELSC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EGISKSYVFR | GTKDLTAKQI | QEMLGLTKSA | MPVQQARPAQ | PQEQPFVSSR | FLQPIHKIDM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NLTDLLGELQ | RDPWPVTQGK | RPLRSTGVAL | SIAVGLLEGT | FPNTGARIML | FTGGPPTQGP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GMVVGDELKT | PIRSWHDIEK | DNARFMKKAT | KHYEMLANRT | ATNGHCIDIY | ACALDQTGLL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EMKCCPNLTG | GHMVMGDSFN | TSLFKQTFQR | IFSKDFNGDF | RMAFGATLDV | KTSRELKIAG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AIGPCVSLNV | KGPCVSENEL | GVGGTSQWKI | CGLDPSSTLG | IYFEVVNQHN | APVPQGGRGA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IQFVTQYQHS | STQKRIRVTT | IARNWADAQS | QLRHIEAAFD | QEAAAVLMAR | LGVFRAESEE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GPDVLRWLDR | QLIRLCQKFG | QYNKEDPTSF | RLSDSFSLYP | QFMFHLRRSP | FLQVFNNSPD |
| 610 | 620 | 630 | 640 | 650 | 660 |
| ESSYYRHHFA | RQDLTQSLIM | IQPILYSYSF | HGPPEPVLLD | SSSILADRIL | LMDTFFQIVI |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YLGETIAQWR | KAGYQDMPEY | ENFKHLLQAP | LDDAQEILQA | RFPMPRYINT | EHGGSQARFL |
| 730 | 740 | 750 | 760 | ||
| LSKVNPSQTH | NNLYAWGQET | GAPILTDDVS | LQVFMDHLKK | LAVSSAS |