Q94AU2
Gene name |
SEC22 (At1g11890, F12F1.27) |
Protein name |
25.3 kDa vesicle transport protein |
Names |
AtSEC22 |
Species |
Arabidopsis thaliana (Mouse-ear cress) |
KEGG Pathway |
ath:AT1G11890 |
EC number |
|
Protein Class |
|
Descriptions
(Annotation based on sequence homology with O08547)
Sec22b is a SNARE involved in endoplasmic reticulum/Golgi membrane trafficking. The SNARE protein Sec22 contains a signal that binds the COPII subcomplex Sec23/24 and specifies its endoplasmic reticulum (ER) exit as an unassembled SNARE. The N-terminal longin domain of Sec22 regulates the function of SNARE. SNARE motif in Sec22 folds against the N-terminal longin domain, and this closed form of Sec22 binds at the Sec23/24 interface.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q94AU2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q94AU2-F1 | Predicted | AlphaFoldDB |
2 variants for Q94AU2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| tmp_1_4012100_C_A | 102 | P>H | No | 1000Genomes | |
| ENSVATH04007845 | 219 | W>= | No | 1000Genomes |
No associated diseases with Q94AU2
Functions
10 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 membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| endoplasmic reticulum-Golgi intermediate compartment | A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport. |
| ER to Golgi transport vesicle membrane | The lipid bilayer surrounding a vesicle transporting substances from the endoplasmic reticulum to the Golgi. |
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
| Golgi apparatus | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| SNARE complex | A protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers. One well-characterized example is the neuronal SNARE complex formed of synaptobrevin 2, syntaxin 1a, and SNAP-25. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| SNAP receptor activity | Acting as a marker to identify a membrane and interacting selectively with one or more SNAREs on another membrane to mediate membrane fusion. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| endoplasmic reticulum to Golgi vesicle-mediated transport | The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi. |
| protein transport | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum | The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG. |
| vesicle fusion with Golgi apparatus | The joining of the lipid bilayer membrane around a vesicle to the lipid bilayer membrane around the Golgi. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q5ZJW4 | SEC22B | Vesicle-trafficking protein SEC22b | Gallus gallus (Chicken) | SS |
| O75396 | SEC22B | Vesicle-trafficking protein SEC22b | Homo sapiens (Human) | SS |
| O08547 | Sec22b | Vesicle-trafficking protein SEC22b | Mus musculus (Mouse) | EV |
| Q4KM74 | Sec22b | Vesicle-trafficking protein SEC22b | Rattus norvegicus (Rat) | SS |
| Q6P7L4 | sec22b | Vesicle-trafficking protein SEC22b | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | SS |
| Q7SXP0 | sec22bb | Vesicle-trafficking protein SEC22b-B | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| Q7ZV15 | sec22ba | Vesicle-trafficking protein SEC22b-A | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVKMTLIARV | TDGLPLAEGL | DDGRDLPDSD | MYKQQVKALF | KNLSRGQNDA | SRMSVETGPY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VFHYIIEGRV | CYLTMCDRSY | PKKLAFQYLE | DLKNEFERVN | GPNIETAARP | YAFIKFDTFI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QKTKKLYQDT | RTQRNIAKLN | DELYEVHQIM | TRNVQEVLGV | GEKLDQVSEM | SSRLTSESRI |
| 190 | 200 | 210 | |||
| YADKAKDLNR | QALIRKWAPV | AIVFGVVFLL | FWVKNKLW |