O08547
Gene name |
Sec22b (Sec22l1) |
Protein name |
Vesicle-trafficking protein SEC22b |
Names |
ER-Golgi SNARE of 24 kDa, ERS-24, ERS24, SEC22 vesicle-trafficking protein homolog B, SEC22 vesicle-trafficking protein-like 1, mSec22b |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:20333 |
EC number |
|
Protein Class |
VESICLE-TRAFFICKING PROTEIN SEC22B (PTHR45837) |
Descriptions
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 |
134-194 (v-SNARE coiled-coil homology) |
Relief mechanism |
Others, PTM |
Assay |
Structural analysis |
Accessory elements
No accessory elements
References
- Gonzalez LC Jr et al. (2001) "A novel snare N-terminal domain revealed by the crystal structure of Sec22b", The Journal of biological chemistry, 276, 24203-11
- Wen W et al. (2010) "Lipid-Induced conformational switch controls fusion activity of longin domain SNARE Ykt6", Molecular cell, 37, 383-95
- Mancias JD et al. (2007) "The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope", Molecular cell, 26, 403-14
Autoinhibited structure
Activated structure
13 structures for O08547
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1IFQ | X-ray | 240 A | A/B | 2-127 | PDB |
| 5VNE | X-ray | 270 A | C | 1-157 | PDB |
| 5VNF | X-ray | 241 A | C | 1-157 | PDB |
| 5VNG | X-ray | 260 A | C | 1-157 | PDB |
| 5VNH | X-ray | 260 A | C | 1-157 | PDB |
| 5VNI | X-ray | 279 A | C | 1-157 | PDB |
| 5VNJ | X-ray | 281 A | C | 1-157 | PDB |
| 5VNK | X-ray | 255 A | C | 1-157 | PDB |
| 5VNL | X-ray | 239 A | C | 1-157 | PDB |
| 5VNM | X-ray | 277 A | C | 1-157 | PDB |
| 5VNN | X-ray | 250 A | C | 1-157 | PDB |
| 5VNO | X-ray | 290 A | C | 1-157 | PDB |
| AF-O08547-F1 | Predicted | AlphaFoldDB |
1 variants for O08547
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs222451417 | 93 | S>L | No | Ensembl |
No associated diseases with O08547
Functions
| Description | ||
|---|---|---|
| EC Number | ||
| Subcellular Localization |
|
|
| PANTHER Family | PTHR45837 | VESICLE-TRAFFICKING PROTEIN SEC22B |
| PANTHER Subfamily | PTHR45837:SF3 | VESICLE-TRAFFICKING PROTEIN SEC22B |
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
10 GO annotations of cellular component
| Name | Definition |
|---|---|
| COPI-coated vesicle | A vesicle with a coat formed of the COPI coat complex proteins. COPI-coated vesicles are found associated with Golgi membranes at steady state, are involved in Golgi to endoplasmic reticulum (retrograde) vesicle transport, and possibly also in intra-Golgi transport. |
| 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. |
| endoplasmic reticulum-Golgi intermediate compartment membrane | The lipid bilayer surrounding any of the compartments of the endoplasmic reticulum (ER)-Golgi intermediate compartment system. |
| ER to Golgi transport vesicle membrane | The lipid bilayer surrounding a vesicle transporting substances from the endoplasmic reticulum to the Golgi. |
| 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. |
| melanosome | A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells. |
| 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. |
| synaptic vesicle | A secretory organelle, typically 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane. |
2 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. |
| syntaxin binding | Binding to a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse. |
7 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. |
| negative regulation of autophagosome assembly | Any process that stops, prevents or reduces the frequency, rate or extent of autophagosome assembly. |
| positive regulation of protein catabolic process | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
| 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. |
| vesicle-mediated transport | A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane. |
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 |
| Q4KM74 | Sec22b | Vesicle-trafficking protein SEC22b | Rattus norvegicus (Rat) | SS |
| Q94AU2 | SEC22 | 25.3 kDa vesicle transport protein | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 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 |
| MVLLTMIARV | ADGLPLAASM | QEDEQSGRDL | QQYQSQAKQL | FRKLNEQSPT | RCTLEAGAMT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FHYIIEQGVC | YLVLCEAAFP | KKLAFAYLED | LHSEFDEQHG | KKVPTVSRPY | SFIEFDTFIQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KTKKLYIDSR | ARRNLGSINT | ELQDVQRIMV | ANIEEVLQRG | EALSALDSKA | NNLSSLSKKY |
| 190 | 200 | 210 | |||
| RQDAKYLNMR | STYAKLAAVA | VFFIMLIVYV | RFWWL |