Q5ZJW4
Gene name |
SEC22B (RCJMB04_15c3) |
Protein name |
Vesicle-trafficking protein SEC22b |
Names |
SEC22 vesicle-trafficking protein homolog B |
Species |
Gallus gallus (Chicken) |
KEGG Pathway |
gga:424377 |
EC number |
|
Protein Class |
|
Descriptions
Autoinhibitory domains (AIDs)
Target domain |
134-194 (v-SNARE coiled-coil homology) |
Relief mechanism |
Others, PTM |
Assay |
|
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
1 structures for Q5ZJW4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5ZJW4-F1 | Predicted | AlphaFoldDB |
7 variants for Q5ZJW4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs740117324 | 5 | T>P | No | EVA | |
| rs736484234 | 58 | A>G | No | EVA | |
| rs732939134 | 112 | F>L | No | EVA | |
| rs736500333 | 113 | I>N | No | EVA | |
| rs741253532 | 114 | E>* | No | EVA | |
| rs736580516 | 145 | V>G | No | EVA | |
| rs738887418 | 216 | L>W | No | EVA |
No associated diseases with Q5ZJW4
5 regional properties for Q5ZJW4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Cation-transporting P-type ATPase, N-terminal | 140 - 214 | IPR004014 |
| domain | Cation-transporting P-type ATPase, C-terminal | 877 - 1054 | IPR006068 |
| ptm | P-type ATPase, phosphorylation site | 486 - 492 | IPR018303 |
| domain | Calcium-transporting P-type ATPase, N-terminal autoinhibitory domain | 32 - 73 | IPR024750 |
| domain | P-type ATPase, haloacid dehalogenase domain | 466 - 844 | IPR044492 |
Functions
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| 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. |
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. |
6 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. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| 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 |
| 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 | RCTLEAGAMA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FHYIIEKGVC | YLVLCEAAFP | KKLAFAYLED | LQSEFDEQHG | KKVPTVSRPY | SFIEFDTYIQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KTKKLYIDSR | ARRNLGSINT | ELQDVQRIMV | ANIEEVLQRG | EALSALDSKA | NNLSSLSKKY |
| 190 | 200 | 210 | |||
| RQDAKYLNMR | STYAKLAAVA | VFFIMLIVYV | RFWWL |