Golgi SNAP receptor complex member 1 isoform X2 [Macaca mulatta]
Protein Classification
SNARE domain-containing protein; synaptobrevin family protein( domain architecture ID 10205211)
SNARE domain-containing protein such as SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which interact to form a SNARE complex that mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation| synaptobrevin family protein with similarity to the C-terminal domain of vesicle-associated membrane proteins (VAMPs) which are involved in the targeting and/or fusion of transport vesicles to their target membrane
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| SNARE_GS28 | cd15864 | SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms ... |
160-215 | 1.61e-24 | ||
SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms complexes with syntaxin-5 (Qa), Ykt6 (R-SNARE) and either Bet1 (Qc) or GS15 (Qc). These complexes regulate the early secretory pathway of eukaryotic cells at the level of the transport from the ER-Golgi intermediate compartment (ERGIC) to the cis-Golgi and transport from the trans-Golgi network to the cis-Golgi, respectively. GS28 is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. : Pssm-ID: 277217 Cd Length: 66 Bit Score: 92.50 E-value: 1.61e-24
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| SNARE_GS28 | cd15864 | SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms ... |
160-215 | 1.61e-24 | ||
SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms complexes with syntaxin-5 (Qa), Ykt6 (R-SNARE) and either Bet1 (Qc) or GS15 (Qc). These complexes regulate the early secretory pathway of eukaryotic cells at the level of the transport from the ER-Golgi intermediate compartment (ERGIC) to the cis-Golgi and transport from the trans-Golgi network to the cis-Golgi, respectively. GS28 is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Pssm-ID: 277217 Cd Length: 66 Bit Score: 92.50 E-value: 1.61e-24
|
||||||
| V-SNARE_C | pfam12352 | Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ... |
161-216 | 1.59e-10 | ||
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins interactions in the C-terminal half of the SNARE helix are critical to the driving of membrane fusion; whereas interactions in the N-terminal half of the SNARE domain are important for promoting priming or docking of the vesicle pfam05008. Pssm-ID: 289148 Cd Length: 66 Bit Score: 55.31 E-value: 1.59e-10
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| SNARE_GS28 | cd15864 | SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms ... |
160-215 | 1.61e-24 | ||
SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms complexes with syntaxin-5 (Qa), Ykt6 (R-SNARE) and either Bet1 (Qc) or GS15 (Qc). These complexes regulate the early secretory pathway of eukaryotic cells at the level of the transport from the ER-Golgi intermediate compartment (ERGIC) to the cis-Golgi and transport from the trans-Golgi network to the cis-Golgi, respectively. GS28 is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Pssm-ID: 277217 Cd Length: 66 Bit Score: 92.50 E-value: 1.61e-24
|
||||||
| V-SNARE_C | pfam12352 | Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ... |
161-216 | 1.59e-10 | ||
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins interactions in the C-terminal half of the SNARE helix are critical to the driving of membrane fusion; whereas interactions in the N-terminal half of the SNARE domain are important for promoting priming or docking of the vesicle pfam05008. Pssm-ID: 289148 Cd Length: 66 Bit Score: 55.31 E-value: 1.59e-10
|
||||||
| Blast search parameters | ||||
|
