Golgi SNAP receptor complex member 2 isoform X1 [Mus musculus]
Protein Classification
golgi SNAP receptor complex member 2 family protein( domain architecture ID 10205203)
golgi SNAP receptor complex member 2 (GOSR2) family protein similar to human GOSR2 which is involved in ER-to-Golgi trafficking; belongs to the Qb-SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family of vesicle docking proteins
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| SNARE_GS27 | cd15863 | SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or ... |
102-167 | 1.10e-28 | ||
SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or GOSR2) is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. GS27 forms a complex together with Bet1 (Qc), syntaxin-5 (Qa) and Sec22B (R-SNARE). This complex regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of 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. : Pssm-ID: 277216 Cd Length: 66 Bit Score: 101.45 E-value: 1.10e-28
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| Name | Accession | Description | Interval | E-value | ||
| SNARE_GS27 | cd15863 | SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or ... |
102-167 | 1.10e-28 | ||
SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or GOSR2) is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. GS27 forms a complex together with Bet1 (Qc), syntaxin-5 (Qa) and Sec22B (R-SNARE). This complex regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of 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. Pssm-ID: 277216 Cd Length: 66 Bit Score: 101.45 E-value: 1.10e-28
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| V-SNARE_C | pfam12352 | Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ... |
103-168 | 1.92e-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: 54.54 E-value: 1.92e-10
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| Name | Accession | Description | Interval | E-value | ||
| SNARE_GS27 | cd15863 | SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or ... |
102-167 | 1.10e-28 | ||
SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or GOSR2) is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. GS27 forms a complex together with Bet1 (Qc), syntaxin-5 (Qa) and Sec22B (R-SNARE). This complex regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of 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. Pssm-ID: 277216 Cd Length: 66 Bit Score: 101.45 E-value: 1.10e-28
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| SNARE_Qb | cd15842 | SNARE motif, subgroup Qb; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ... |
102-163 | 4.84e-12 | ||
SNARE motif, subgroup Qb; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which 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. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27. Pssm-ID: 277195 Cd Length: 62 Bit Score: 58.66 E-value: 4.84e-12
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| V-SNARE_C | pfam12352 | Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ... |
103-168 | 1.92e-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: 54.54 E-value: 1.92e-10
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| Blast search parameters | ||||
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