vesicle transport through interaction with t-SNAREs homolog 1A isoform X12 [Mus musculus]
Protein Classification
V-SNARE and SNARE domain-containing protein( domain architecture ID 10523371)
V-SNARE and SNARE domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| V-SNARE | pfam05008 | Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ... |
12-90 | 8.50e-25 | ||
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins. : Pssm-ID: 461516 Cd Length: 79 Bit Score: 91.13 E-value: 8.50e-25
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| SNARE super family | cl22856 | SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ... |
122-142 | 6.33e-06 | ||
SNARE motif; 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-, 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. The actual alignment was detected with superfamily member cd15891: Pssm-ID: 473982 Cd Length: 62 Bit Score: 41.90 E-value: 6.33e-06
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| Name | Accession | Description | Interval | E-value | ||
| V-SNARE | pfam05008 | Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ... |
12-90 | 8.50e-25 | ||
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins. Pssm-ID: 461516 Cd Length: 79 Bit Score: 91.13 E-value: 8.50e-25
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| SNARE_Vti1a | cd15891 | SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ... |
122-142 | 6.33e-06 | ||
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). SNARE 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: 277244 Cd Length: 62 Bit Score: 41.90 E-value: 6.33e-06
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| Name | Accession | Description | Interval | E-value | ||
| V-SNARE | pfam05008 | Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ... |
12-90 | 8.50e-25 | ||
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins. Pssm-ID: 461516 Cd Length: 79 Bit Score: 91.13 E-value: 8.50e-25
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| SNARE_Vti1a | cd15891 | SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ... |
122-142 | 6.33e-06 | ||
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). SNARE 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: 277244 Cd Length: 62 Bit Score: 41.90 E-value: 6.33e-06
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