SNARE motif of syntaxin 17; Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and interacts with SNAP29 (Qb/Qc) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials, including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. 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 complexes mediate 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568927284 161 IPQDQNAAESWETLEADLIELSHLVTDMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQK 222
Cdd:cd15846    1 LPQRQACLESWETLQQDLEDLHGLFTDFHQLVHDQGEQVDTIEDNVEEALENVQEGTKNLRK 62

SNARE motif of syntaxin 17; Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and interacts with SNAP29 (Qb/Qc) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials, including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. 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 complexes mediate 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568927284 161 IPQDQNAAESWETLEADLIELSHLVTDMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQK 222
Cdd:cd15846    1 LPQRQACLESWETLQQDLEDLHGLFTDFHQLVHDQGEQVDTIEDNVEEALENVQEGTKNLRK 62

t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927284 111 ESVEELKKQVndeELLQPSLTRSTTVDGVLHTGEAEAASQSLTQIYALPE----IPQDQNAAESWETLEADLIELSHLVT 186
Cdd:COG5074  126 EEKEQARRQY---IIAQPEATEDEVEAAINDVNGQQVFSQALLNANRRGEaktaLAEVQARHQEIKKIEKTMAELTQLFN 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568927284 187 DMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQKAAKYKLAA 230
Cdd:COG5074  203 DMEELVIEQQENVDVIDKNVEDAQENVEQGVGHTDKAVKSARAA 246

SNARE motif of syntaxin 17; Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and interacts with SNAP29 (Qb/Qc) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials, including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. 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 complexes mediate 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568927284 161 IPQDQNAAESWETLEADLIELSHLVTDMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQK 222
Cdd:cd15846    1 LPQRQACLESWETLQQDLEDLHGLFTDFHQLVHDQGEQVDTIEDNVEEALENVQEGTKNLRK 62

SNARE motif of syntaxin 1 and related proteins; 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. This subgroup of the Qa SNAREs includes syntaxin 1, syntaxin 11, syntaxin 19, syntaxin 2, syntaxin 3, syntaxin 4 and related proteins.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568927284 173 TLEADLIELSHLVTDMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQK 222
Cdd:cd15848   14 KLEKSIRELHQMFLDMAVLVESQGELIDNIEYNVEKAKDYVEKGNEELKK 63

SNARE motif of syntaxin 12; Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex with SNAP25 (Qb/Qc) or SNAP29 (Qb/Qc) and VAMP2 or VAMP3 (R-SNARE) and plays a role in plasma membrane to early endosome transport. Syntaxin 12 is a member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate 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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568927284 174 LEADLIELSHLVTDMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQKAAKYK 227
Cdd:cd15876   11 LEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQ 64

SNARE motif of syntaxin 7; Syntaxin 7 forms a complex with syntaxin 8 (Qc), Vti1b (Qb) and either VAMP7 or VAMP8 (R-SNARE) and is involved in the transport from early endosomes to the lysosome. Syntaxin 7 is member of the Qa subgroup of 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 complexes mediate 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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568927284 168 AESWETLEADLIELSHLVTDMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQKA 223
Cdd:cd15875    5 ERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA 60

t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568927284 111 ESVEELKKQVndeELLQPSLTRSTTVDGVLHTGEAEAASQSLTQIYALPE----IPQDQNAAESWETLEADLIELSHLVT 186
Cdd:COG5074  126 EEKEQARRQY---IIAQPEATEDEVEAAINDVNGQQVFSQALLNANRRGEaktaLAEVQARHQEIKKIEKTMAELTQLFN 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568927284 187 DMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQKAAKYKLAA 230
Cdd:COG5074  203 DMEELVIEQQENVDVIDKNVEDAQENVEQGVGHTDKAVKSARAA 246

SNARE motif of syntaxin 5; Syntaxin 5 (Syn5) regulates the transport from the ER to the Golgi, as well as the early/recycling endosomes to the trans-Golgi network and participates in the assembly of transitional ER and the Golgi, lipid droplet fusion, and cytokinesis. Syn5 exists in 2 isoforms, long (42 kDa) and short (35 kDa). The short form is localized in the Golgi complex, whereas the long form is additionally found in the endoplasmic reticulum (ER). The syntaxin-5 SNARE complexes, which also contain Bet1 (Qc) and either GS27 (Qb) and Sec22B (R-SNARE) or GS28 (Qb) and Ykt6 (R-SNARE), regulate the early secretory pathway of eukaryotic cells at the level of endoplasmic reticulum (ER) to Golgi transport. The syntaxin-5 SNARE complex, which also contains GS15 (Qc), GS28 (Qb) and Ykt6 (R-SNAREs) is involved in the transport from the trans-Golgi network to the cis-Golgi. Syn5 is member of the Qa subgroup of 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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568927284 165 QNAAESWETLEADLIELSHLVTDMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQK 222
Cdd:cd15844    2 QSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDENVEDALANVEAAHSELLK 59

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568927284 169 ESWETLEADLIELSHLVTDMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQK 222
Cdd:cd00193    1 ESLEQLEASIGELKDIGRDMAMELEEQGEQLDRIEERAESTQARVSRAEKSLAK 54

SNARE motif of syntaxin 3; Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 (R-SNARE) and SNAP-23 (Qb/c) in mast cells. Mutations have been implicated in human microvillus inclusion disease (MVID), a disorder of the differentiation of intestinal epithelium. Syntaxin 3 is a member of the Qa subgroup of 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 complexes mediate 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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568927284 174 LEADLIELSHLVTDMSLLVSSQQEKIDSIADHVNSAAVNVEEGTKNLQKAAKYK 227
Cdd:cd15881   15 LESSIKELHDMFVDIAMLVENQGEMLDNIELNVMKTVDHVEKARDETKKAVKYQ 68