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        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139979 168 IHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRA 227
Cdd:cd15875   1 LEERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA 60

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        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139979 168 IHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRA 227
Cdd:cd15875   1 LEERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA 60

Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139979  13 QLAQRISSNIQKITQCSVEIQRTLNQLGTPQD-SPELRQLLQQKQQYTNQLAKETDKYIKEFGSLPTTP------SEQRQ 85
Cdd:cd00179   6 EEVEEIRGNIDKISEDVEELQKLHSQLLTAPDaDPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNealngsSVDRI 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20139979  86 RKIQKDRLVAEFTTSLTNFQKAQRQAAEREKEFVARVRASSRVSGGFPEDSSKEKNlVSWESQTQ 150
Cdd:cd00179  86 RKTQHSGLSKKFVEVMTEFNKAQRKYRERYKERIQRQLEITGGEATDEELEDMLES-GNSEIFTS 149

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139979     13 QLAQRISSNIQKITQCSVEIQRTLNQLGTPQDS-PELRQLLQQKQQYTNQLAKETDKYIKEFGSLPTT-----PSEQRQR 86
Cdd:smart00503   8 EKVEEIRANIQKISQNVAELQKLHEELLTPPDAdKELREKLERLIDDIKRLAKEIRAKLKELEKENLEnrasgSASDRTR 87

                           90       100       110
                   ....*....|....*....|....*....|
gi 20139979     87 KIQKDRLVAEFTTSLTNFQKAQRQAAEREK 116
Cdd:smart00503  88 KAQTEKLRKKFKEVMNEFQRLQRKYREREK 117

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20139979    162 EDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRA 227
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66

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        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139979 168 IHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRA 227
Cdd:cd15875   1 LEERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA 60

SNARE motif of syntaxin 7, 12 and related sequences; 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 7, syntaxin 12, TSNARE1 and related proteins.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139979 168 IHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRA 227
Cdd:cd15847   1 LLEREERIRQIESDILDVNQIFKDLATLVHEQGETIDSIEANIESAYVNVESGNSQLAKA 60

Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139979  13 QLAQRISSNIQKITQCSVEIQRTLNQLGTPQD-SPELRQLLQQKQQYTNQLAKETDKYIKEFGSLPTTP------SEQRQ 85
Cdd:cd00179   6 EEVEEIRGNIDKISEDVEELQKLHSQLLTAPDaDPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNealngsSVDRI 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20139979  86 RKIQKDRLVAEFTTSLTNFQKAQRQAAEREKEFVARVRASSRVSGGFPEDSSKEKNlVSWESQTQ 150
Cdd:cd00179  86 RKTQHSGLSKKFVEVMTEFNKAQRKYRERYKERIQRQLEITGGEATDEELEDMLES-GNSEIFTS 149

SNARE motif, subgroup Qa; 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 Qa SNAREs are syntaxin 18, syntaxin 5, syntaxin 16, and syntaxin 1.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20139979 168 IHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSR 226
Cdd:cd15840   1 IEEREEEIREIESSIGEVNEIFKDLATLVTEQGEQIDNIENNIEEAAANTEEANKELRK 59

SNARE motif of TSNARE1; TSNARE1 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. Its function is unknown, but polymorphisms in human TSNARE1 have been associated with schizophrenia susceptibility. 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. TSNARE1 is part of a subgroup of the Qa SNAREs that also includes syntaxin 7, syntaxin 12 and related proteins.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20139979 165 LRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRAA 228
Cdd:cd15877   1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQQLAKAS 64

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        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139979 165 LRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQL 224
Cdd:cd15848   2 LADIEERHQDILKLEKSIRELHQMFLDMAVLVESQGELIDNIEYNVEKAKDYVEKGNEEL 61

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20139979    162 EDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRA 227
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66

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
                ....*....|....*....|....*....|....*....|....*....
gi 20139979 178 LEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSR 226
Cdd:cd15846  14 LQQDLEDLHGLFTDFHQLVHDQGEQVDTIEDNVEEALENVQEGTKNLRK 62

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139979 165 LRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRAADYQRKSRKTLCIIIFI 244
Cdd:COG5074 177 LAEVQARHQEIKKIEKTMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQENVEQGVGHTDKAVKSARAARKKKIRCYGI 256

                        90
                ....*....|....
gi 20139979 245 LVVRIVIICLIVWG 258
Cdd:COG5074 257 CFIIIIVIVVVVFK 270

SNARE motif of syntaxin 1; Syntaxin-1 belongs to the Qa subgroup of SNAREs and interacts with SNAP-25 (Qb/Qc) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in exocytosis of synaptic vesicles. 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        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20139979 165 LRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRAADYQ 231
Cdd:cd15880   2 LSEIEARHNDIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQ 68

SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with synaptobrevin homolog Snc1p (R-SNARE) and the SNAP-25 homolog Sec9p (Qb/c) which is involved in exocytosis. Sso1 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        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20139979 165 LRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRA 227
Cdd:cd15849   1 LGEVQARHNEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIEQNAEEVETDLEKGNVHLEKA 63

SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, VAMP2 and VAMP7 which plays a role in exocytosis of secetory granule. Syntaxin 4 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        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20139979 165 LRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLS 225
Cdd:cd15883   2 LNEIEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNILSSADYVEKAQEHVK 62

Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three main regions - a C-terminal transmembrane region, a central SNARE domain which is characteriztic of and conserved in all syntaxins (pfam05739), and an N-terminal domain that is featured in this entry. This domain varies between syntaxin isoforms; in syntaxin 1A it is found as three alpha-helices with a left-handed twist. It may fold back on the SNARE domain to allow the molecule to adopt a 'closed' configuration that prevents formation of the core fusion complex - it thus has an auto-inhibitory role. The function of syntaxins is determined by their localization. They are involved in neuronal exocytosis, ER-Golgi transport and Golgi-endosome transport, for example. They also interact with other proteins as well as those involved in SNARE complexes. These include vesicle coat proteins, Rab GTPases, and tethering factors.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20139979    84 RQRKIQKDRLVAEFTTSLTNFQKAQRQAAEREKEFVARvRASsrVSGGFPEDSSKEKNLVSWESQT--QPQVQVQDEEIT 161
Cdd:pfam00804  88 RIRRSQTAALRKKLKEVMAEYNELRERIREEYKEVIQR-QYE--TVTGKEVSEEEIEEMIETGSESvfQKAILEQGRGQA 164

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 20139979   162 EDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQG 200
Cdd:pfam00804 165 RSALSEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203