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 332656907   38 EFFGYVESVKEDMKAVDEIHKRLQDANEESKTVHDSKAVKKLRARMDSSVTEVLKRVKMIKTKLVALEKSNAAQRKVAGC 117
Cdd:pfam00804   1 DFFKEVQEIKEEIEKIRLLVKKLQKQNEESKLLTSARRMSVIKRRMNSIARDIKKRAESIKRRLEALDKSNAENEKKPGC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332656907  118 GPGSSADRTRTSVVSGLGKKLKDMMDDFQRLRTKMATEYKETVERRYFTVTGQKADEETVEKLISSGeSERFLQKAIQEQ 197
Cdd:pfam00804  81 GPGSAVDRIRRSQTAALRKKLKEVMAEYNELRERIREEYKEVIQRQYETVTGKEVSEEEIEEMIETG-SESVFQKAILEQ 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 332656907  198 GRGQVMDTLSEIQERHDTVKEIERSLLELHQVFLDMAALVEAQG 241
Cdd:pfam00804 160 GRGQARSALSEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203

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 332656907   38 EFFGYVESVKEDMKAVDEIHKRLQDANEESKTVHDSKAVKKLRARMDSSVTEVLKRVKMIKTKLVALEKSNAAQRKVAGC 117
Cdd:pfam00804   1 DFFKEVQEIKEEIEKIRLLVKKLQKQNEESKLLTSARRMSVIKRRMNSIARDIKKRAESIKRRLEALDKSNAENEKKPGC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332656907  118 GPGSSADRTRTSVVSGLGKKLKDMMDDFQRLRTKMATEYKETVERRYFTVTGQKADEETVEKLISSGeSERFLQKAIQEQ 197
Cdd:pfam00804  81 GPGSAVDRIRRSQTAALRKKLKEVMAEYNELRERIREEYKEVIQRQYETVTGKEVSEEEIEEMIETG-SESVFQKAILEQ 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 332656907  198 GRGQVMDTLSEIQERHDTVKEIERSLLELHQVFLDMAALVEAQG 241
Cdd:pfam00804 160 GRGQARSALSEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203

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 332656907    34 GNLDEFFGYVESVKEDMKAVDEIHKRLQDANEESKTVHDskAVKKLRARMDSSVTEVLKRVKMIKTKLVALEKSNAAQRK 113
Cdd:smart00503   1 SNLDEFFEKVEEIRANIQKISQNVAELQKLHEELLTPPD--ADKELREKLERLIDDIKRLAKEIRAKLKELEKENLENRA 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 332656907   114 VagcgpGSSADRTRTSVVSGLGKKLKDMMDDFQRLRTKMATEYK 157
Cdd:smart00503  79 S-----GSASDRTRKAQTEKLRKKFKEVMNEFQRLQRKYREREK 117

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        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332656907 209 IQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVSKASSFVMRGTDQLHGAKVLQRNN 275
Cdd:cd15876    1 IKERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQKKS 67

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 332656907   38 EFFGYVESVKEDMKAVDEIHKRLQDANEESKTVHDSKAVKKLRARMDSSVTEVLKRVKMIKTKLVALEKSNAAQRKVAGC 117
Cdd:pfam00804   1 DFFKEVQEIKEEIEKIRLLVKKLQKQNEESKLLTSARRMSVIKRRMNSIARDIKKRAESIKRRLEALDKSNAENEKKPGC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332656907  118 GPGSSADRTRTSVVSGLGKKLKDMMDDFQRLRTKMATEYKETVERRYFTVTGQKADEETVEKLISSGeSERFLQKAIQEQ 197
Cdd:pfam00804  81 GPGSAVDRIRRSQTAALRKKLKEVMAEYNELRERIREEYKEVIQRQYETVTGKEVSEEEIEEMIETG-SESVFQKAILEQ 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 332656907  198 GRGQVMDTLSEIQERHDTVKEIERSLLELHQVFLDMAALVEAQG 241
Cdd:pfam00804 160 GRGQARSALSEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203

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 332656907 205 TLSEIQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVSKASSFVMRGTDQL 265
Cdd:cd15848    1 ALADIEERHQDILKLEKSIRELHQMFLDMAVLVESQGELIDNIEYNVEKAKDYVEKGNEEL 61

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 332656907 209 IQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVSKASSFVMRGTDQL 265
Cdd:cd15840    1 IEEREEEIREIESSIGEVNEIFKDLATLVTEQGEQIDNIENNIEEAAANTEEANKEL 57

SNARE motif of syntaxin 2; Syntaxin 2 (STX2), also known as epimorphin (EPM or EPIM), may interact with SNAP-23 (Qb/c) and genetic varioations are associated with type 1 von Willebrand disease (VWD). Syntaxin 2 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 332656907 206 LSEIQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVSKASSFV 258
Cdd:cd15882    2 LNEIESRHKDIMKLESSIRELHDMFVDMAMLVETQGEMINNIEKNVHNAVEYV 54

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 332656907   204 DTLSEIQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVSKASSFVMRGTDQLHGA 268
Cdd:smart00397   2 QALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66

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 332656907 206 LSEIQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVSKASSFVMRGTDQLHGAK 269
Cdd:cd15849    1 LGEVQARHNEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIEQNAEEVETDLEKGNVHLEKAV 64

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        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332656907 209 IQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVSKASSFVMRGTDQLHGAKVLQRNN 275
Cdd:cd15876    1 IKERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQKKS 67

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 332656907 209 IQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVSKASSFVMRGTDQLHGA 268
Cdd:cd15875    1 LEERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA 60

SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are believed to be mediated by a conserved fusion machinery, the SNARE [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors] machinery. The SNARE domain is thought to act as a protein-protein interaction module in the assembly of a SNARE protein complex.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 332656907  242 NMLNDIESNVSKASSFVMRGTDQLHGAKVLQRNNRKWACIA 282
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRKLKCII 41

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332656907 173 DEETVEKLISSGESERFLQKaiQEQGRGQVMDTLSEIQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVS 252
Cdd:COG5325  156 EEEEDEESLSSLGSQQTLQQ--QGLSNEELEYQQILITERDEEIKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFNIE 233

                         90       100
                 ....*....|....*....|....*.
gi 332656907 253 KASSFVMRGTDQLHGAKVLQRNNRKW 278
Cdd:COG5325  234 NTSDNLKNANKELEKAPAHQRRTKKC 259

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        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332656907 209 IQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVSKASSFVMRGTDQLhgAKVLQR--NNR 276
Cdd:cd15844    1 LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDENVEDALANVEAAHSEL--LKYYRSisSNR 68

SNARE motif of syntaxin 19; Syntaxin 19 has been shown to have the potential to form SNARE complexes with SNAP-23, 25 and 29 (Qb/Qc) and VAMP3 and VAMP8 (R-SNARE), indicating a role in post-Golgi trafficking or plasma membrane fusion. Syntaxin 19 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 332656907 206 LSEIQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVSKASSFV 258
Cdd:cd15879    2 LSEIEQRHKELVSLENQIKDLKDLFIQISLLVEEQGEMINNIEISVNNTQEYV 54