syntaxin-2 isoform X4 [Rattus norvegicus]
Protein Classification
SynN domain-containing protein( domain architecture ID 12010187)
SynN domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Syntaxin | pfam00804 | Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three ... |
33-227 | 9.87e-64 | ||||
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. : Pssm-ID: 459942 [Multi-domain] Cd Length: 203 Bit Score: 197.02 E-value: 9.87e-64
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| Name | Accession | Description | Interval | E-value | ||||
| Syntaxin | pfam00804 | Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three ... |
33-227 | 9.87e-64 | ||||
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. Pssm-ID: 459942 [Multi-domain] Cd Length: 203 Bit Score: 197.02 E-value: 9.87e-64
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| SynN | cd00179 | Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ... |
31-182 | 2.74e-57 | ||||
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 Pssm-ID: 238105 [Multi-domain] Cd Length: 151 Bit Score: 179.02 E-value: 2.74e-57
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| SynN | smart00503 | Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ... |
29-147 | 1.26e-31 | ||||
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p Pssm-ID: 214699 [Multi-domain] Cd Length: 117 Bit Score: 112.05 E-value: 1.26e-31
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| COG5074 | COG5074 | t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ... |
33-228 | 5.05e-13 | ||||
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 227406 [Multi-domain] Cd Length: 280 Bit Score: 66.83 E-value: 5.05e-13
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| Name | Accession | Description | Interval | E-value | ||||
| Syntaxin | pfam00804 | Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three ... |
33-227 | 9.87e-64 | ||||
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. Pssm-ID: 459942 [Multi-domain] Cd Length: 203 Bit Score: 197.02 E-value: 9.87e-64
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| SynN | cd00179 | Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ... |
31-182 | 2.74e-57 | ||||
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 Pssm-ID: 238105 [Multi-domain] Cd Length: 151 Bit Score: 179.02 E-value: 2.74e-57
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| SynN | smart00503 | Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ... |
29-147 | 1.26e-31 | ||||
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p Pssm-ID: 214699 [Multi-domain] Cd Length: 117 Bit Score: 112.05 E-value: 1.26e-31
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| SNARE_syntaxin2 | cd15882 | SNARE motif of syntaxin 2; Syntaxin 2 (STX2), also known as epimorphin (EPM or EPIM), may ... |
192-227 | 2.67e-17 | ||||
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. Pssm-ID: 277235 Cd Length: 69 Bit Score: 73.54 E-value: 2.67e-17
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| SNARE_syntaxin1-like | cd15848 | SNARE motif of syntaxin 1 and related proteins; SNARE (soluble N-ethylmaleimide-sensitive ... |
192-227 | 4.12e-17 | ||||
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. Pssm-ID: 277201 Cd Length: 63 Bit Score: 72.95 E-value: 4.12e-17
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| SNARE_syntaxin1 | cd15880 | SNARE motif of syntaxin 1; Syntaxin-1 belongs to the Qa subgroup of SNAREs and interacts with ... |
192-227 | 1.27e-13 | ||||
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. Pssm-ID: 277233 Cd Length: 69 Bit Score: 63.68 E-value: 1.27e-13
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| COG5074 | COG5074 | t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ... |
33-228 | 5.05e-13 | ||||
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 227406 [Multi-domain] Cd Length: 280 Bit Score: 66.83 E-value: 5.05e-13
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| SNARE_syntaxin3 | cd15881 | SNARE motif of syntaxin 3; Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 ... |
192-227 | 2.51e-12 | ||||
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. Pssm-ID: 277234 Cd Length: 69 Bit Score: 60.42 E-value: 2.51e-12
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| SNARE_syntaxin11 | cd15878 | SNARE motif of syntaxin 11; Syntaxin 11 (also known as STX11, FHL4, HLH4, HPLH4) is present on ... |
192-227 | 2.30e-10 | ||||
SNARE motif of syntaxin 11; Syntaxin 11 (also known as STX11, FHL4, HLH4, HPLH4) is present on endosomal membranes, including late endosomes and lysosomes in macrophages, and has been shown to bind Vti1b and regulate the availability of Vti1b to form other SNARE-complexes. Mutations in human STX11 has been linked to familial hemophagocytic lymphohistiocytosis type-4 (FHL-4), an autosomal recessive disorder of immune dysregulation. Syntaxin 11 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. Pssm-ID: 277231 Cd Length: 63 Bit Score: 54.85 E-value: 2.30e-10
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| SNARE_syntaxin4 | cd15883 | SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, ... |
192-227 | 3.17e-09 | ||||
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. Pssm-ID: 277236 Cd Length: 63 Bit Score: 51.87 E-value: 3.17e-09
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| SNARE_Sso1 | cd15849 | SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with ... |
193-227 | 5.59e-07 | ||||
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. Pssm-ID: 277202 Cd Length: 64 Bit Score: 45.60 E-value: 5.59e-07
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| t_SNARE | smart00397 | Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ... |
190-227 | 6.83e-05 | ||||
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". Pssm-ID: 197699 [Multi-domain] Cd Length: 66 Bit Score: 39.87 E-value: 6.83e-05
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| SNARE_Qa | cd15840 | SNARE motif, subgroup Qa; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ... |
196-227 | 2.22e-04 | ||||
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. Pssm-ID: 277193 [Multi-domain] Cd Length: 59 Bit Score: 38.26 E-value: 2.22e-04
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| SNARE_syntaxin19 | cd15879 | SNARE motif of syntaxin 19; Syntaxin 19 has been shown to have the potential to form SNARE ... |
193-227 | 2.68e-04 | ||||
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. Pssm-ID: 277232 Cd Length: 63 Bit Score: 38.28 E-value: 2.68e-04
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| COG5325 | COG5325 | t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
12-227 | 8.97e-03 | ||||
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 36.74 E-value: 8.97e-03
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