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Conserved domains on  [gi|77736535|ref|NP_081235|]
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syntaxin-18 isoform 1 [Mus musculus]

Protein Classification

SNARE domain-containing protein; synaptobrevin family protein( domain architecture ID 10564682)

SNARE domain-containing protein such as SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which interact to form a SNARE complex that mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation| synaptobrevin family protein with similarity to the C-terminal domain of vesicle-associated membrane proteins (VAMPs) which are involved in the targeting and/or fusion of transport vesicles to their target membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNARE_syntaxin18 cd15850
SNARE motif, subgroup Qa; Syntaxin18 (also known as Ufe1p) is involved in retrograde transport ...
 245-303 4.86e-23

SNARE motif, subgroup Qa; Syntaxin18 (also known as Ufe1p) is involved in retrograde transport of CopI coatomer coated vesicles from the Golgi to the ER. It forms a complex with USE1 (SLT1, Qc), Bnip1 (Sec20p, Qb) and Sec22b (R-SNARE). Syntaxin18 is a member of the Qa subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family. 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). Qc-, as well as Qa- and Qb-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.


:

Pssm-ID: 277203  Cd Length: 59  Bit Score: 90.43  E-value: 4.86e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 77736535 245 MNSLFDEVRQIEGKVVEISRLQEIFTEKVLQQETEIDSIHQLVVGATENIKEGNEDIRE 303
Cdd:cd15850   1 KNSQLDKVRQIEKTVVEIASLQEEFAEKLLVQEQNIDSLLDLVVDTTENVKKGNEELRK 59
Syntaxin-18_N pfam10496
SNARE-complex protein Syntaxin-18 N-terminus; This is the conserved N-terminal of Syntaxin-18. ...
 4-96 9.25e-22

SNARE-complex protein Syntaxin-18 N-terminus; This is the conserved N-terminal of Syntaxin-18. Syntaxin-18 is found in the SNARE complex of the endoplasmic reticulum and functions in the trafficking between the ER intermediate compartment and the cis-Golgi vesicle. In particular, the N-terminal region is important for the formation of ER aggregates. More specifically, syntaxin-18 is involved in endoplasmic reticulum-mediated phagocytosis, presumably by regulating the specific and direct fusion of the ER with the plasma or phagosomal membranes.


:

Pssm-ID: 463116  Cd Length: 87  Bit Score: 87.86  E-value: 9.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736535     4 DITLLFRASVKTVKTRNKALGVAVGGGADgSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKEYINAYSHTms 83
Cdd:pfam10496   2 DLTPLFKASVKTVRGPASASSKDEIPKAK-KRKSPRLKKSKPKDEFLKEAYEILKHITELRKFLLSIRKDYLSLSSHL-- 78

                          90
                  ....*....|...
gi 77736535    84 dygrMTDTERDQI 96
Cdd:pfam10496  79 ----MTDQERDDI 87
 
Name Accession Description Interval E-value
SNARE_syntaxin18 cd15850
SNARE motif, subgroup Qa; Syntaxin18 (also known as Ufe1p) is involved in retrograde transport ...
 245-303 4.86e-23

SNARE motif, subgroup Qa; Syntaxin18 (also known as Ufe1p) is involved in retrograde transport of CopI coatomer coated vesicles from the Golgi to the ER. It forms a complex with USE1 (SLT1, Qc), Bnip1 (Sec20p, Qb) and Sec22b (R-SNARE). Syntaxin18 is a member of the Qa subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family. 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). Qc-, as well as Qa- and Qb-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.


Pssm-ID: 277203  Cd Length: 59  Bit Score: 90.43  E-value: 4.86e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 77736535 245 MNSLFDEVRQIEGKVVEISRLQEIFTEKVLQQETEIDSIHQLVVGATENIKEGNEDIRE 303
Cdd:cd15850   1 KNSQLDKVRQIEKTVVEIASLQEEFAEKLLVQEQNIDSLLDLVVDTTENVKKGNEELRK 59
Syntaxin-18_N pfam10496
SNARE-complex protein Syntaxin-18 N-terminus; This is the conserved N-terminal of Syntaxin-18. ...
 4-96 9.25e-22

SNARE-complex protein Syntaxin-18 N-terminus; This is the conserved N-terminal of Syntaxin-18. Syntaxin-18 is found in the SNARE complex of the endoplasmic reticulum and functions in the trafficking between the ER intermediate compartment and the cis-Golgi vesicle. In particular, the N-terminal region is important for the formation of ER aggregates. More specifically, syntaxin-18 is involved in endoplasmic reticulum-mediated phagocytosis, presumably by regulating the specific and direct fusion of the ER with the plasma or phagosomal membranes.


Pssm-ID: 463116  Cd Length: 87  Bit Score: 87.86  E-value: 9.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736535     4 DITLLFRASVKTVKTRNKALGVAVGGGADgSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKEYINAYSHTms 83
Cdd:pfam10496   2 DLTPLFKASVKTVRGPASASSKDEIPKAK-KRKSPRLKKSKPKDEFLKEAYEILKHITELRKFLLSIRKDYLSLSSHL-- 78

                          90
                  ....*....|...
gi 77736535    84 dygrMTDTERDQI 96
Cdd:pfam10496  79 ----MTDQERDDI 87
 
Name Accession Description Interval E-value
SNARE_syntaxin18 cd15850
SNARE motif, subgroup Qa; Syntaxin18 (also known as Ufe1p) is involved in retrograde transport ...
 245-303 4.86e-23

SNARE motif, subgroup Qa; Syntaxin18 (also known as Ufe1p) is involved in retrograde transport of CopI coatomer coated vesicles from the Golgi to the ER. It forms a complex with USE1 (SLT1, Qc), Bnip1 (Sec20p, Qb) and Sec22b (R-SNARE). Syntaxin18 is a member of the Qa subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family. 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). Qc-, as well as Qa- and Qb-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.


Pssm-ID: 277203  Cd Length: 59  Bit Score: 90.43  E-value: 4.86e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 77736535 245 MNSLFDEVRQIEGKVVEISRLQEIFTEKVLQQETEIDSIHQLVVGATENIKEGNEDIRE 303
Cdd:cd15850   1 KNSQLDKVRQIEKTVVEIASLQEEFAEKLLVQEQNIDSLLDLVVDTTENVKKGNEELRK 59
Syntaxin-18_N pfam10496
SNARE-complex protein Syntaxin-18 N-terminus; This is the conserved N-terminal of Syntaxin-18. ...
 4-96 9.25e-22

SNARE-complex protein Syntaxin-18 N-terminus; This is the conserved N-terminal of Syntaxin-18. Syntaxin-18 is found in the SNARE complex of the endoplasmic reticulum and functions in the trafficking between the ER intermediate compartment and the cis-Golgi vesicle. In particular, the N-terminal region is important for the formation of ER aggregates. More specifically, syntaxin-18 is involved in endoplasmic reticulum-mediated phagocytosis, presumably by regulating the specific and direct fusion of the ER with the plasma or phagosomal membranes.


Pssm-ID: 463116  Cd Length: 87  Bit Score: 87.86  E-value: 9.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736535     4 DITLLFRASVKTVKTRNKALGVAVGGGADgSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKEYINAYSHTms 83
Cdd:pfam10496   2 DLTPLFKASVKTVRGPASASSKDEIPKAK-KRKSPRLKKSKPKDEFLKEAYEILKHITELRKFLLSIRKDYLSLSSHL-- 78

                          90
                  ....*....|...
gi 77736535    84 dygrMTDTERDQI 96
Cdd:pfam10496  79 ----MTDQERDDI 87
SNARE_Sso1 cd15849
SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with ...
 250-305 7.96e-04

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: 37.12  E-value: 7.96e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 77736535 250 DEVRQIEGKVVEISRLQEIFTEKVLQQETEIDSIHQLVVGATENIKEGNEDIREAI 305
Cdd:cd15849   9 NEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIEQNAEEVETDLEKGNVHLEKAV 64
SNARE_syntaxin7_like cd15847
SNARE motif of syntaxin 7, 12 and related sequences; SNARE (soluble N-ethylmaleimide-sensitive ...
 250-304 1.47e-03

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.


Pssm-ID: 277200 [Multi-domain]  Cd Length: 60  Bit Score: 36.40  E-value: 1.47e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 77736535 250 DEVRQIEGKVVEISrlqEIFTE---KVLQQETEIDSIHQLVVGATENIKEGNEDIREA 304
Cdd:cd15847   6 ERIRQIESDILDVN---QIFKDlatLVHEQGETIDSIEANIESAYVNVESGNSQLAKA 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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