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Conserved domains on  [gi|8394376|ref|NP_058626|]
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syntaxin-18 isoform 1 [Homo sapiens]

Protein Classification

SNARE domain-containing protein; syntaxin 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; syntaxin family protein similar to syntaxin 5 (Syn5) that 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

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 ...
 246-304 5.56e-22

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: 87.35  E-value: 5.56e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 8394376  246 MNSLFDEVRQIEGRVVEISRLQEIFTEKVLQQEAEIDSIHQLVVGATENIKEGNEDIRE 304
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 7.40e-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: 7.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8394376      4 DITLLFRASVKTVKTRNKALGVAVGGGVDgSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKDYINAYSHTms 83
Cdd:pfam10496   2 DLTPLFKASVKTVRGPASASSKDEIPKAK-KRKSPRLKKSKPKDEFLKEAYEILKHITELRKFLLSIRKDYLSLSSHL-- 78

                          90
                  ....*....|...
gi 8394376     84 eygrMTDTERDQI 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 ...
 246-304 5.56e-22

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: 87.35  E-value: 5.56e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 8394376  246 MNSLFDEVRQIEGRVVEISRLQEIFTEKVLQQEAEIDSIHQLVVGATENIKEGNEDIRE 304
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 7.40e-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: 7.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8394376      4 DITLLFRASVKTVKTRNKALGVAVGGGVDgSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKDYINAYSHTms 83
Cdd:pfam10496   2 DLTPLFKASVKTVRGPASASSKDEIPKAK-KRKSPRLKKSKPKDEFLKEAYEILKHITELRKFLLSIRKDYLSLSSHL-- 78

                          90
                  ....*....|...
gi 8394376     84 eygrMTDTERDQI 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 ...
 246-304 5.56e-22

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: 87.35  E-value: 5.56e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 8394376  246 MNSLFDEVRQIEGRVVEISRLQEIFTEKVLQQEAEIDSIHQLVVGATENIKEGNEDIRE 304
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 7.40e-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: 7.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8394376      4 DITLLFRASVKTVKTRNKALGVAVGGGVDgSRDELFRRSPRPKGDFSSRAREVISHIGKLRDFLLEHRKDYINAYSHTms 83
Cdd:pfam10496   2 DLTPLFKASVKTVRGPASASSKDEIPKAK-KRKSPRLKKSKPKDEFLKEAYEILKHITELRKFLLSIRKDYLSLSSHL-- 78

                          90
                  ....*....|...
gi 8394376     84 eygrMTDTERDQI 96
Cdd:pfam10496  79 ----MTDQERDDI 87
SNARE_Sso1 cd15849
SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with ...
 251-306 2.14e-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: 39.05  E-value: 2.14e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 8394376  251 DEVRQIEGRVVEISRLQEIFTEKVLQQEAEIDSIHQLVVGATENIKEGNEDIREAI 306
Cdd:cd15849   9 NEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIEQNAEEVETDLEKGNVHLEKAV 64
 
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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