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Conserved domains on  [gi|34364694|emb|CAE45797|]
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hypothetical protein [Homo sapiens]

Protein Classification

complexin/synaphin family protein( domain architecture ID 10530757)

complexin/synaphin family protein regulates SNAP receptor function by competing with alpha-SNAP for binding to the core complex

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Synaphin pfam05835
Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. ...
 1-140 6.33e-38

Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. Synaphin/complexin is a cytosolic protein that preferentially binds to syntaxin within the SNARE complex. Synaphin promotes SNAREs to form precomplexes that oligomerise into higher order structures. A peptide from the central, syntaxin binding domain of synaphin competitively inhibits these two proteins from interacting and prevents SNARE complexes from oligomerising. It is thought that oligomerization of SNARE complexes into a higher order structure creates a SNARE scaffold for efficient, regulated fusion of synaptic vesicles. Synaphin promotes neuronal exocytosis by promoting interaction between the complementary syntaxin and synaptobrevin transmembrane regions that reside in opposing membranes prior to fusion.


:

Pssm-ID: 461755 [Multi-domain]  Cd Length: 142  Bit Score: 126.41  E-value: 6.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364694     1 MAFLMKSMISNQVKNL--GFGGGSEENKEEGGasdpaaaqgMTREEYEEYQKQMIEEKMERDAAFTQKKAERACLRVHLR 78
Cdd:pfam05835   1 MAFLAKQMVGNQLKNVkgGLGGKGGEEKEDAE---------MTREEEEEYQEALREEEEERKAKHRKMEAEREKMRQHIR 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34364694    79 EKYRLPKSEMDENQIQMA---------GDDVDLPEDLRKMVDEDQEEEEDKDSILGQIQNLQNMDLDTIKE 140
Cdd:pfam05835  72 DKYRLKKKEEDEAEIQAAmepstegrlGRDKKTPEELAKMVEEDEEEEEEKDSVLGKLQNTLNTDVDELKE 142
 
Name Accession Description Interval E-value
Synaphin pfam05835
Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. ...
 1-140 6.33e-38

Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. Synaphin/complexin is a cytosolic protein that preferentially binds to syntaxin within the SNARE complex. Synaphin promotes SNAREs to form precomplexes that oligomerise into higher order structures. A peptide from the central, syntaxin binding domain of synaphin competitively inhibits these two proteins from interacting and prevents SNARE complexes from oligomerising. It is thought that oligomerization of SNARE complexes into a higher order structure creates a SNARE scaffold for efficient, regulated fusion of synaptic vesicles. Synaphin promotes neuronal exocytosis by promoting interaction between the complementary syntaxin and synaptobrevin transmembrane regions that reside in opposing membranes prior to fusion.


Pssm-ID: 461755 [Multi-domain]  Cd Length: 142  Bit Score: 126.41  E-value: 6.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364694     1 MAFLMKSMISNQVKNL--GFGGGSEENKEEGGasdpaaaqgMTREEYEEYQKQMIEEKMERDAAFTQKKAERACLRVHLR 78
Cdd:pfam05835   1 MAFLAKQMVGNQLKNVkgGLGGKGGEEKEDAE---------MTREEEEEYQEALREEEEERKAKHRKMEAEREKMRQHIR 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34364694    79 EKYRLPKSEMDENQIQMA---------GDDVDLPEDLRKMVDEDQEEEEDKDSILGQIQNLQNMDLDTIKE 140
Cdd:pfam05835  72 DKYRLKKKEEDEAEIQAAmepstegrlGRDKKTPEELAKMVEEDEEEEEEKDSVLGKLQNTLNTDVDELKE 142
Complexin_NTD_CPLX_III_IV cd22809
N-terminal SNARE complex binding domain found in complexins III and IV; Complexins (CPXs) are ...
 43-86 4.45e-21

N-terminal SNARE complex binding domain found in complexins III and IV; Complexins (CPXs) are small, cytosolic proteins that bind to the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex to regulate synaptic vesicle exocytosis. Complexins III (CPX III) and IV (CPX IV) are the only CPX isoforms present in retinal ribbon synapses. They carry an extension with a functional CAAX-box farnesylation site that is absent in CPXs I and II. Their C-terminal farnesylation regulates their synaptic targeting and modulatory function in transmitter release. They may contribute to the unique release efficacy of retinal sensory neurons. CPXs III and IV can functionally replace CPXs I and II, which regulate a late step in the release process, most likely by stabilizing SNARE complexes and thus maintaining synaptic vesicles in a highly release competent state. This model corresponds to the N-terminal SNARE complex binding domain of CPXs III and IV.


Pssm-ID: 439283  Cd Length: 44  Bit Score: 80.38  E-value: 4.45e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 34364694  43 EEYEEYQKQMIEEKMERDAAFTQKKAERACLRVHLREKYRLPKS 86
Cdd:cd22809   1 EEEEEYQKQLEEEKKERDAAFAQKKAERAAMRAHLREKYRLPKN 44
 
Name Accession Description Interval E-value
Synaphin pfam05835
Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. ...
 1-140 6.33e-38

Synaphin protein; This family consists of several eukaryotic synaphin 1 and 2 proteins. Synaphin/complexin is a cytosolic protein that preferentially binds to syntaxin within the SNARE complex. Synaphin promotes SNAREs to form precomplexes that oligomerise into higher order structures. A peptide from the central, syntaxin binding domain of synaphin competitively inhibits these two proteins from interacting and prevents SNARE complexes from oligomerising. It is thought that oligomerization of SNARE complexes into a higher order structure creates a SNARE scaffold for efficient, regulated fusion of synaptic vesicles. Synaphin promotes neuronal exocytosis by promoting interaction between the complementary syntaxin and synaptobrevin transmembrane regions that reside in opposing membranes prior to fusion.


Pssm-ID: 461755 [Multi-domain]  Cd Length: 142  Bit Score: 126.41  E-value: 6.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34364694     1 MAFLMKSMISNQVKNL--GFGGGSEENKEEGGasdpaaaqgMTREEYEEYQKQMIEEKMERDAAFTQKKAERACLRVHLR 78
Cdd:pfam05835   1 MAFLAKQMVGNQLKNVkgGLGGKGGEEKEDAE---------MTREEEEEYQEALREEEEERKAKHRKMEAEREKMRQHIR 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34364694    79 EKYRLPKSEMDENQIQMA---------GDDVDLPEDLRKMVDEDQEEEEDKDSILGQIQNLQNMDLDTIKE 140
Cdd:pfam05835  72 DKYRLKKKEEDEAEIQAAmepstegrlGRDKKTPEELAKMVEEDEEEEEEKDSVLGKLQNTLNTDVDELKE 142
Complexin_NTD_CPLX_III_IV cd22809
N-terminal SNARE complex binding domain found in complexins III and IV; Complexins (CPXs) are ...
 43-86 4.45e-21

N-terminal SNARE complex binding domain found in complexins III and IV; Complexins (CPXs) are small, cytosolic proteins that bind to the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex to regulate synaptic vesicle exocytosis. Complexins III (CPX III) and IV (CPX IV) are the only CPX isoforms present in retinal ribbon synapses. They carry an extension with a functional CAAX-box farnesylation site that is absent in CPXs I and II. Their C-terminal farnesylation regulates their synaptic targeting and modulatory function in transmitter release. They may contribute to the unique release efficacy of retinal sensory neurons. CPXs III and IV can functionally replace CPXs I and II, which regulate a late step in the release process, most likely by stabilizing SNARE complexes and thus maintaining synaptic vesicles in a highly release competent state. This model corresponds to the N-terminal SNARE complex binding domain of CPXs III and IV.


Pssm-ID: 439283  Cd Length: 44  Bit Score: 80.38  E-value: 4.45e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 34364694  43 EEYEEYQKQMIEEKMERDAAFTQKKAERACLRVHLREKYRLPKS 86
Cdd:cd22809   1 EEEEEYQKQLEEEKKERDAAFAQKKAERAAMRAHLREKYRLPKN 44
Complexin_NTD cd22740
N-terminal SNARE complex binding domain of the complexin family of SNARE regulators; ...
 43-83 5.19e-13

N-terminal SNARE complex binding domain of the complexin family of SNARE regulators; Complexins (CPXs) are small, cytosolic proteins that bind to the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex to regulate synaptic vesicle exocytosis. There are four CPX isoforms: complexin I/synaphin-2, complexin II/synaphin-1, complexin III and complexin IV. CPXs I and II are highly homologous hydrophilic proteins that are enriched in neurons where they colocalize with syntaxin and SNAP25. They regulate the sequential interactions of alpha-SNAP and synaptotagmins with the SNAP receptor during exocytosis. CPXs III and IV are the only CPX isoforms present in retinal ribbon synapses. In addition, CPXs III and IV carry an extension with a functional CAAX-box farnesylation site that is absent in CPXs I and II. Their C-terminal farnesylation regulates their synaptic targeting and modulatory function in transmitter release. They may contribute to the unique release efficacy of retinal sensory neurons. CPXs III and IV can functionally replace CPXs I and II. Most of the invertebrate CPXs are more similar to CPXs I and II than to CPXs III and IV. This model corresponds to the N-terminal region of CPX that is responsible for SNARE complex binding.


Pssm-ID: 439281  Cd Length: 41  Bit Score: 59.50  E-value: 5.19e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 34364694  43 EEYEEYQKQMIEEKMERDAAFTQKKAERACLRVHLREKYRL 83
Cdd:cd22740   1 EEEEEYQEALREEEEERDAKHAQMKAERAAMRQHIRDKYGL 41
 
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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