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Conserved domains on  [gi|893571730|ref|NP_001297584|]
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leukocyte cell-derived chemotaxin 1 isoform 1 [Mus musculus]

Protein Classification

BRICHOS domain-containing protein( domain architecture ID 10660096)

BRICHOS domain-containing protein such as human gastrokines that may be involved in maintaining the integrity of the gastric mucosal epithelium

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRICHOS smart01039
The BRICHOS domain is found in a variety of proteins implicated in dementia, respiratory ...
 105-201 3.21e-30

The BRICHOS domain is found in a variety of proteins implicated in dementia, respiratory distress and cancer; Its exact function is unknown; roles that have been proposed for the domain, which is about 100 amino acids long, include (a) targeting of the protein to the secretory pathway, (b) intramolecular chaperone-like function, and (c) assisting the specialised intracellular protease processing system. This C-terminal domain is embedded in the endoplasmic reticulum lumen, and binds to the N-terminal, transmembrane, SP_C, pfam08999 provided that it is in non-helical conformation. Thus the Brichos domain of proSP-C is a chaperone that induces alpha-helix formation of an aggregation-prone TM region.


:

Pssm-ID: 198107  Cd Length: 96  Bit Score: 110.44  E-value: 3.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893571730   105 GSGAEEAIEVNDFKNGITGIRFAGGEKCYIKAQVKARIPEVgtvtkQSISEL-EGKIMPANYEENSLIWVA---VDQPVK 180
Cdd:smart01039   1 FSGSDSWTVIHDFKNGLTAYRPLGKKKCYIKKMNKEVIPSL-----QSLLELlENKKMPGGPYPKQTYYVVepvVGEKIK 75

                           90       100
                   ....*....|....*....|.
gi 893571730   181 DSSFLSSKILELCGDLPIFWL 201
Cdd:smart01039  76 DLSFLGSPIAELCKGVPTYWL 96
 
Name Accession Description Interval E-value
BRICHOS smart01039
The BRICHOS domain is found in a variety of proteins implicated in dementia, respiratory ...
 105-201 3.21e-30

The BRICHOS domain is found in a variety of proteins implicated in dementia, respiratory distress and cancer; Its exact function is unknown; roles that have been proposed for the domain, which is about 100 amino acids long, include (a) targeting of the protein to the secretory pathway, (b) intramolecular chaperone-like function, and (c) assisting the specialised intracellular protease processing system. This C-terminal domain is embedded in the endoplasmic reticulum lumen, and binds to the N-terminal, transmembrane, SP_C, pfam08999 provided that it is in non-helical conformation. Thus the Brichos domain of proSP-C is a chaperone that induces alpha-helix formation of an aggregation-prone TM region.


Pssm-ID: 198107  Cd Length: 96  Bit Score: 110.44  E-value: 3.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893571730   105 GSGAEEAIEVNDFKNGITGIRFAGGEKCYIKAQVKARIPEVgtvtkQSISEL-EGKIMPANYEENSLIWVA---VDQPVK 180
Cdd:smart01039   1 FSGSDSWTVIHDFKNGLTAYRPLGKKKCYIKKMNKEVIPSL-----QSLLELlENKKMPGGPYPKQTYYVVepvVGEKIK 75

                           90       100
                   ....*....|....*....|.
gi 893571730   181 DSSFLSSKILELCGDLPIFWL 201
Cdd:smart01039  76 DLSFLGSPIAELCKGVPTYWL 96
BRICHOS pfam04089
BRICHOS domain; The BRICHOS domain is about 100 amino acids long. It is found in a variety of ...
 107-200 7.64e-27

BRICHOS domain; The BRICHOS domain is about 100 amino acids long. It is found in a variety of proteins implicated in dementia, respiratory distress and cancer. Its exact function is unknown; roles that have been proposed for it include (a) in targeting of the protein to the secretory pathway, (b) intramolecular chaperone-like function, and (c) assisting the specialized intracellular protease processing system. This C-terminal domain is embedded in the endoplasmic reticulum lumen, and binds to the N-terminal, transmembrane, SP_C, pfam08999, provided that it is in non-helical conformation. Thus the Brichos domain of proSP-C is a chaperone that induces alpha-helix formation of an aggregation-prone TM region.


Pssm-ID: 461168  Cd Length: 91  Bit Score: 101.61  E-value: 7.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893571730  107 GAEEAIEVNDFKNGITGIRFAGGEKCYIKAQVKARIPEVGTVTKQSISELEGKIMPAnyeENSLIWVAVDQPVKDSSFLS 186
Cdd:pfam04089   1 GNDSATVIHDFKNGLTAYRDLSLKKCYIMKMDKSDVPPLQELLRLLENKEEGEGPPP---ESLGVYVPQTRPVKDLSFLG 77

                          90
                  ....*....|....
gi 893571730  187 SKILELCGDLPIFW 200
Cdd:pfam04089  78 SPIQELCRGLPTYW 91
 
Name Accession Description Interval E-value
BRICHOS smart01039
The BRICHOS domain is found in a variety of proteins implicated in dementia, respiratory ...
 105-201 3.21e-30

The BRICHOS domain is found in a variety of proteins implicated in dementia, respiratory distress and cancer; Its exact function is unknown; roles that have been proposed for the domain, which is about 100 amino acids long, include (a) targeting of the protein to the secretory pathway, (b) intramolecular chaperone-like function, and (c) assisting the specialised intracellular protease processing system. This C-terminal domain is embedded in the endoplasmic reticulum lumen, and binds to the N-terminal, transmembrane, SP_C, pfam08999 provided that it is in non-helical conformation. Thus the Brichos domain of proSP-C is a chaperone that induces alpha-helix formation of an aggregation-prone TM region.


Pssm-ID: 198107  Cd Length: 96  Bit Score: 110.44  E-value: 3.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893571730   105 GSGAEEAIEVNDFKNGITGIRFAGGEKCYIKAQVKARIPEVgtvtkQSISEL-EGKIMPANYEENSLIWVA---VDQPVK 180
Cdd:smart01039   1 FSGSDSWTVIHDFKNGLTAYRPLGKKKCYIKKMNKEVIPSL-----QSLLELlENKKMPGGPYPKQTYYVVepvVGEKIK 75

                           90       100
                   ....*....|....*....|.
gi 893571730   181 DSSFLSSKILELCGDLPIFWL 201
Cdd:smart01039  76 DLSFLGSPIAELCKGVPTYWL 96
BRICHOS pfam04089
BRICHOS domain; The BRICHOS domain is about 100 amino acids long. It is found in a variety of ...
 107-200 7.64e-27

BRICHOS domain; The BRICHOS domain is about 100 amino acids long. It is found in a variety of proteins implicated in dementia, respiratory distress and cancer. Its exact function is unknown; roles that have been proposed for it include (a) in targeting of the protein to the secretory pathway, (b) intramolecular chaperone-like function, and (c) assisting the specialized intracellular protease processing system. This C-terminal domain is embedded in the endoplasmic reticulum lumen, and binds to the N-terminal, transmembrane, SP_C, pfam08999, provided that it is in non-helical conformation. Thus the Brichos domain of proSP-C is a chaperone that induces alpha-helix formation of an aggregation-prone TM region.


Pssm-ID: 461168  Cd Length: 91  Bit Score: 101.61  E-value: 7.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893571730  107 GAEEAIEVNDFKNGITGIRFAGGEKCYIKAQVKARIPEVGTVTKQSISELEGKIMPAnyeENSLIWVAVDQPVKDSSFLS 186
Cdd:pfam04089   1 GNDSATVIHDFKNGLTAYRDLSLKKCYIMKMDKSDVPPLQELLRLLENKEEGEGPPP---ESLGVYVPQTRPVKDLSFLG 77

                          90
                  ....*....|....
gi 893571730  187 SKILELCGDLPIFW 200
Cdd:pfam04089  78 SPIQELCRGLPTYW 91
 
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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