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Conserved domains on  [gi|1958768920|ref|XP_038963293|]
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gastrokine-2 isoform X1 [Rattus norvegicus]

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 ...
 63-158 8.12e-34

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: 115.83  E-value: 8.12e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768920   63 HSGSCSSTTIFDYKHGYIASRVLSRRACYIIKMDHKAIPALDKLQRFLYEKQTMNaMASTEYTWVKYNPLksLITKV-DW 141
Cdd:smart01039   1 FSGSDSWTVIHDFKNGLTAYRPLGKKKCYIKKMNKEVIPSLQSLLELLENKKMPG-GPYPKQTYYVVEPV--VGEKIkDL 77

                           90
                   ....*....|....*..
gi 1958768920  142 FLFGSPIEQLCKHIPLY 158
Cdd:smart01039  78 SFLGSPIAELCKGVPTY 94
 
Name Accession Description Interval E-value
BRICHOS smart01039
The BRICHOS domain is found in a variety of proteins implicated in dementia, respiratory ...
 63-158 8.12e-34

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: 115.83  E-value: 8.12e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768920   63 HSGSCSSTTIFDYKHGYIASRVLSRRACYIIKMDHKAIPALDKLQRFLYEKQTMNaMASTEYTWVKYNPLksLITKV-DW 141
Cdd:smart01039   1 FSGSDSWTVIHDFKNGLTAYRPLGKKKCYIKKMNKEVIPSLQSLLELLENKKMPG-GPYPKQTYYVVEPV--VGEKIkDL 77

                           90
                   ....*....|....*..
gi 1958768920  142 FLFGSPIEQLCKHIPLY 158
Cdd:smart01039  78 SFLGSPIAELCKGVPTY 94
BRICHOS pfam04089
BRICHOS domain; The BRICHOS domain is about 100 amino acids long. It is found in a variety of ...
 65-158 3.26e-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: 98.53  E-value: 3.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768920  65 GSCSSTTIFDYKHGYIASRVLSRRACYIIKMDHKAIPALDKLQRFLYEKQTMNAMASTE--YTWVKYNPLKslitkvDWF 142
Cdd:pfam04089   1 GNDSATVIHDFKNGLTAYRDLSLKKCYIMKMDKSDVPPLQELLRLLENKEEGEGPPPESlgVYVPQTRPVK------DLS 74

                          90
                  ....*....|....*.
gi 1958768920 143 LFGSPIEQLCKHIPLY 158
Cdd:pfam04089  75 FLGSPIQELCRGLPTY 90
 
Name Accession Description Interval E-value
BRICHOS smart01039
The BRICHOS domain is found in a variety of proteins implicated in dementia, respiratory ...
 63-158 8.12e-34

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: 115.83  E-value: 8.12e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768920   63 HSGSCSSTTIFDYKHGYIASRVLSRRACYIIKMDHKAIPALDKLQRFLYEKQTMNaMASTEYTWVKYNPLksLITKV-DW 141
Cdd:smart01039   1 FSGSDSWTVIHDFKNGLTAYRPLGKKKCYIKKMNKEVIPSLQSLLELLENKKMPG-GPYPKQTYYVVEPV--VGEKIkDL 77

                           90
                   ....*....|....*..
gi 1958768920  142 FLFGSPIEQLCKHIPLY 158
Cdd:smart01039  78 SFLGSPIAELCKGVPTY 94
BRICHOS pfam04089
BRICHOS domain; The BRICHOS domain is about 100 amino acids long. It is found in a variety of ...
 65-158 3.26e-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: 98.53  E-value: 3.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768920  65 GSCSSTTIFDYKHGYIASRVLSRRACYIIKMDHKAIPALDKLQRFLYEKQTMNAMASTE--YTWVKYNPLKslitkvDWF 142
Cdd:pfam04089   1 GNDSATVIHDFKNGLTAYRDLSLKKCYIMKMDKSDVPPLQELLRLLENKEEGEGPPPESlgVYVPQTRPVK------DLS 74

                          90
                  ....*....|....*.
gi 1958768920 143 LFGSPIEQLCKHIPLY 158
Cdd:pfam04089  75 FLGSPIQELCRGLPTY 90
SF_P smart00019
Pulmonary surfactant proteins; Pulmonary surfactant associated proteins promote alveolar ...
 57-158 2.86e-06

Pulmonary surfactant proteins; Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-C, a component of surfactant, is a highly hydrophobic peptide of 35 amino acid residues which is processed from a larger precursor protein. SP-C is post-translationally modified by the covalent attachment of two palmitoyl groups on two adjacent cysteines


Pssm-ID: 128335 [Multi-domain]  Cd Length: 191  Bit Score: 45.74  E-value: 2.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768920   57 TATINIHSgscSSTTIFDYKHGYIASRVLSRRACYIIKMDHKAIPALDKLQRFLYEKQTMNAMASTEYTWVKYNPLKSLI 136
Cdd:smart00019  91 TATFSIGS---TGIVVYDYQRLLIAYKPAPGTCCYIMKMAPESIPSLEALARKVQNFQAKPAVPTSKLGQEEGHDAGSAS 167

                           90       100
                   ....*....|....*....|..
gi 1958768920  137 TKVDWFLFGSPIEQLCKHIPLY 158
Cdd:smart00019 168 SGGDLAFLGMAVSTLCGEVPLY 189
 
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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