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Conserved domains on  [gi|4502895|ref|NP_001823|]
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colipase isoform 1 preproprotein [Homo sapiens]

Protein Classification

CLPS domain-containing protein( domain architecture ID 12184505)

CLPS domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COLIPASE smart00023
Colipase; Colipase is a protein that functions as a cofactor for pancreatic lipase, with which ...
 18-112 8.66e-60

Colipase; Colipase is a protein that functions as a cofactor for pancreatic lipase, with which it forms a stoichiometric complex. It also binds to the bile-salt covered triacylglycerol interface thus allowing the enzyme to anchor itself to the water-lipid interface. Colipase is a small protein of approximately 100 amino-acid residues with five conserved disulfide bonds.


:

Pssm-ID: 128339  Cd Length: 95  Bit Score: 178.10  E-value: 8.66e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502895      18 APGPRGIIINLENGELCMNSAQCKSNCCQHSSALGLARCTSMASENSECSVKTLYGIYYKCPCERGLTCEGDKTIVGSIT 97
Cdd:smart00023   1 APDPRGLIINLEAGELCLNSAQCKSGCCQHDSGLSLARCAPKASENSECSAKTLYGVYYKCPCERGLTCEGDKSIVGSIT 80

                           90
                   ....*....|....*
gi 4502895      98 NTNFGICHDAGRSKQ 112
Cdd:smart00023  81 NTNFGICHDAGRSKQ 95
 
Name Accession Description Interval E-value
COLIPASE smart00023
Colipase; Colipase is a protein that functions as a cofactor for pancreatic lipase, with which ...
 18-112 8.66e-60

Colipase; Colipase is a protein that functions as a cofactor for pancreatic lipase, with which it forms a stoichiometric complex. It also binds to the bile-salt covered triacylglycerol interface thus allowing the enzyme to anchor itself to the water-lipid interface. Colipase is a small protein of approximately 100 amino-acid residues with five conserved disulfide bonds.


Pssm-ID: 128339  Cd Length: 95  Bit Score: 178.10  E-value: 8.66e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502895      18 APGPRGIIINLENGELCMNSAQCKSNCCQHSSALGLARCTSMASENSECSVKTLYGIYYKCPCERGLTCEGDKTIVGSIT 97
Cdd:smart00023   1 APDPRGLIINLEAGELCLNSAQCKSGCCQHDSGLSLARCAPKASENSECSAKTLYGVYYKCPCERGLTCEGDKSIVGSIT 80

                           90
                   ....*....|....*
gi 4502895      98 NTNFGICHDAGRSKQ 112
Cdd:smart00023  81 NTNFGICHDAGRSKQ 95
CLPS cd23011
Colipase; Colipase, also called CLPS, is a protein co-enzyme required for optimal enzyme ...
 23-106 1.14e-54

Colipase; Colipase, also called CLPS, is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. Bile salts, at concentrations near their critical micellar concentration, desorb lipase from emulsified triacylglycerol and, thereby, inhibit lipolysis. Colipase functions by anchoring pancreatic lipase to the lipid-water interface through the formation of the stoichiometric colipase-lipase complex.


Pssm-ID: 437996  Cd Length: 84  Bit Score: 164.76  E-value: 1.14e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502895   23 GIIINLENGELCMNSAQCKSNCCQHSSALGLARCTSMASENSECSVKTLYGIYYKCPCERGLTCEGDKTIVGSITNTNFG 102
Cdd:cd23011   1 GLIINLDNGELCLNSAQCKSGCCHRDSGLSLARCAPKAAENQECSPKTLYGVYYKCPCESGLTCDADKSIVGSITNTNFG 80


                ....
gi 4502895  103 ICHD 106
Cdd:cd23011  81 ICKD 84
Colipase_C pfam02740
Colipase, C-terminal domain; SCOP reports duplication of common fold with Colipase N-terminal ...
 63-106 6.61e-24

Colipase, C-terminal domain; SCOP reports duplication of common fold with Colipase N-terminal domain.


Pssm-ID: 426952  Cd Length: 44  Bit Score: 85.99  E-value: 6.61e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 4502895     63 NSECSVKTLYGIYYKCPCERGLTCEGDKTIVGSITNTNFGICHD 106
Cdd:pfam02740   1 NSECSPKSLYGVYYKCPCERGLTCEVDKTIVGSITNTNFGICHD 44
 
Name Accession Description Interval E-value
COLIPASE smart00023
Colipase; Colipase is a protein that functions as a cofactor for pancreatic lipase, with which ...
 18-112 8.66e-60

Colipase; Colipase is a protein that functions as a cofactor for pancreatic lipase, with which it forms a stoichiometric complex. It also binds to the bile-salt covered triacylglycerol interface thus allowing the enzyme to anchor itself to the water-lipid interface. Colipase is a small protein of approximately 100 amino-acid residues with five conserved disulfide bonds.


Pssm-ID: 128339  Cd Length: 95  Bit Score: 178.10  E-value: 8.66e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502895      18 APGPRGIIINLENGELCMNSAQCKSNCCQHSSALGLARCTSMASENSECSVKTLYGIYYKCPCERGLTCEGDKTIVGSIT 97
Cdd:smart00023   1 APDPRGLIINLEAGELCLNSAQCKSGCCQHDSGLSLARCAPKASENSECSAKTLYGVYYKCPCERGLTCEGDKSIVGSIT 80

                           90
                   ....*....|....*
gi 4502895      98 NTNFGICHDAGRSKQ 112
Cdd:smart00023  81 NTNFGICHDAGRSKQ 95
CLPS cd23011
Colipase; Colipase, also called CLPS, is a protein co-enzyme required for optimal enzyme ...
 23-106 1.14e-54

Colipase; Colipase, also called CLPS, is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. Bile salts, at concentrations near their critical micellar concentration, desorb lipase from emulsified triacylglycerol and, thereby, inhibit lipolysis. Colipase functions by anchoring pancreatic lipase to the lipid-water interface through the formation of the stoichiometric colipase-lipase complex.


Pssm-ID: 437996  Cd Length: 84  Bit Score: 164.76  E-value: 1.14e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502895   23 GIIINLENGELCMNSAQCKSNCCQHSSALGLARCTSMASENSECSVKTLYGIYYKCPCERGLTCEGDKTIVGSITNTNFG 102
Cdd:cd23011   1 GLIINLDNGELCLNSAQCKSGCCHRDSGLSLARCAPKAAENQECSPKTLYGVYYKCPCESGLTCDADKSIVGSITNTNFG 80


                ....
gi 4502895  103 ICHD 106
Cdd:cd23011  81 ICKD 84
COLIPASE cd00039
Colipase; a stoichiometric cofactor for pancreatic lipase, allowing the enzyme to anchor ...
 18-107 1.40e-51

Colipase; a stoichiometric cofactor for pancreatic lipase, allowing the enzyme to anchor itself to the water-lipid interface and stabilizing the active enzyme conformation


Pssm-ID: 119409  Cd Length: 90  Bit Score: 157.29  E-value: 1.40e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502895   18 APGPRGIIINLENGELCMNSAQCKSNCCQHSSALGLARCTSMASENSECSVKTLYGIYYKCPCERGLTCEGDKTIVGSIT 97
Cdd:cd00039   1 APDPRGIIINLEAGELCLNSAQCKSGCCQHASSLSLARCAAKASENSECSPQTLYGVYYKCPCERGLTCEGDKSIVGSIT 80

                        90
                ....*....|
gi 4502895   98 NTNFGICHDA 107
Cdd:cd00039  81 NTNYGICLDA 90
Colipase_C pfam02740
Colipase, C-terminal domain; SCOP reports duplication of common fold with Colipase N-terminal ...
 63-106 6.61e-24

Colipase, C-terminal domain; SCOP reports duplication of common fold with Colipase N-terminal domain.


Pssm-ID: 426952  Cd Length: 44  Bit Score: 85.99  E-value: 6.61e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 4502895     63 NSECSVKTLYGIYYKCPCERGLTCEGDKTIVGSITNTNFGICHD 106
Cdd:pfam02740   1 NSECSPKSLYGVYYKCPCERGLTCEVDKTIVGSITNTNFGICHD 44
CLPS_Dkk_Cys2 cd23008
Colipase and the second cysteine-rich (Cys-2) domain of Dickkopf proteins; Colipase (also ...
 27-104 3.36e-21

Colipase and the second cysteine-rich (Cys-2) domain of Dickkopf proteins; Colipase (also called CLPS) is a cysteine-rich protein that adopts a similar fold to a cysteine-rich domain (Cys-2) of the Dickkopf (Dkk) family proteins. Colipase functions to prevent the inhibitory effect of bile salts on lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. Dickkopf proteins are a discrete class of secreted Wnt inhibitors that are required for many developmental processes, including segmentation, endoderm development, limb polarity, neural crest differentiation, kidney morphogenesis, sex determination and brain development. They possess an N-terminal signal peptide and contain two conserved cysteine-rich domains (Cys-1 and Cys-2) separated by a linker region. The Dickkopf Cys-2 domain is similar to proteins in the colipase family and it has been suggested that the Cys-2 domain of Dkks may enable interaction with lipids in order to regulate Wnt function.


Pssm-ID: 437995  Cd Length: 82  Bit Score: 80.04  E-value: 3.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502895   27 NLENGELCMNSAQCKS-NCCQHSsaLGLARCTSMASENSECSVKTLYG-----IYYKCPCERGLTCEGDKTIVGSITNTN 100
Cdd:cd23008   1 KGDEGELCLRSSDCKSgNCCARH--FWLKICKPVLREGSVCTKFRLKGshgleIFQRCPCERGLSCEGDKDLVGSSTNTR 78


                ....
gi 4502895  101 FGIC 104
Cdd:cd23008  79 LHIC 82
Colipase pfam01114
Colipase, N-terminal domain; SCOP reports duplication of common fold with Colipase C-terminal ...
 21-60 2.01e-18

Colipase, N-terminal domain; SCOP reports duplication of common fold with Colipase C-terminal domain.


Pssm-ID: 279458  Cd Length: 40  Bit Score: 72.13  E-value: 2.01e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 4502895     21 PRGIIINLENGELCMNSAQCKSNCCQHSSALGLARCTSMA 60
Cdd:pfam01114   1 PRGIIINLEDGELCLNSAQCKSNCCQHDSILSLARCAPKA 40
 
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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