Colipase
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| Aliases | CLPS, entrez:1208 | ||||||||||||||||
| External IDs | OMIM: 120105 MGI: 88421 HomoloGene: 1383 GeneCards: CLPS | ||||||||||||||||
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| Species | Human | Mouse | |||||||||||||||
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| Location (UCSC) | Chr 6: 35.79 – 35.8 Mb | Chr 17: 28.56 – 28.56 Mb | |||||||||||||||
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| Colipase N-terminal domain | |||||||||
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Structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate.
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| Identifiers | |||||||||
| Symbol | Colipase | ||||||||
| Pfam | PF01114 | ||||||||
| InterPro | IPR001981 | ||||||||
| PROSITE | PDOC00111 | ||||||||
| SCOP | 1lpb | ||||||||
| SUPERFAMILY | 1lpb | ||||||||
| CDD | cd00039 | ||||||||
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| Available protein structures: | |
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| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
| Colipase C-terminal domain | |||||||||
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solution structure of porcine pancreatic procolipase as determined from 1h homonuclear two-and three-dimensional nmr
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| Identifiers | |||||||||
| Symbol | Colipase_C | ||||||||
| Pfam | PF02740 | ||||||||
| InterPro | IPR017914 | ||||||||
| PROSITE | PDOC00111 | ||||||||
| SCOP | 1lpb | ||||||||
| SUPERFAMILY | 1lpb | ||||||||
| CDD | cd00039 | ||||||||
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| Available protein structures: | |
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| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
NM_001832
NM_001252597
NM_001252598
NP_001239526
NP_001239527
NP_001823
NP_079745.1
NP_001303994.1
NP_001303994
NP_079745
Colipase 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.
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Wikipedia