| IED ID | IndEnz0005000377 |
| Enzyme Type ID | lipase000377 |
| Protein Name |
Inactive pancreatic lipase-related protein 1 PL-RP1 |
| Gene Name | PNLIPRP1 PLRP1 |
| Organism | Canis lupus familiaris (Dog) (Canis familiaris) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris) |
| Enzyme Sequence | MVSIWTIALFLLGAAKAKEVCYEQIGCFSDAEPWAGTAIRPLKVLPWSPERIGTRFLLYTNKNPNNFQTLLPSDPSTIEASNFQTDKKTRFIIHGFIDKGEENWLLDMCKNMFKVEEVNCICVDWKKGSQTSYTQAANNVRVVGAQVAQMLSMLSANYSYSPSQVQLIGHSLGAHVAGEAGSRTPGLGRITGLDPVEASFQGTPEEVRLDPTDADFVDVIHTDAAPLIPFLGFGTSQQMGHLDFFPNGGEEMPGCKKNALSQIVDLDGIWEGTRDFVACNHLRSYKYYSESILNPDGFASYPCASYRAFESNKCFPCPDQGCPQMGHYADKFAVKTSDETQKYFLNTGDSSNFARWRYGVSITLSGKRATGQAKVALFGSKGNTHQFNIFKGILKPGSTHSNEFDAKLDVGTIEKVKFLWNNNVVNPTFPKVGAAKITVQKGEEKTVHSFCSESTVREDVLLTLTPC |
| Enzyme Length | 467 |
| Uniprot Accession Number | P06857 |
| Absorption | |
| Active Site | ACT_SITE 171; /note=Nucleophile; ACT_SITE 194; /note=Charge relay system; ACT_SITE 281; /note=Charge relay system |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: May function as inhibitor of dietary triglyceride digestion. Lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters (in vitro). |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (23); Chain (1); Disulfide bond (6); Domain (1); Erroneous gene model prediction (1); Glycosylation (1); Helix (13); Metal binding (4); Mutagenesis (2); Sequence conflict (3); Signal peptide (1); Turn (7) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Lipid degradation;Lipid metabolism;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9726421}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000269|PubMed:9726421 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1RP1; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,482 |
| Kinetics | |
| Metal Binding | METAL 205; /note=Calcium; via carbonyl oxygen; METAL 208; /note=Calcium; via carbonyl oxygen; METAL 210; /note=Calcium; METAL 213; /note=Calcium |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.26; |