Detail Information for IndEnz0005000417
IED ID IndEnz0005000417
Enzyme Type ID lipase000417
Protein Name Angiopoietin-like protein 8
Betatrophin
Lipasin
Refeeding-induced fat and liver protein
Gene Name Angptl8 Gm6484 Rifl
Organism Mus musculus (Mouse)
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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MAVLALCLLWTLASAVRPAPVAPLGGPEPAQYEELTLLFHGALQLGQALNGVYRATEARLTEAGHSLGLYDRALEFLGTEVRQGQDATQELRTSLSEIQVEEDALHLRAEATARSLGEVARAQQALRDTVRRLQVQLRGAWLGQAHQEFETLKARADKQSHLLWALTGHVQRQQREMAEQQQWLRQIQQRLHTAALPA
Enzyme Length 198
Uniprot Accession Number Q8R1L8
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels (PubMed:22569073, PubMed:22809513, PubMed:23150577, PubMed:24043787). May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state (PubMed:24043787). According to a report, may act by promoting ANGPTL3 cleavage (PubMed:23150577). According to another study, not required for cleavage of ANGPTL3 (PubMed:24043787). {ECO:0000269|PubMed:22569073, ECO:0000269|PubMed:22809513, ECO:0000269|PubMed:23150577, ECO:0000269|PubMed:24043787}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Sequence conflict (1); Signal peptide (1)
Keywords Hormone;Lipid metabolism;Reference proteome;Secreted;Signal
Interact With
Induction INDUCTION: Highly up-regulated following high-fat diet treatment. Down-regulated upon fasting. Strongly induced in the cold environment (4 Degrees Celsius for 4 hours). {ECO:0000269|PubMed:22809513, ECO:0000269|PubMed:23150577, ECO:0000269|PubMed:23261442}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22569073}.
Modified Residue
Post Translational Modification PTM: Proteolytically cleaved at the N-terminus. {ECO:0000250|UniProtKB:Q6UXH0}.
Signal Peptide SIGNAL 1..15; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 21677750; 25917759; 25954050; 26569053; 26687026; 27045862; 27097546; 27459526; 27469268; 28204173; 28413163; 28528274; 29031715; 29768498; 31388006; 31470507; 32154742; 32730227; 32739681; 33684391; 34163433;
Motif
Gene Encoded By
Mass 22,063
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda