IED ID | IndEnz0005001383 |
Enzyme Type ID | lipase001383 |
Protein Name |
Angiopoietin-like protein 8 Betatrophin Lipasin Refeeding-induced fat and liver protein |
Gene Name | ANGPTL8 C19orf80 RIFL UNQ599/PRO1185 |
Organism | Homo sapiens (Human) |
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MPVPALCLLWALAMVTRPASAAPMGGPELAQHEELTLLFHGTLQLGQALNGVYRTTEGRLTKARNSLGLYGRTIELLGQEVSRGRDAAQELRASLLETQMEEDILQLQAEATAEVLGEVAQAQKVLRDSVQRLEVQLRSAWLGPAYREFEVLKAHADKQSHILWALTGHVQRQRREMVAQQHRLRQIQERLHTAALPA |
Enzyme Length | 198 |
Uniprot Accession Number | Q6UXH0 |
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). 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 (By similarity). {ECO:0000250|UniProtKB:Q8R1L8, ECO:0000269|PubMed:22569073, ECO:0000269|PubMed:22809513, ECO:0000269|PubMed:23150577}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Erroneous gene model prediction (1); Erroneous initiation (1); Natural variant (2); Signal peptide (1) |
Keywords | Diabetes mellitus;Hormone;Lipid metabolism;Reference proteome;Secreted;Signal |
Interact With | Q96PM5 |
Induction | INDUCTION: In response to food intake. Stimulated by insulin. {ECO:0000269|PubMed:22569073, ECO:0000269|PubMed:23150577}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23150577}. |
Modified Residue | |
Post Translational Modification | PTM: Proteolytically cleaved at the N-terminus. {ECO:0000303|PubMed:25099942}. |
Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10900462; 16109723; 17088546; 20581395; 21988832; 23261442; 23415864; 24262987; 24397894; 24960069; 25325797; 25753914; 25850828; 25981323; 26004022; 26077345; 26115519; 26171798; 26289721; 26291796; 26387753; 26457026; 26649318; 26697500; 26739706; 26739836; 26784326; 26822414; 26832343; 26850725; 26863068; 26864934; 26933753; 26934567; 26934667; 27045862; 27053679; 27103367; 27117576; 27188865; 27196053; 27213151; 27238790; 27242389; 27276680; 27402552; 27459526; 27554132; 27578619; 27596060; 27716289; 27733177; 27823982; 27960599; 28125672; 28222635; 28257453; 28319674; 28347650; 28351091; 28351093; 28413163; 28600576; 28684091; 28754724; 28931172; 28938482; 29167926; 29255244; 29266821; 29363048; 29397342; 29490644; 29663480; 29754072; 29890866; 29940978; 29973202; 30007407; 30021605; 30021607; 30054251; 30191588; 30241452; 30248338; 30261196; 30392425; 30409151; 30518729; 30614305; 30900216; 31211513; 31380419; 31772685; 31772689; 31923423; 32034642; 32129695; 32196463; 32239421; 32299395; 32317770; 32421465; 32487544; 32554846; 32732946; 32739681; 32746907; 32829168; 32858055; 32988370; 33011191; 33067796; 33239171; 33909604; 34023284; 34034750; 34167540; 34293055; 34557469; 34884755; 8020465; |
Motif | |
Gene Encoded By | |
Mass | 22,105 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |