| IED ID | IndEnz0005000058 |
| Enzyme Type ID | lipase000058 |
| Protein Name |
Perilipin-5 Lipid storage droplet protein 5 |
| Gene Name | Plin5 Lsdp5 Oxpat |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MDQRGKDTTLALHSRMSGDQTAQDPGSSLGELDQHNVVKRVVALPLVRATCTAVSGAYNSAKDRHPLLGSACRFAEHCVCSVATCALDHAQPLLEHLQPKLATVNDLACRGLDKLEEKLPFLQQPSDTVVTSAKDAVAKSVTGVVDLAQRGRRWSGELRRSVSQAMDTVLRRSVSQAMDTVLGKSEELVDHFLPMTEAELVALATESQGPEVGSVEEQRQKQGYFVRLGSLSARLRHLAYQHSLGKLRESKHRTQEMLAQLQKTLELIQHMQSRASPTPTFHHPKVQELCGDWSPCLENGYRHSQVELETLALSRSLTLELQSAVDALAGCVRGLPPSAQAKVAEVQRSVDALQATFADAHCLGDVAPTALAEGQDSVAQAHACVDEFLDLVLRAMPLAWLVGPFAPILVERSEPLINLATCVDEVVGDPDPRWAHMDWPAQQRAWEAEPADPGGQEAEPPLGQVKHTMMPELDF |
| Enzyme Length | 475 |
| Uniprot Accession Number | M0R7Z9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE. {ECO:0000269|PubMed:21885430, ECO:0000269|PubMed:22127648, ECO:0000269|PubMed:23353597}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Modified residue (3); Region (6) |
| Keywords | Cytoplasm;Lipid droplet;Mitochondrion;Phosphoprotein;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:21885430, ECO:0000269|PubMed:22127648}. Cytoplasm {ECO:0000250|UniProtKB:Q8BVZ1}. Mitochondrion {ECO:0000269|PubMed:21885430, ECO:0000269|PubMed:22127648}. Note=Lipid droplet surface-associated. Exchanges between lipid droplets and the cytoplasm. {ECO:0000250|UniProtKB:Q8BVZ1}. |
| Modified Residue | MOD_RES 17; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8BVZ1; MOD_RES 175; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8BVZ1; MOD_RES 349; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q00G26 |
| Post Translational Modification | PTM: Phosphorylated by PKA. Phosphorylated on serine in skeletal muscle at rest or upon lipolytic stimulation. {ECO:0000269|PubMed:24303154}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,805 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |