| IED ID | IndEnz0005000053 |
| Enzyme Type ID | lipase000053 |
| Protein Name |
Perilipin-1 Lipid droplet-associated protein Perilipin A |
| Gene Name | Plin1 Peri Plin |
| 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 | MSMNKGPTLLDGDLPEQENVLQRVLQLPVVSGTCECFQKTYNSTKEAHPLVASVCNAYEKGVQGASNLAAWSMEPVVRRLSTQFTAANELACRGLDHLEEKIPALQYPPEKIASELKGTISTRLRSARNSISVPIASTSDKVLGATLAGCELALGMAKETAEYAANTRVGRLASGGADLALGSIEKVVEFLLPPDKESAPSSGRQRTQKAPKAKPSLVRRVSTLANTLSRHTMQTTAWALKQGHSLAMWIPGVAPLSSLAQWGASAAMQVVSRRQSEVRVPWLHNLAASQDESHDDQTDTEGEETDDEEEEEESEAEENVLREVTALPNPRGLLGGVVHTVQNTLRNTISAVTWAPAAVLGTVGRILHLTPAQAVSSTKGRAMSLSDALKGVTDNVVDTVVHYVPLPRLSLMEPESEFRDIDNPSAEAERKGSGARPASPESTPRPGQPRGSLRSVRGLSAPSCPGLDDKTEASARPGFLAMPREKPARRVSDSFFRPSVMEPILGRAQYSQLRKKS |
| Enzyme Length | 517 |
| Uniprot Accession Number | Q8CGN5 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness (By similarity). Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels. {ECO:0000250, ECO:0000269|PubMed:23481402}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (6); Chain (1); Compositional bias (1); Modified residue (19); Region (4); Sequence conflict (2) |
| Keywords | Alternative splicing;Endoplasmic reticulum;Lipid droplet;Lipid metabolism;Phosphoprotein;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:O60240}. Lipid droplet {ECO:0000269|PubMed:23481402, ECO:0000269|PubMed:24945349}. Note=Lipid droplet surface-associated. {ECO:0000250|UniProtKB:O60240}. |
| Modified Residue | MOD_RES 81; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 85; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 126; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 130; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 132; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 137; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 174; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 223; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 298; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P43884"; MOD_RES 300; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P43884"; MOD_RES 314; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P43884"; MOD_RES 384; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 386; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P43884"; MOD_RES 410; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:19921680, ECO:0007744|PubMed:21183079"; MOD_RES 433; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:O60240"; MOD_RES 439; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P43884"; MOD_RES 460; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:19921680"; MOD_RES 492; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:24945349, ECO:0007744|PubMed:21183079"; MOD_RES 494; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079" |
| Post Translational Modification | PTM: Major cAMP-dependent protein kinase-substrate in adipocytes, also dephosphorylated by PP1. When phosphorylated, may be maximally sensitive to HSL and when unphosphorylated, may play a role in the inhibition of lipolysis, by acting as a barrier in lipid droplet (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11101849; 11371650; 11751901; 12407111; 12466851; 12810697; 12832420; 14527948; 14578284; 14610073; 14704148; 14726448; 15111495; 15136565; 15197189; 15342676; 16243839; 16448845; 16571721; 16595669; 16679289; 17114792; 17401109; 17463056; 17488708; 17921437; 18390901; 18393390; 18487449; 18719666; 18762440; 19116774; 19299455; 19324970; 19515989; 19797618; 19850935; 20091459; 21103377; 21944269; 21983901; 21989031; 22028793; 22609209; 22685330; 22940098; 23204327; 23296636; 23734208; 23805974; 23907538; 24706781; 24727056; 24927580; 25197048; 25351614; 25416668; 25535287; 25677823; 25695774; 25855981; 26220403; 26243869; 26411340; 26417690; 26521150; 26659641; 26963625; 27185876; 27373682; 27408775; 27807033; 27832861; 28049691; 28111199; 28964716; 29191637; 29407594; 29579167; 30042231; 30862682; 31246957; 31361546; 31706571; 31980640; 32748596; 33567267; 33732701; 33846639; 34023333; |
| Motif | |
| Gene Encoded By | |
| Mass | 55,596 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |