Detail Information for IndEnz0005000589
IED ID IndEnz0005000589
Enzyme Type ID lipase000589
Protein Name Coatomer subunit gamma-1
Gamma-1-coat protein
Gamma-1-COP
Gene Name Copg1 Copg
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 MLKKFDKKDEESGGGSNPLQHLEKSAVLQEARVFNETPINPRKCAHILTKILYLINQGEHLGTTEATEAFFAMTKLFQSNDPTLRRMCYLTIKEMSCIAEDVIIVTSSLTKDMTGKEDNYRGPAVRALCQITDSTMLQAVERYMKQAIVDKVPSVSSSALVSSLHLLKCSFDVVKRWVNEAQEAASSDNIMVQYHALGLLYHVRKNDRLAVSKMISKFTRHGLKSPFAYCMMIRVASKQLEEEDGSRDSPLFDFIESCLRNKHEMVVYEAASAIVNLPGCSAKELAPAVSVLQLFCSSPKAALRYAAVRTLNKVAMKHPSAVTACNLDLENLVTDSNRSIATLAITTLLKTGSESSIDRLMKQISSFMSEISDEFKVVVVQAISALCQKYPRKHAVLMNFLFTMLREEGGFEYKRAIVDCIISIIEENSESKETGLSHLCEFIEDCEFTVLATRILHLLGQEGPKTNNPSKYIRFIYNRVVLEHEEVRAGAVSALAKFGAQNEEMLPSILVLLKRCVMDDDNEVRDRATFYLNVLEQKQKALNAGYILNGLTVSIPGLEKALQQYTLEPSEKPFDLKSVPLATTPMAEQRPESTATAAVKQPEKVAATRQEIFQEQLAAVPEFQGLGPLFKSSPEPVALTESETEYVIRCTKHTFSDHLVFQFDCTNTLNDQTLENVTVQMEPTEAYEVLSYVPARSLPYNQPGTCYTLVALPTEDPTAVACTFSCVMKFTVKDCDPNTGEIDEEGYEDEYVLEDLEVTVADHIQKVMKVNFEAAWDEVGDEFEKEETFTLSTIKTLEEAVGNIVKFLGMHPCERSDKVPENKNTHTLLLAGVFRGGHDILVRSRLLLLDTVTMQVTARSSEELPVDIILASVG
Enzyme Length 874
Uniprot Accession Number Q9QZE5
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis. {ECO:0000250, ECO:0000269|PubMed:19067489}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Frameshift (1); Modified residue (1); Region (2); Repeat (4); Sequence conflict (5)
Keywords 3D-structure;Cytoplasm;Cytoplasmic vesicle;ER-Golgi transport;Golgi apparatus;Membrane;Phosphoprotein;Protein transport;Reference proteome;Repeat;Transport
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}. Golgi apparatus membrane {ECO:0000269|PubMed:17360540}; Peripheral membrane protein {ECO:0000269|PubMed:17360540}; Cytoplasmic side {ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Predominantly located in the cis-Golgi apparatus. {ECO:0000250}.
Modified Residue MOD_RES 594; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9Y678
Post Translational Modification
Signal Peptide
Structure 3D Electron microscopy (10)
Cross Reference PDB 5A1U; 5A1V; 5A1W; 5A1X; 5A1Y; 5NZR; 5NZS; 5NZT; 5NZU; 5NZV;
Mapped Pubmed ID 10725249; 10788617; 11217851; 12466851; 12520002; 14610273; 14681479; 18554416; 18799693; 21267068; 21677750; 25438880; 26160949; 28621666; 29437892; 9811942;
Motif
Gene Encoded By
Mass 97,513
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda