| IED ID | IndEnz0005001392 |
| Enzyme Type ID | lipase001392 |
| Protein Name |
Coatomer subunit gamma-1 Gamma-1-coat protein Gamma-1-COP |
| Gene Name | COPG1 COPG |
| 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 | MLKKFDKKDEESGGGSNPFQHLEKSAVLQEARVFNETPINPRKCAHILTKILYLINQGEHLGTTEATEAFFAMTKLFQSNDPTLRRMCYLTIKEMSCIAEDVIIVTSSLTKDMTGKEDNYRGPAVRALCQITDSTMLQAIERYMKQAIVDKVPSVSSSALVSSLHLLKCSFDVVKRWVNEAQEAASSDNIMVQYHALGLLYHVRKNDRLAVNKMISKVTRHGLKSPFAYCMMIRVASKQLEEEDGSRDSPLFDFIESCLRNKHEMVVYEAASAIVNLPGCSAKELAPAVSVLQLFCSSPKAALRYAAVRTLNKVAMKHPSAVTACNLDLENLVTDSNRSIATLAITTLLKTGSESSIDRLMKQISSFMSEISDEFKVVVVQAISALCQKYPRKHAVLMNFLFTMLREEGGFEYKRAIVDCIISIIEENSESKETGLSHLCEFIEDCEFTVLATRILHLLGQEGPKTTNPSKYIRFIYNRVVLEHEEVRAGAVSALAKFGAQNEEMLPSILVLLKRCVMDDDNEVRDRATFYLNVLEQKQKALNAGYILNGLTVSIPGLERALQQYTLEPSEKPFDLKSVPLATAPMAEQRTESTPITAVKQPEKVAATRQEIFQEQLAAVPEFRGLGPLFKSSPEPVALTESETEYVIRCTKHTFTNHMVFQFDCTNTLNDQTLENVTVQMEPTEAYEVLCYVPARSLPYNQPGTCYTLVALPKEDPTAVACTFSCMMKFTVKDCDPTTGETDDEGYEDEYVLEDLEVTVADHIQKVMKLNFEAAWDEVGDEFEKEETFTLSTIKTLEEAVGNIVKFLGMHPCERSDKVPDNKNTHTLLLAGVFRGGHDILVRSRLLLLDTVTMQVTARSLEELPVDIILASVG |
| Enzyme Length | 874 |
| Uniprot Accession Number | Q9Y678 |
| 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. 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 (By similarity). {ECO:0000250, ECO:0000269|PubMed:20674546}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (14); Chain (1); Helix (6); Modified residue (1); Mutagenesis (1); Natural variant (1); Region (2); Repeat (4); Sequence conflict (5); Turn (3) |
| Keywords | 3D-structure;Cytoplasm;Cytoplasmic vesicle;ER-Golgi transport;Golgi apparatus;Membrane;Phosphoprotein;Protein transport;Reference proteome;Repeat;Transport |
| Interact With | Q92538; Q96RS6; Q9NTJ5 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11056392}. Golgi apparatus membrane {ECO:0000269|PubMed:11056392}; Peripheral membrane protein {ECO:0000269|PubMed:11056392}; Cytoplasmic side {ECO:0000269|PubMed:11056392}. 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:0007744|PubMed:23186163 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1R4X; |
| Mapped Pubmed ID | 10052452; 10318838; 10679020; 10761932; 10903204; 10921873; 11035033; 11172815; 11285137; 11306556; 11461920; 11493604; 11689559; 11703931; 11726511; 11739780; 11748249; 11893085; 12388752; 14504276; 14527956; 14654841; 14742712; 15029241; 15272311; 15632110; 15728195; 15878873; 1631136; 16571679; 16633337; 16723730; 1680566; 16926190; 16940185; 17113389; 17253781; 17274799; 17314511; 17353931; 17360540; 17451557; 17760859; 17927562; 18086915; 18182008; 18283113; 18287528; 18809720; 1898986; 19015319; 19039328; 19109418; 19151722; 19164740; 19296914; 19367725; 19369418; 1957170; 19596235; 19615732; 19631211; 19758564; 19805454; 20005805; 20136777; 20360068; 20427317; 20462495; 20467437; 20468064; 20534429; 20637885; 20711500; 21219331; 21550981; 21844168; 21900206; 21988832; 22013193; 22094269; 22304919; 22555292; 23386615; 23396477; 23416715; 23427261; 23606334; 23839779; 24119662; 24806965; 25036637; 25364732; 25436559; 25609649; 26496610; 26638075; 28646128; 32571874; 33529166; 7691276; 7844144; 8001155; 8128252; 8132710; 8253837; 8505331; 8636227; 8991093; 9114004; 9150144; 9244307; 9288971; 9323141; 9380700; 9382863; 9405360; 9472029; 9490716; 9671725; 9751720; 9990005; |
| Motif | |
| Gene Encoded By | |
| Mass | 97,718 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |