| IED ID | IndEnz0005001391 |
| Enzyme Type ID | lipase001391 |
| Protein Name |
Coatomer subunit beta Beta-coat protein Beta-COP |
| Gene Name | COPB1 COPB MSTP026 |
| 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 | MTAAENVCYTLINVPMDSEPPSEISLKNDLEKGDVKSKTEALKKVIIMILNGEKLPGLLMTIIRFVLPLQDHTIKKLLLVFWEIVPKTTPDGRLLHEMILVCDAYRKDLQHPNEFIRGSTLRFLCKLKEAELLEPLMPAIRACLEHRHSYVRRNAVLAIYTIYRNFEHLIPDAPELIHDFLVNEKDASCKRNAFMMLIHADQDRALDYLSTCIDQVQTFGDILQLVIVELIYKVCHANPSERARFIRCIYNLLQSSSPAVKYEAAGTLVTLSSAPTAIKAAAQCYIDLIIKESDNNVKLIVLDRLIELKEHPAHERVLQDLVMDILRVLSTPDLEVRKKTLQLALDLVSSRNVEELVIVLKKEVIKTNNVSEHEDTDKYRQLLVRTLHSCSVRFPDMAANVIPVLMEFLSDNNEAAAADVLEFVREAIQRFDNLRMLIVEKMLEVFHAIKSVKIYRGALWILGEYCSTKEDIQSVMTEIRRSLGEIPIVESEIKKEAGELKPEEEITVGPVQKLVTEMGTYATQSALSSSRPTKKEEDRPPLRGFLLDGDFFVAASLATTLTKIALRYVALVQEKKKQNSFVAEAMLLMATILHLGKSSLPKKPITDDDVDRISLCLKVLSECSPLMNDIFNKECRQSLSHMLSAKLEEEKLSQKKESEKRNVTVQPDDPISFMQLTAKNEMNCKEDQFQLSLLAAMGNTQRKEAADPLASKLNKVTQLTGFSDPVYAEAYVHVNQYDIVLDVLVVNQTSDTLQNCTLELATLGDLKLVEKPSPLTLAPHDFANIKANVKVASTENGIIFGNIVYDVSGAASDRNCVVLSDIHIDIMDYIQPATCTDAEFRQMWAEFEWENKVTVNTNMVDLNDYLQHILKSTNMKCLTPEKALSGYCGFMAANLYARSIFGEDALANVSIEKPIHQGPDAAVTGHIRIRAKSQGMALSLGDKINLSQKKTSI |
| Enzyme Length | 953 |
| Uniprot Accession Number | P53618 |
| 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. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins. 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 surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis (By similarity). Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments. {ECO:0000250, ECO:0000269|PubMed:18385291, ECO:0000269|PubMed:18725938, ECO:0000269|PubMed:19364919, ECO:0000269|PubMed:20056612}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Initiator methionine (1); Modified residue (2); Natural variant (1); Repeat (6); Sequence conflict (12) |
| Keywords | Acetylation;Cataract;Cell membrane;Cytoplasm;Cytoplasmic vesicle;Disease variant;ER-Golgi transport;Golgi apparatus;Host-virus interaction;Membrane;Mental retardation;Protein transport;Reference proteome;Repeat;Transport |
| Interact With | P48444; P56945; Q9BZE4; P42858; Q86T90; Q9Y250; Q96RS6; Q9UH99; O94972; Q9BSA4 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane {ECO:0000269|PubMed:11056392, ECO:0000269|PubMed:17451557, ECO:0000269|PubMed:7573041}; Peripheral membrane protein {ECO:0000269|PubMed:17451557, ECO:0000269|PubMed:18385291, ECO:0000269|PubMed:20056612}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:20362547}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q9JIF7}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it (By similarity). Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm (By similarity). Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack (By similarity). Occasionally present at the trans-side of Golgi, but mainly present at the cis-Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae (By similarity). Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles (By similarity). Some association with high-density and low-density microsomes and mitochondria/nuclei fraction (By similarity). Very little found in plasma membrane fraction (PubMed:20362547). {ECO:0000250|UniProtKB:P23514, ECO:0000269|PubMed:20362547}. |
| Modified Residue | MOD_RES 2; /note="N-acetylthreonine"; /evidence="ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895"; MOD_RES 494; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:Q9JIF7" |
| Post Translational Modification | PTM: Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10052452; 10318838; 10679020; 10761932; 10903204; 10921873; 11035033; 11172815; 11285137; 11306556; 11461920; 11493604; 11689559; 11703931; 11726511; 11739780; 11748249; 12388752; 14504276; 14527956; 14654841; 14742712; 14743216; 15029241; 15272311; 15494376; 15632110; 15728195; 15878873; 16189514; 1631136; 16571679; 16633337; 16713569; 16723730; 1680566; 16926190; 16940185; 17110338; 17113389; 17253781; 17274799; 17360540; 17500595; 17760859; 17927562; 18086915; 18182008; 18283113; 18287528; 18809720; 1898986; 19015319; 19039328; 19109418; 19151722; 19164740; 19296914; 19367725; 19369418; 19463016; 1957170; 19631211; 19738201; 19758564; 20005805; 20136777; 20360068; 20427317; 20462495; 20467437; 20534429; 20551905; 20562859; 20637885; 20711500; 20932832; 21219331; 21550981; 21844168; 21911578; 21988832; 22013193; 22094269; 22304919; 22555292; 22593156; 22810585; 23386615; 23396477; 23416715; 23606334; 23650620; 23752268; 23839779; 24119662; 24189400; 25036637; 25364732; 25436559; 25609649; 26496610; 26638075; 26752685; 27207835; 32986658; 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 | 107,142 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |