Protein: Coatomer subunit beta (Beta-coat protein) (Beta-COP) (P23514)
Organism: Rattus norvegicus (Rat)
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. 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. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in the axonal compartment of dorsal root ganglion (DRG) cells. 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.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8376457, ECO:0000269|PubMed:8458872}. Golgi apparatus membrane {ECO:0000269|PubMed:10359600, ECO:0000269|PubMed:10402461, ECO:0000269|PubMed:12486083, ECO:0000269|PubMed:1957170, ECO:0000269|PubMed:20056612, ECO:0000269|PubMed:8376457, ECO:0000269|PubMed:8458872}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53618}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:10359600, ECO:0000269|PubMed:15749703, ECO:0000269|PubMed:8458872}; Peripheral membrane protein; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P53618}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q9JIF7}. Microsome membrane {ECO:0000269|PubMed:9165027}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it (PubMed:8458872). 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 (PubMed:8458872). 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 (PubMed:8458872). Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles (PubMed:8458872). Some association with high-density and low-density microsomes and mitochondria/nuclei fraction (PubMed:9165027). Very little found in plasma membrane fraction (PubMed:9165027). {ECO:0000250|UniProtKB:Q9JIF7, ECO:0000269|PubMed:8458872, ECO:0000269|PubMed:9165027}.
Interaction partners:
- Coatomer subunit beta'
- Coatomer subunit alpha
- Coatomer subunit gamma-1
- Coatomer subunit delta
- Coatomer subunit zeta
- Coatomer subunit epsilon
- ADP-ribosylation factor GTPase-activating protein 2
- Coatomer subunit gamma
- Coatomer subunit zeta
- ADP-ribosylation factor 1
Sequence:
MTAAENVCYTLINVPMDSEPPSEISLKNDLEKGDVKSKTEALKKVIIMILNGEKLPGLLMTIIRFVLPLQDHTIKKLLLVFWEIVPKTTPDGRLLHEMILVCDAYRKDLQHPNEFIRGSTLRFLCKLKEAELLEPLMPAIRACLEHRHSYVRRNAVLAIYTIYRNFENLIPDAPELIHDFLVNEKDASCKRNAFMMLIHADQDRALDYLSTCIDQVQTFGDILQLVIVELIYKVCHANPSERARFIRCIYNLLQSSSPAVKYEAAGTLVTLSSAPTAIKAAAQCYIDLIIKESDNNVKLIVLDRLVELKEHPAHERVLQDLVMDILRVLSTPDLEVRKKTLQLALDLVSSRNVEELVIVLKKEVIKTNNVSEHEDTDKYRQLLVRTLHSCSVRFPDMAANVIPVLMEFLSDSNEAAAADVLEFVREAIQRFDNLRMLIVEKMLEVFHAIKSVKIYRGALWILGEYCSTKEDIQSVMTEVRRSLGEIPIVESEIKKEAGELKPEEEITVGPVQKLVTEMGTYATQSALSSSRPTKKEEDRPPLRGFLLDGDFFVAASLATTLTKIALRYVALVQEKKKQNSFVAEAMLLMATILHLGKSSLPKKPITDDDVDRISLCLKVLSECSPLMNDIFNKECRQSLSQMLSAKLEEEKLSQKKESEKRNVTVQPDDPISFMQLTAKNEMNCKEDQFQLSLLAAMGNTQRKEAADPLASKLNKVTQLTGFSDPVYAEAYVHVNQYDIVLDVLVVNQTSDTLQNCTLELATLGDLKLVEKPSPLTLAPHDFANIKANVKVASTENGIIFGNIVYDVSGAASDRNCVVLSDIHIDIMDYIQPATCTDAEFRQMWAEFEWENKVTVNTNVTDLNDYLQHILKSTNMKCLTPEKALSGYCGFMAANLYARSIFGEDALANVSIEKPVHQGPDAAVTGHIRIRAKSQGMALSLGDKINLSQKKTSL