Copb1
entrez
114023
canonical
uniprot
P23514
canonical
ensembl
ENSRNOG00000057623
resolver
ensembl
ENSRNOG00055006664
resolver
ensembl
ENSRNOG00060016885
resolver
ensembl
ENSRNOG00065028592
resolver
ensp
ENSRNOP00000072797
resolver
ensp
ENSRNOP00055008458
resolver
ensp
ENSRNOP00060023263
resolver
ensp
ENSRNOP00065040420
resolver
enst
ENSRNOT00000083293
resolver
enst
ENSRNOT00055010874
resolver
enst
ENSRNOT00060028892
resolver
enst
ENSRNOT00065049287
resolver
genesymbol
Copb1
resolver
genesymbol_syn
Copb
resolver
uniprot_entry
COPB_RAT
resolver
amino_acid_sequence
MTAAENVCYTLINVPMDSEPPSEISLKNDLEKGDVKSKTEALKKVIIMILNGEKLPGLLMTIIRFVLPLQDHTIKKLLLVFWEIVPKTTPDGRLLHEMILVCDAYRKDLQHPNEFIRGSTLRFLCKLKEAELLEPLMPAIRACLEHRHSYVRRNAVLAIYTIYRNFENLIPDAPELIHDFLVNEKDASCKRNAFMMLIHADQDRALDYLSTCIDQVQTFGDILQLVIVELIYKVCHANPSERARFIRCIYNLLQSSSPAVKYEAAGTLVTLSSAPTAIKAAAQCYIDLIIKESDNNVKLIVLDRLVELKEHPAHERVLQDLVMDILRVLSTPDLEVRKKTLQLALDLVSSRNVEELVIVLKKEVIKTNNVSEHEDTDKYRQLLVRTLHSCSVRFPDMAANVIPVLMEFLSDSNEAAAADVLEFVREAIQRFDNLRMLIVEKMLEVFHAIKSVKIYRGALWILGEYCSTKEDIQSVMTEVRRSLGEIPIVESEIKKEAGELKPEEEITVGPVQKLVTEMGTYATQSALSSSRPTKKEEDRPPLRGFLLDGDFFVAASLATTLTKIALRYVALVQEKKKQNSFVAEAMLLMATILHLGKSSLPKKPITDDDVDRISLCLKVLSECSPLMNDIFNKECRQSLSQMLSAKLEEEKLSQKKESEKRNVTVQPDDPISFMQLTAKNEMNCKEDQFQLSLLAAMGNTQRKEAADPLASKLNKVTQLTGFSDPVYAEAYVHVNQYDIVLDVLVVNQTSDTLQNCTLELATLGDLKLVEKPSPLTLAPHDFANIKANVKVASTENGIIFGNIVYDVSGAASDRNCVVLSDIHIDIMDYIQPATCTDAEFRQMWAEFEWENKVTVNTNVTDLNDYLQHILKSTNMKCLTPEKALSGYCGFMAANLYARSIFGEDALANVSIEKPVHQGPDAAVTGHIRIRAKSQGMALSLGDKINLSQKKTSL
uniprot
proteins
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. 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. {ECO:0000269|PubMed:17698811, ECO:0000269|PubMed:1957170, ECO:0000269|PubMed:20056612, ECO:0000269|PubMed:8376457}.
uniprot
proteins
mass_dalton
107011
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8. {ECO:0000250}.
uniprot
proteins
pubmed
10359600
uniprot
proteins
pubmed
10402461
uniprot
proteins
pubmed
12486083
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15749703
uniprot
proteins
pubmed
17698811
uniprot
proteins
pubmed
1840503
uniprot
proteins
pubmed
18556652
uniprot
proteins
pubmed
1957170
uniprot
proteins
pubmed
20056612
uniprot
proteins
pubmed
21545355
uniprot
proteins
pubmed
8376457
uniprot
proteins
pubmed
8458872
uniprot
proteins
pubmed
9165027
uniprot
proteins
pubmed
9360998
uniprot
proteins
sequence_length
953
uniprot
proteins
subcellular_location
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}.
uniprot
proteins