UniProt functional annotation for Q9JIF7



	UniProt functional annotation for Q9JIF7

UniProt code: Q9JIF7.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

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 (By similarity). Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. 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:17698811, ECO:0000269|PubMed:19067489}.

Subunit: Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits (By similarity). Interacts with CAPN8. Interacts with SCYL1 and PRKCE (By similarity). Interacts with COPG1 (By similarity). Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes (By similarity). Interacts (via trunk domain) with ARF1 (via switch I region); the interaction is direct (By similarity). Interacts with KCNK2 (via N-terminus); this interaction increases the channel-mediated whole cell currents and promotes plasma membrane expression of KCNK2 (By similarity). Interacts with STX17 (By similarity). Interacts with TMEM115 (By similarity). Interacts with TMEM41B (By similarity). {ECO:0000250|UniProtKB:P23514, ECO:0000250|UniProtKB:P53618}.

Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P23514}. Golgi apparatus membrane {ECO:0000269|PubMed:16476741, ECO:0000269|PubMed:19587158, ECO:0000269|PubMed:7593324}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53618}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:7593324}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P53618}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:7593324}. 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 (PubMed:16476741). 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 (By similarity). {ECO:0000250|UniProtKB:P23514, ECO:0000269|PubMed:16476741}.

Tissue specificity: Predominantly expressed in the upper one-third of the oxyntic mucosa and in most regions of the pyloric mucosa (PubMed:16476741). Ubiquitously expressed including platelet, liver, heart, spleen, lung and kidney (PubMed:11441537). {ECO:0000269|PubMed:11441537, ECO:0000269|PubMed:16476741}.

Ptm: Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.

Miscellaneous: Brefeldin A induces dissociation from the Golgi of the beta-COP and presumably the other coatomer subunits.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



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 (By similarity). Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. 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:17698811, ECO:0000269\|PubMed:19067489}.


Subunit:		Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits (By similarity). Interacts with CAPN8. Interacts with SCYL1 and PRKCE (By similarity). Interacts with COPG1 (By similarity). Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes (By similarity). Interacts (via trunk domain) with ARF1 (via switch I region); the interaction is direct (By similarity). Interacts with KCNK2 (via N-terminus); this interaction increases the channel-mediated whole cell currents and promotes plasma membrane expression of KCNK2 (By similarity). Interacts with STX17 (By similarity). Interacts with TMEM115 (By similarity). Interacts with TMEM41B (By similarity). {ECO:0000250\|UniProtKB:P23514, ECO:0000250\|UniProtKB:P53618}.
Subcellular location:		Cytoplasm {ECO:0000250\|UniProtKB:P23514}. Golgi apparatus membrane {ECO:0000269\|PubMed:16476741, ECO:0000269\|PubMed:19587158, ECO:0000269\|PubMed:7593324}; Peripheral membrane protein {ECO:0000250\|UniProtKB:P53618}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269\|PubMed:7593324}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000250\|UniProtKB:P53618}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269\|PubMed:7593324}. 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 (PubMed:16476741). 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 (By similarity). {ECO:0000250\|UniProtKB:P23514, ECO:0000269\|PubMed:16476741}.
Tissue specificity:		Predominantly expressed in the upper one-third of the oxyntic mucosa and in most regions of the pyloric mucosa (PubMed:16476741). Ubiquitously expressed including platelet, liver, heart, spleen, lung and kidney (PubMed:11441537). {ECO:0000269\|PubMed:11441537, ECO:0000269\|PubMed:16476741}.
Ptm:		Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.
Miscellaneous:		Brefeldin A induces dissociation from the Golgi of the beta-COP and presumably the other coatomer subunits.