{"metadata":{"accession":"PF12022","entry_id":null,"type":"repeat","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR024603","hierarchy":null,"name":{"name":"COG complex component, COG2, C-terminal","short":"COG2_C"},"description":[{"text":"<p>The COG complex comprises eight proteins (COG1-8) and plays critical roles in Golgi structure and function [[cite:PUB00012274]]. It is necessary for retrograde trafficking in the Golgi apparatus and for protein glycosylation [[cite:PUB00097774]]. COG complex, together with exocyst, Golgi-associated retrograde protein (GARP) and Dsl1 complexes, is a member of the CATHR (complexes associated with tethering containing helical rods) family sharing an evolutionary origin and structural features [[cite:PUB00100047]]. This domain represents the C-terminal of COG complex subunit 2 and consists of a conserved alpha-helical bundle. In Arabidopsis, COG2 forms a complex with FPP3/VETH1 and FPP2/VETH2 and ensures the correct secondary cell wall (SCW) deposition pattern by recruiting exocyst components to cortical microtubules in xylem cells during secondary cell wall deposition [[cite:PUB00097774]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00097774":{"PMID":25541219,"ISBN":null,"volume":"56","issue":"2","year":2015,"title":"Novel coiled-coil proteins regulate exocyst association with cortical microtubules in xylem cells via the conserved oligomeric golgi-complex 2 protein.","URL":null,"raw_pages":"277-86","medline_journal":"Plant Cell Physiol","ISO_journal":"Plant Cell Physiol","authors":["Oda Y","Iida Y","Nagashima Y","Sugiyama Y","Fukuda H."],"DOI_URL":null},"PUB00100047":{"PMID":34061181,"ISBN":null,"volume":"13","issue":"7","year":2021,"title":"Homology and Modular Evolution of CATCHR at the Origin of the Eukaryotic Endomembrane System.","URL":null,"raw_pages":null,"medline_journal":"Genome Biol Evol","ISO_journal":"Genome Biol Evol","authors":["Santana-Molina C","Gutierrez F","Devos DP."],"DOI_URL":null},"PUB00012274":{"PMID":11980916,"ISBN":null,"volume":"157","issue":"3","year":2002,"title":"Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function.","URL":null,"raw_pages":"405-15","medline_journal":"J Cell Biol","ISO_journal":"J. Cell Biol.","authors":["Ungar D","Oka T","Brittle EE","Vasile E","Lupashin VV","Chatterton JE","Heuser JE","Krieger M","Waters MG."],"DOI_URL":"http://dx.doi.org/10.1083/jcb.200202016"}},"set_info":{"accession":"CL0020","name":"TPR"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":68,"interactions":0,"matches":3267,"pathways":0,"proteins":3152,"proteomes":2247,"sets":1,"structural_models":{"alphafold":2684},"structures":0,"taxa":6622},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":68,"alignment:full":2492},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}