{"metadata":{"accession":"PF12053","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR021922","hierarchy":null,"name":{"name":"N-terminal of Par3 and HAL proteins","short":"Par3_HAL_N_term"},"description":[{"text":"<p>This domain is about 150 amino acids in length found associated with [pfam:PF00595] in eukaryotes. It has a conserved GILD sequence motif.  Family members have been found to be essential for cell polarity establishment and maintenance such as Par3 (partitioning defective) [swissprot:Q8TEW0] and involved in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine ammonia lyase (HAL) [swissprot:P42357]. This N-terminal domain is found to mediate oligomerization critical for the membrane localization of Par-3. It is also found to possess a self-association capacity via a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due to the absence of equivalent charged residues that are essential for the longitudinal packing of the Par-3 N-terminal domain filament [[cite:PUB00085056]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00085056":{"PMID":23643951,"ISBN":null,"volume":"21","issue":"6","year":2013,"title":"Structural insights into the intrinsic self-assembly of Par-3 N-terminal domain.","URL":null,"raw_pages":"997-1006","medline_journal":"Structure","ISO_journal":"Structure","authors":["Zhang Y","Wang W","Chen J","Zhang K","Gao F","Gao B","Zhang S","Dong M","Besenbacher F","Gong W","Zhang M","Sun F","Feng W."],"DOI_URL":"https://doi.org/10.1016/j.str.2013.04.004"}},"set_info":{"accession":"CL0072","name":"Ubiquitin"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":54,"interactions":0,"matches":5617,"pathways":0,"proteins":5578,"proteomes":1060,"sets":1,"structural_models":{"alphafold":2696},"structures":3,"taxa":3712},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":9,"alignment:full":4203},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}