{"metadata":{"accession":"PF04258","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR064098","hierarchy":null,"name":{"name":"Signal peptide peptidase","short":"Peptidase_A22B"},"description":[{"text":"<p>The members of this family are membrane proteins. In some proteins this region is found associated with [pfam:PF02225]. This family corresponds with Merops subfamily A22B, the type example of which is signal peptide peptidase. There is a sequence-similarity relationship with [pfam:PF01080].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Signal_peptide_peptidase","extract":"<p>In molecular biology, the <b>Signal Peptide Peptidase</b> (SPP) is a type of protein that specifically cleaves parts of other proteins. It is an intramembrane aspartyl protease with the conserved active site motifs 'YD' and 'GxGD' in adjacent transmembrane domains (TMDs). Its sequences is highly conserved in different vertebrate species. SPP cleaves remnant signal peptides left behind in membrane by the action of signal peptidase and also plays key roles in immune surveillance and the maturation of certain viral proteins.</p>","thumbnail":null}],"literature":{"PUB00020020":{"PMID":12077416,"ISBN":null,"volume":"296","issue":"5576","year":2002,"title":"Identification of signal peptide peptidase, a presenilin-type aspartic protease.","URL":null,"raw_pages":"2215-8","medline_journal":"Science","ISO_journal":"Science","authors":["Weihofen A","Binns K","Lemberg MK","Ashman K","Martoglio B."],"DOI_URL":"http://dx.doi.org/10.1126/science.1070925"},"PUB00020022":{"PMID":11714810,"ISBN":null,"volume":"167","issue":"11","year":2001,"title":"Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes.","URL":null,"raw_pages":"6441-6","medline_journal":"J Immunol","ISO_journal":"J. Immunol.","authors":["Lemberg MK","Bland FA","Weihofen A","Braud VM","Martoglio B."],"DOI_URL":"http://www.jimmunol.org/cgi/content/full/167/11/6441"},"PUB00020019":{"PMID":12145199,"ISBN":null,"volume":"21","issue":"15","year":2002,"title":"Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets.","URL":null,"raw_pages":"3980-8","medline_journal":"EMBO J","ISO_journal":"EMBO J.","authors":["McLauchlan J","Lemberg MK","Hope G","Martoglio B."],"DOI_URL":"http://dx.doi.org/10.1093/emboj/cdf414"},"PUB00020017":{"PMID":12419218,"ISBN":null,"volume":"10","issue":"4","year":2002,"title":"Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis.","URL":null,"raw_pages":"735-44","medline_journal":"Mol Cell","ISO_journal":"Mol. Cell","authors":["Lemberg MK","Martoglio B."],"DOI_URL":"http://dx.doi.org/10.1016/S1097-2765(02)00655-X"}},"set_info":{"accession":"CL0130","name":"Peptidase_AD"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":192,"interactions":0,"matches":14137,"pathways":0,"proteins":13660,"proteomes":3348,"sets":1,"structural_models":{"alphafold":11659},"structures":2,"taxa":8908},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":14,"alignment:full":10629},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}