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http://purl.uniprot.org/citations/10085102http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10085102http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10085102http://www.w3.org/2000/01/rdf-schema#comment"Major histocompatibility complex (MHC) class I molecules present antigenic peptides to CD8 T cells. The peptides are generated in the cytosol, then translocated across the membrane of the endoplasmic reticulum by the transporter associated with antigen processing (TAP). TAP is a trimeric complex consisting of TAP1, TAP2, and tapasin (TAP-A) as indicated for human cells by reciprocal coprecipitation with anti-TAP1/2 and anti-tapasin antibodies, respectively. TAP1 and TAP2 are required for the peptide transport. Tapasin is involved in the association of class I with TAP and in the assembly of class I with peptide. The mechanisms of tapasin function are still unknown. Moreover, there has been no evidence for a murine tapasin analogue, which has led to the suggestion that murine MHC class I binds directly to TAP1/2. In this study, we have cloned the mouse analogue of tapasin. The predicted amino acid sequence showed 78% identity to human tapasin with identical consensus sequences of signal peptide, N-linked glycosylation site, transmembrane domain and double lysine motif. However, there was less homology (47%) found at the predicted cytosolic domain, and in addition, mouse tapasin is 14 amino acids longer than the human analogue at the C terminus. This part of the molecule may determine the species specificity for interaction with MHC class I or TAP1/2. Like human tapasin, mouse tapasin binds both to TAP1/2 and MHC class I. In TAP2-mutated RMA-S cells, both TAP1 and MHC class I were coprecipitated by anti-tapasin antiserum indicative of association of tapasin with TAP1 but not TAP2. With crosslinker-modified peptides and purified microsomes, anti-tapasin coprecipitated both peptide-bound MHC class I and TAP1/2. In contrast, anti-calreticulin only coprecipitated peptide-free MHC class I molecules. This difference in association with peptide-loaded class I suggests that tapasin functions later than calreticulin during MHC class I assembly, and controls peptide loading onto MHC class I molecules in the endoplasmic reticulum."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.13.8649"xsd:string
http://purl.uniprot.org/citations/10085102http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.13.8649"xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/author"Wang P."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/author"Wang P."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/author"Paulsson K.M."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/author"Paulsson K.M."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/author"Sjoegren H.-O."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/author"Sjoegren H.-O."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/pages"8649-8654"xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/pages"8649-8654"xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/title"Peptide-bound major histocompatibility complex class I molecules associate with tapasin before dissociation from transporter associated with antigen processing."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/title"Peptide-bound major histocompatibility complex class I molecules associate with tapasin before dissociation from transporter associated with antigen processing."xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10085102http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10085102http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10085102
http://purl.uniprot.org/citations/10085102http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10085102
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