EC Number   |
General Information |
Reference |
|---|
   7.4.2.14 | evolution |
human TAP and rat TAPa translocate peptides with hydrophobic and basic C termini, whereas mouse TAP and rat TAPu prefer peptides with hydrophobic C-termini. This pattern correlates with the predominant peptide binding profiles of mouse and human class I molecules |
-, 762003 |
| 7.4.2.14 | evolution |
TAP is a member of the ATP-binding cassette (ABC) family of transmembrane transport proteins |
761450 |
| 7.4.2.14 | evolution |
TAP1 and TAP2 are members of the ABC transporter family |
761417 |
| 7.4.2.14 | evolution |
TAP1 and TAP2 are members of the ATP-binding cassette family of membrane transIocators |
-, 760824 |
| 7.4.2.14 | evolution |
TAP1 and TAP2 belong to the ATP-binding cassette (ABC) transporter family |
761233 |
| 7.4.2.14 | evolution |
the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All avian TAP complexes can assemble chimeric PLC with subunits originating from different taxa. The transmembrane domain (TMD)0 of avian TAP2 is essential and sufficient for mediating the interaction with human tapasin, because all avian TAP1 subunits sequenced so far lack a TMD0, in analogy to human core-TAP1. The dimerization interface between avian and human TAP1 and TAP2 is complementary over a long distance in evolution. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates. Avian TAP complexes are functional but not across taxa |
761450 |
| 7.4.2.14 | evolution |
the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All avian TAP complexes can assemble chimeric PLC with subunits originating from different taxa. The transmembrane domain (TMD)0 of avian TAP2 is essential and sufficient for mediating the interaction with human tapasin, because all avian TAP1 subunits sequenced so far lack a TMD0, in analogy to human core-TAP1. The dimerization interface between avian and human TAP1 and TAP2 is complementary over a long distance in evolution. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates. Avian TAP complexes are functional but not across taxa. Chicken TAP1 is only functional in combination with avian TAP2 and not with endogenous or overexpressed human TAP2 |
761450 |
| 7.4.2.14 | evolution |
the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates |
761450 |
| 7.4.2.14 | evolution |
the assembly of TAP1, TAP2, and tapasin is conserved across mammals and birds, analysis using recombinant enzymes, overview. The dimerization interface between avian and human TAP1 and TAP2 is complementary over a long distance in evolution. All TAP complexes are capable to assemble the peptide-loading complex via specific recruitment of tapasin, indicating that the modules required for assembly of the peptide-loading complex are conserved in evolution across different classes of jawed vertebrates |
761450 |
| 7.4.2.14 | evolution |
the enzyme belongs to the ABC transporters, which have a conserved architecture of two transmembrane domains (TMDs) and two cytosolic nucleotide-binding domains (NBD). These domains can be expressed individually or can be arranged on a single polypeptide chain. While the TMDs of ABC import and export systems show diversity in their structural organization, the NBDs are highly conserved. The species-dependent differences in substrate specificity correlate with the epitope repertoire presented by MHC class I molecules, reflecting a co-evolution of TAP, MHC, and the T-cell receptor |
760660 |
