pfam11989: Dsl1_C (This model is not part of the current CDD release)
Retrograde transport protein Dsl1 C terminal
Dsl1 is a peripheral membrane protein required for transport between the Golgi and the endoplasmic reticulum. It is localised to the ER membrane, and in vitro it specifically binds to coatomer, the major component of the protein coat of COPI vesicles. Binding sites for coatomer are found on a disorganised region between the C and N termini of Dsl1. The C terminal domain is involved in binding to the Sec39 subunit of the Dsl1p complex. The N terminal complexes with another subunit of the Dsl1p complex called Tip20 which forms heterodimers by pairing the N termini of each protein. It is a component of DSL1 complex, which, together with the exocyst, conserved oligomeric Golgi (COG) and Golgi-associated retrograde protein (GARP), are part of the complexes associated with tethering containing helical rods (CATCHR) family, sharing an evolutionary origin and structure organisation. This domain has an alpha-helical bundle fold.
Jiyao W et al.(2023). "The conserved domain database in 2023.",