SAM (sterile alpha motif) domain of SAM_Atherin and Atherin-like subfamily proteins is a putative protein-protein and/or protein-lipid interaction domain. In addition to the C-terminal SAM domain, the majority of proteins belonging to this group also have PHD (or Zn finger) domain. As potential members of the polycomb group, these proteins may be involved in regulation of some key regulatory genes during development. Atherin can be recruited by Ruk/CIN85 kinase-binding proteins via its SH3 domains thus participating in the signal transferring kinase cascades. Also, atherin was found associated with low density lipids (LDL) in atherosclerotic lesions in human. It was suggested that atherin plays an essential role in atherogenesis via immobilization of LDL in the arterial wall. SAM domains of atherins are predicted to form polymers. Inhibition of polymer formation could be a potential antiatherosclerotic therapy.
Feature 1:putative oligomer interface ML [polypeptide binding site]
Evidence:
Comment:The mid-loop (ML) surface of the SAM domain of Ph protein interacts with the end-helix (EH) surface of the SAM domain of Scm protein forming heterodimers.
Comment:SAM domains of Scm and Ph proteins can form head-to-tail homooligomers via interactions between the mid-loop (ML) and end-helix (EH) surfaces.
Jiyao W et al.(2023). "The conserved domain database in 2023.",