SAM (sterile alpha motif) domain of SAM_aveugle-like subfamily is a protein-protein interaction domain. In Drosophila, the aveugle (AVE) protein (also known as HYP (Hyphen)) is involved in normal photoreceptor differentiation, and required for epidermal growth factor receptor (EGFR) signaling between ras and raf genes during eye development and wing vein formation. SAM domain of the HYP(AVE) protein interacts with SAM domain of CNK, the multidomain scaffold protein connector enhancer of kinase suppressor of ras. CNK/HYP(AVE) complex interacts with KSR (kinase suppressor of Ras) protein. This interaction leads to stimulation of Ras-dependent Raf activation. This subfamily also includes vertebrate AVE homologs - Samd10 and Samd12 proteins. Their exact function is unknown, but they may play a role in signal transduction during embryogenesis.
Feature 1:heterodimer interface ML [polypeptide binding site]
Evidence:
Structure:3BS5; Drosophila/Human, SAM_HYP /SAM_CNK2 dimer, contacts at 4A.
Comment:The mid-loop (ML) surface of the SAM domain of HYP (or aveugle) Drosophila protein interacts with the end-helix (EH) surface of the SAM domain of human CNK2 protein.
Jiyao W et al.(2023). "The conserved domain database in 2023.",