Protein Domain : Schwannomin interacting protein 1, C-terminal IPR015649

Type	Domain
Description	SCHIP-1 is a coiled-coil protein that specifically associates with schwannomin in vitro and in vivo. The product of the neurofibromatosis type 2 (NF2) tumour suppressor gene, known as schwannomin or merlin, is involved in NF2-associated and sporadic schwannomas and meningiomas. It is closely related to the ezrin-radixin-moesin family members, which link membrane proteins to the cytoskeleton. Association with SCHIP-1 can be observed only with some naturally occurring mutants of schwannomin, or a schwannomin spliced isoform lacking exons 2 and 3, but not with the schwannomin isoform exhibiting growth-suppressive activity [ ].This entry represents the C-terminal domain of mammalian SCHIP-1. This domain contains a leucine zipper coiled-coil structure implicated in their dimerization [ ]. This domain is also found in its isoforms such as IQCJ-SCHIP-1 (IQ motif containing J-Schwannomin-Interacting Protein 1). The N-terminal part of IQCJ-SCHIP-1 possesses an additional IQ motif, which typically serves as a Ca2+-independent CaM-binding site [].
Short Name	SCHIP_1_C