| Description | This superfamily represents a structural domain with a complex fold consisting of several coiled β-sheets. This domain exists as a duplication, consisting of a tandem repeat of two similar structural motifs. This entry represents copies of this structural motif in the following protein families:Mss4, which contains a zinc-binding site.Translationally controlled tumour-associated protein TCTP, which contains an insertion of an α-helix hairpin, and which lacks a zinc-binding site.Mss4 is a conserved accessory factor for Rab GTPases, which function as ubiquitous regulators of intracellular membrane trafficking [ ]. Mss4 acts to promote nucleotide release from exocytic but not endocytic Rab GTPases. Mss4 has a complex fold made of several coiled β-sheets, and consists of a duplication of tandem repeats of two similar structural motifs. It contains a zinc-binding site.Other proteins that show structural similarity to Mss4 include the translationally controlled tumour-associated proteins TCTPs, which contain an insertion of an α helical hairpin, and lack the zinc-binding site. TCTPs are a highly conserved and abundantly expressed family of eukaryotic proteins that are implicated in both cell growth and the human acute allergic response [ ]. | Name | Mss4/translationally controlled tumour-associated TCTP |
| Short Name | Mss4/transl-control_tumour | Type | Homologous_superfamily |
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