Stannin

Stannins are small proteins that consist of a single transmembrane helix, an unstructured linker domain, and a cytoplasmic domain. The transmembrane region contains a conserved cysteine residue (Cys32) that, together with Cys34 found in the stannin unstructured linker domain, constitutes the putative trimethyltin-binding site, close to the lipid/solvent interface.[1]

Stannin
Identifiers
SymbolSNN_transmemb
PfamPF09049
InterProIPR015135
OPM superfamily47
OPM protein1zza
Membranome104

The unstructured protein region connects two adjacent helical domains. It contains a conserved CXC metal-binding motif and a putative 14-3-3-zeta binding domain. Upon coordinating dimethytin, considerable structural or dynamic changes in the flexible loop region of SNN may take place, recruiting other binding partners such as 14-3-3-zeta, and thereby initiating the apoptotic cascade.[1]

The cytoplasmic domain forms a distorted helix that is partially absorbed into the plane of the lipid bilayer. It interacts with the surface of the lipid bilayer, and contributes to the initiation of the apoptotic cascade on binding of the unstructured linker domain to dimethyltin.[1]

Human proteins containing this domain

SNN;

gollark: Anyway, adding more packages for basically-one-line tasks incurs costs.
gollark: More efficient than `x % 2 === 0`? Is that likely?
gollark: > I created this in 2014, when I was learning how to program. - literally on the github page for `is-even` and yet 110,720 weekly downloads
gollark: `is-even` actually depends on `is-odd`, and just uses that with the `!` operator.
gollark: `is-even` is popular too. It checks if a number is *even*.

References
  1. Mascioni A, Veglia G, Buck-Koehntop BA, Buffy JJ (2005). "Structure, dynamics, and membrane topology of stannin: a mediator of neuronal cell apoptosis induced by trimethyltin chloride". J. Mol. Biol. 354 (3): 652–65. doi:10.1016/j.jmb.2005.09.038. PMID 16246365.
This article incorporates text from the public domain Pfam and InterPro: IPR015136


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