InterPro : IPR001322

Name  Lamin Tail Domain Short Name  Lamin_tail_dom
Type  Domain Description  Intermediate filaments (IF) are primordial components of the cytoskeleton and the nuclear envelope []. They generally form filamentous structures 8 to 14 nm wide. IF proteins are members of a very large multigene family of proteins which has been subdivided in five major subgroups, type I: acidic cytokeratins, type II: basic cytokeratins, type III: vimentin, desmin, glial fibrillary acidic protein (GFAP),peripherin, and plasticin, type IV: neurofilaments L, H and M, alpha-internexin and nestin, and type V: nuclear lamins A, B1, B2 and C. The lamins are components of thenuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membranethat may provide a framework for the nuclear envelope and may interact with chromatin.All IF proteins are structurally similar in that they consist of a central rod domain arranged in coiled-coil alpha-helices, with at least two short characteristic interruptions; a N-terminal non-helical domain (head) of variable length; and a C-terminaldomain (tail) which is also non-helical, and which shows extreme length variation between different IF proteins. The C-terminal domain has been characterised for the lamins [].The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in nuclear lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase, synaptojanin, and calcineurin-like phosphoesterase superfamilies [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

1 Found In

Id Name Short Name Type
IPR016451 Intermediate filament, ifa/ifb Intermed_filament_ifa/ifb Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Quinlan R Intermediate filament proteins. 1995 Protein Profile 2 795-952
Dhe-Paganon S Structure of the globular tail of nuclear lamin. 2002 J Biol Chem 277 17381-4
Mans BJ Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex. 2004 Cell Cycle 3 1612-37



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)