The following text describes a protein:
Function:
Nuclear lamina-associated inner nuclear membrane protein that is involved in nuclear structure organization, maintenance of nuclear envelope (NE) integrity and NE reformation after mitosis. Plays a role as transmembrane adapter for the endosomal sorting complexes required for transport (ESCRT), and is thereby involved in ESCRT-mediated NE reformation. Promotes ESCRT-mediated NE closure by recruiting CHMP7 and downstream ESCRT-III proteins IST1/CHMP8 and CHMP2A to the reforming NE during anaphase. During nuclear reassembly, condenses into a liquid-like coating around microtubule spindles and coassembles with CHMP7 to form a macromolecular O-ring seal at the confluence between membranes, chromatin, and the spindle to facilitate early nuclear sealing. Plays a role in the organization of heterochromatin associated with the NE and in the maintenance of NE organization under mechanical stress (By similarity). Required for embryonic development and involved in regulation of several signaling pathways such as MAPK and AKT (By similarity). Required for myoblast differentiation involving regulation of ERK signaling (By similarity). Essential for cardiac homeostasis and proper heart function (By similarity).
Subcellular Localization:
Nucleus inner membrane; Multi-pass membrane protein. Nucleus envelope. Cytoplasm, cytoskeleton, spindle. Note=Lamina-associated protein residing in the inner nuclear membrane (INM) of the nuclear envelope (NE). The localization to the INM is dependent on LMNA. Evenly distributed around the NE during interphase. During metaphase, found in a reticular network. Recruited to the reforming NE on chromatin disks in early anaphase. In late anaphase, concentrates at the NE core proximal to spindle microtubules, and then broadening to a distributed nuclear rim pattern.
Domain:
The LEM domain is required for inner nuclear membrane (INM) localization and contains a BANF1 conserved binding motif which allows localization to chromatin. In late anaphase, as the reforming nuclear envelope (NE) surrounds the chromatin disk, both the LEM domain and the disordered regions are necessary for localization to the NE core; The disordered regions, also named low complexity domain, confer the ability to phase separate. In late anaphase, as the reforming nuclear envelope (NE) surrounds the chromatin disk, both the LEM domain and the disordered regions are necessary for localization to the NE core. During NE reformation, the proline-arginine-rich sequence within the disordered region binds microtubules, targeting LEM2 condensation to spindle microtubules traversing the nascent NE; The winged-helix (WH) region (residues 395-503) activates the ESCRT-II/ESCRT-III hybrid protein CHMP7 to form co-oligomeric rings around spindle microtubules to facilitate early nuclear sealing.
Sequence:
MAGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGEARLRDEERLREEARPRGEERLREEARLREDAPLRARPAAASPRAEPWLSQPASGSAYATPGAYGDIRPSAASWVGSRGLAYPARPAQLRRRASVRGSSEEDEDARTPDRATQGPGLAARRWWAASPAPARLPSSLLGPDPRPGLRATRAGPAGAARARPEVGRRLERWLSRLLLWASLGLLLVFLGILWVKMGKPSAPQEAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPENLKSKCIPVMEAQEYIANVTSSSSAKFEAALTWILSSNKDVGIWLKGEDQSELVTTVDKVVCLESAHPRMGVGCRLSRALLTAVTNVLIFFWCLAFLWGLLILLKYRWRKLEEEEQAMYEMVKKIIDVVQDHYVDWEQDMERYPYVGILHVRDSLIPPQSRRRMKRVWDRAVEFLASNESRIQTESHRVAGEDMLVWRWTKPSSFSDSER