ID  Q6DVA0;
PN  LEM domain-containing protein 2;
GN  Lemd2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17062158}; Multi-pass membrane protein {ECO:0000269|PubMed:16339967}. Nucleus envelope {ECO:0000250|UniProtKB:Q8NC56}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NC56}. Note=Lamina-associated protein residing in the inner nuclear membrane (INM) of the nuclear envelope (NE) (PubMed:16339967). The localization to the INM is dependent on LMNA (By similarity). Evenly distributed around the NE during interphase (PubMed:16339967). During metaphase, found in a reticular network (By similarity). Recruited to the reforming NE on chromatin disks in early anaphase (By similarity). In late anaphase, concentrates at the NE core proximal to spindle microtubules, and then broadening to a distributed nuclear rim pattern (By similarity). {ECO:0000250|UniProtKB:Q8NC56, ECO:0000269|PubMed:16339967}.
DR  UNIPROT: Q6DVA0;
DR  UNIPROT: Q8C4H8;
DR  UNIPROT: Q8R0N2;
DR  Pfam: PF03020;
DR  Pfam: PF09402;
DR  PROSITE: PS50954;
DE  Function: Nuclear lamina-associated inner nuclear membrane protein that is involved in nuclear structure organization and maintenance of nuclear structure integrity and nuclear envelope reformation after mitosis (PubMed:16339967). Plays a role as transmembrane adapter for the endosomal sorting complexes required for transport (ESCRT), and is thereby involved in ESCRT-mediated nuclear envelope reformation (By similarity). Promotes ESCRT-mediated nuclear envelope closure by recruiting CHMP7 and downstream ESCRT-III proteins IST1/CHMP8 and CHMP2A to the reforming NE during anaphase (By similarity). 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 (By similarity). Required for embryonic development and is involved in regulation of several signaling pathways such as MAPK and AKT (PubMed:25790465). Required for myoblast differentiation involving regulation of ERK signaling (PubMed:17062158, PubMed:19720741). {ECO:0000250|UniProtKB:Q8NC56, ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19720741, ECO:0000269|PubMed:25790465}.
DE  Reference Proteome: Yes;
DE  Interaction: Q8VI24; IntAct: EBI-26885060; Score: 0.35
GO  GO:0000785;
GO  GO:0005783;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0031965;
GO  GO:0005819;
GO  GO:0031490;
GO  GO:0060914;
GO  GO:0030514;
GO  GO:0043409;
GO  GO:0051898;
GO  GO:0022008;
GO  GO:0006998;
GO  GO:0071168;
GO  GO:0035914;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAGLSDLELRRELQALGFQPGPITDTTRNVYRNKLRRLRGEARLRDDERLREDAGPREDAGPRGPERQREEARLREEAPL
SQ  RARPAASVLRSEPWPLSPSPPAPSAASDASGPYGNFGASASPWAASRGLSYPPHAGPGPLRRRASVRGSSEDDEDTRTPD
SQ  RHAPGRGRHWWAPPSASARPHSALLGADARPGLKGSRTGSAGAGRTRPEVGRWLERCLSRLLLWASLGLLLGFLAILWVK
SQ  MGKPSAPQEAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPEKLKSKCIPVLEAQEYIANV
SQ  TSSPSSRFKAALTWILSSNKDVGIWLKGEDPSELATTVDKVVCLESARPRMGIGCRLSRALLTAVTHVLIFFWCLAFLWG
SQ  LLILLKYRWRKLEEEEQAMYEMVKKIIDVVQDHYVDWEQDMERYPYVGILHVRDSLIPPQSRRRMKRVWDRAVEFLASNE
SQ  SRIQTESHRVAGEDMLVWRWTKPSSFSDSER
//