ID  Q9XTB5;
PN  LEM protein 2;
GN  lem;
OS  6239;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0179;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus inner membrane {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:12684533}; Multi-pass membrane protein {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:12684533}; Nucleoplasmic side {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:21176223, ECO:0000269|PubMed:25653391, ECO:0000269|PubMed:32271860}. Chromosome {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:25653391, ECO:0000269|PubMed:32271860}. Note=Remains in the nuclear envelope until mid-late anaphase and reassociates with the chromatin periphery at telophase (PubMed:10982402). Recruited to the reforming nuclear envelope initially at the apical surfaces of chromatin, from where it spreads to the lateral surfaces facing the spindle microtubules (PubMed:25653391). Requires mel-28 for chromatin reassociation after mitosis and for nuclear envelope localization (PubMed:16950114). In meiosis at anaphase II, appears on the chromatin surface farthest from the extruding polar body (PubMed:32271860). After anaphase II, forms a plaque on the oocyte-derived pronucleus adjacent to the meiotic spindle (PubMed:32271860). Later disperses into a uniform rim around the oocyte-derived pronucleus (PubMed:32271860). {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:25653391, ECO:0000269|PubMed:32271860}.
DR  UNIPROT: Q9XTB5;
DR  Pfam: PF03020;
DR  PROSITE: PS50954;
DE  Function: Nuclear lamina-associated inner nuclear membrane protein that is involved in cell division, nuclear structure organization, maintenance of nuclear envelope integrity and nuclear envelope reformation after mitosis (PubMed:12684533, PubMed:21176223, PubMed:22171324, PubMed:25653391, PubMed:32271860). In interphase cells, plays a role in anchoring and spatial arrangement of chromosome arms at the nuclear periphery, forming so-called lem-2 subdomains (PubMed:21176223). Both arms of autosomes but only the left arm of the X chromosome are anchored in lem-2 subdomains; sequences bound by lem-2 are mainly repetitive chromosome sequences and inactive genes (PubMed:21176223). Involved in chromosome segregation and cell division, probably via its interaction with the nuclear intermediate filament protein lmn-1, the main component of nuclear lamina (PubMed:12684533). Required to organize the distribution of lmn-1, nuclear pore complexes (NPCs) and chromatin in mitotically active cells (PubMed:22171324). Involved in the nuclear positioning and efficient anchoring of microtubule-organizing centers (MTOCs) to the nuclear envelope during mitosis as well as on maintaining correct nuclear morphology (PubMed:25653391). Contributes to closure of nuclear envelope (NE) holes and prevents excess nuclear membranes after meiosis and mitosis (PubMed:32271860). Together with emr-1, plays a role in baf-1 enrichment at the nuclear envelope in anaphase (PubMed:12684533). Together with emr-1, involved in muscle cell attachment to hypodermal cells, as well as muscle cell location and sarcomere organization (PubMed:22171324). May play a role in radiation-induced DNA damage repair response (PubMed:22383942). {ECO:0000269|PubMed:12684533, ECO:0000269|PubMed:21176223, ECO:0000269|PubMed:22171324, ECO:0000269|PubMed:22383942, ECO:0000269|PubMed:25653391, ECO:0000269|PubMed:32271860}.
DE  Reference Proteome: Yes;
DE  Interaction: O01971; IntAct: EBI-6260324; Score: 0.27
DE  Interaction: Q21443; IntAct: EBI-2535415; Score: 0.53
DE  Interaction: Q03565; IntAct: EBI-2535622; Score: 0.44
GO  GO:0005694;
GO  GO:0005639;
GO  GO:0005635;
GO  GO:0031490;
GO  GO:0005521;
GO  GO:0051276;
GO  GO:0007059;
GO  GO:0031023;
GO  GO:0000281;
GO  GO:0030514;
GO  GO:0006998;
GO  GO:0031468;
GO  GO:1902531;
GO  GO:0010165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MVDVEKMSDAELRAELNVRGANVGPVTGTTRSLYEKKLKKLLSGGAKTPARPTVAKPAPKPTPKSAPAPKSPKSPPARRS
SQ  IPRAAATAANSTINSTFNRSEIEEMSDSDDDMRDDDDDDEEILSPKSKQSSFRSANSTASSVGRGRPVSSTPNKRLSPVY
SQ  KPSPVPKNTPRTTSSSSKTTINTTTTRIPSTPRRITSVPGLITDFTPSFSTFGSDRPGATPPRKSIYTSKVSKVLHDLGN
SQ  TTGEEDDDDEFEGQETSRIIYKTEEPSRRGIVKNAWNKVLGYGFDASKNPGDSYDLRAGASRIRVQKNPRTGKVTVKQTN
SQ  IFNEAIYFALYVILILFVVLGIAYALTTTHRPKTADFSGYWGVLKAAGRDSLNFFYNYAILPVVSLGIFVVLGAGIYFGH
SQ  RKYKEAKEQEEAKLYELIERITELIRESSIDGDPYVSQPHVRDVLFPPAKRRSAELARWEQAVKFIDTNESRVATDVLVL
SQ  PSGNECAVWKWIGNQSQKRW
//