<Entry>
<Accession>Q9XTB5</Accession>
        <ProteinName>LEM</ProteinName>
        <GeneName>lem</GeneName>
        <OS_id>6239</OS_id>
        <ReferenceProteome>None</ReferenceProteome>
        <SubcellularLocation>
<Location>SL-0178</Location>
<Location>SL-0179</Location>
<Location>SL-0182</Location>
<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}.</Comments>
</SubcellularLocation>
<CrossReferences>
<CrossReference>
<Database>UNIPROT</Database>
<ID>Q9XTB5</ID>
</CrossReference>
<CrossReference>
<Database>Pfam</Database>
<ID>PF03020</ID>
</CrossReference>
<CrossReference>
<Database>PROSITE</Database>
<ID>PS50954</ID>
</CrossReference>
</CrossReferences>
<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}.</Function>
<Interactions>
<Interaction>
<Partner>O01971</Partner>
<IntAct>EBI-6260324</IntAct>
<Score>0.27</Score>
</Interaction>
<Interaction>
<Partner>Q21443</Partner>
<IntAct>EBI-2535415</IntAct>
<Score>0.53</Score>
</Interaction>
<Interaction>
<Partner>Q03565</Partner>
<IntAct>EBI-2535622</IntAct>
<Score>0.44</Score>
</Interaction>
</Interactions>
<OntologyTerms>
<Ontology>GO:0005694</Ontology>
<Ontology>GO:0005639</Ontology>
<Ontology>GO:0005635</Ontology>
<Ontology>GO:0031490</Ontology>
<Ontology>GO:0005521</Ontology>
<Ontology>GO:0051276</Ontology>
<Ontology>GO:0007059</Ontology>
<Ontology>GO:0031023</Ontology>
<Ontology>GO:0000281</Ontology>
<Ontology>GO:0030514</Ontology>
<Ontology>GO:0006998</Ontology>
<Ontology>GO:0031468</Ontology>
<Ontology>GO:1902531</Ontology>
<Ontology>GO:0010165</Ontology>
</OntologyTerms>
<Topology>
        <Type>Transmembrane</Type>
        <Source>UniProt</Source>
        <Annotation>Sequence Analysis {ECO:0000255}</Annotation>
        </Topology>
<Sequence>MVDVEKMSDAELRAELNVRGANVGPVTGTTRSLYEKKLKKLLSGGAKTPARPTVAKPAPKPTPKSAPAPKSPKSPPARRSIPRAAATAANSTINSTFNRSEIEEMSDSDDDMRDDDDDDEEILSPKSKQSSFRSANSTASSVGRGRPVSSTPNKRLSPVYKPSPVPKNTPRTTSSSSKTTINTTTTRIPSTPRRITSVPGLITDFTPSFSTFGSDRPGATPPRKSIYTSKVSKVLHDLGNTTGEEDDDDEFEGQETSRIIYKTEEPSRRGIVKNAWNKVLGYGFDASKNPGDSYDLRAGASRIRVQKNPRTGKVTVKQTNIFNEAIYFALYVILILFVVLGIAYALTTTHRPKTADFSGYWGVLKAAGRDSLNFFYNYAILPVVSLGIFVVLGAGIYFGHRKYKEAKEQEEAKLYELIERITELIRESSIDGDPYVSQPHVRDVLFPPAKRRSAELARWEQAVKFIDTNESRVATDVLVLPSGNECAVWKWIGNQSQKRW</Sequence>
        <SequenceLength>500</SequenceLength>
        </Entry>