EMR1_CAEEL
ID EMR1_CAEEL Reviewed; 166 AA.
AC O01971;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Emerin homolog 1;
DE AltName: Full=Ce-emerin;
GN Name=emr-1; ORFNames=M01D7.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=10982402; DOI=10.1091/mbc.11.9.3089;
RA Lee K.K., Gruenbaum Y., Spann P., Liu J., Wilson K.L.;
RT "C. elegans nuclear envelope proteins emerin, MAN1, lamin, and nucleoporins
RT reveal unique timing of nuclear envelope breakdown during mitosis.";
RL Mol. Biol. Cell 11:3089-3099(2000).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INTERACTION WITH LMN-1.
RX PubMed=11870211; DOI=10.1242/jcs.115.5.923;
RA Gruenbaum Y., Lee K.K., Liu J., Cohen M., Wilson K.L.;
RT "The expression, lamin-dependent localization and RNAi depletion phenotype
RT for emerin in C. elegans.";
RL J. Cell Sci. 115:923-929(2002).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12490171; DOI=10.1016/s1047-8477(02)00516-6;
RA Cohen M., Tzur Y.B., Neufeld E., Feinstein N., Delannoy M.R., Wilson K.L.,
RA Gruenbaum Y.;
RT "Transmission electron microscope studies of the nuclear envelope in
RT Caenorhabditis elegans embryos.";
RL J. Struct. Biol. 140:232-240(2002).
RN [5]
RP FUNCTION, INTERACTION WITH LMN-1 AND BAF-1, AND DISRUPTION PHENOTYPE.
RX PubMed=12684533; DOI=10.1073/pnas.0730821100;
RA Liu J., Lee K.K., Segura-Totten M., Neufeld E., Wilson K.L., Gruenbaum Y.;
RT "MAN1 and emerin have overlapping function(s) essential for chromosome
RT segregation and cell division in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4598-4603(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16950114; DOI=10.1016/j.cub.2006.06.067;
RA Galy V., Askjaer P., Franz C., Lopez-Iglesias C., Mattaj I.W.;
RT "MEL-28, a novel nuclear-envelope and kinetochore protein essential for
RT zygotic nuclear-envelope assembly in C. elegans.";
RL Curr. Biol. 16:1748-1756(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20714352; DOI=10.1371/journal.pgen.1001060;
RA Fakhouri T.H., Stevenson J., Chisholm A.D., Mango S.E.;
RT "Dynamic chromatin organization during foregut development mediated by the
RT organ selector gene PHA-4/FoxA.";
RL PLoS Genet. 6:0-0(2010).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22171324; DOI=10.1091/mbc.e11-06-0505;
RA Barkan R., Zahand A.J., Sharabi K., Lamm A.T., Feinstein N., Haithcock E.,
RA Wilson K.L., Liu J., Gruenbaum Y.;
RT "Ce-emerin and LEM-2: essential roles in Caenorhabditis elegans
RT development, muscle function, and mitosis.";
RL Mol. Biol. Cell 23:543-552(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22383942; DOI=10.1371/journal.pone.0024555;
RA Dittrich C.M., Kratz K., Sendoel A., Gruenbaum Y., Jiricny J.,
RA Hengartner M.O.;
RT "LEM-3 - a LEM domain containing nuclease involved in the DNA damage
RT response in C. elegans.";
RL PLoS ONE 7:E24555-E24555(2012).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25653391; DOI=10.1242/jcs.164202;
RA Morales-Martinez A., Dobrzynska A., Askjaer P.;
RT "Inner nuclear membrane protein LEM-2 is required for correct nuclear
RT separation and morphology in C. elegans.";
RL J. Cell Sci. 128:1090-1096(2015).
CC -!- FUNCTION: Nuclear lamina-associated inner nuclear membrane protein that
CC is involved in cell division, nuclear structure organization,
CC maintenance of nuclear envelope integrity and nuclear envelope
CC reformation after mitosis (PubMed:11870211, PubMed:12684533,
CC PubMed:22171324). Involved in chromosome segregation and cell division,
CC probably via its interaction with the nuclear intermediate filament
CC protein lmn-1, the main component of nuclear lamina (PubMed:11870211,
CC PubMed:12684533). Required to organize the distribution of lmn-1,
CC nuclear pore complexes (NPCs) and chromatin in mitotically active cells
CC (PubMed:22171324). Together with lem-2, plays a role in baf-1
CC enrichment at the nuclear envelope in anaphase (PubMed:12684533).
CC Together with lem-2, involved in muscle cell attachment to hypodermal
CC cells, as well as muscle cell location and sarcomere organization
CC (PubMed:22171324). May play a role in radiation-induced DNA damage
CC repair response (PubMed:22383942). May repress binding of transcription
CC factor pha-4 with target sequences in pharyngeal cells.
CC {ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12684533,
CC ECO:0000269|PubMed:20714352, ECO:0000269|PubMed:22171324,
CC ECO:0000269|PubMed:22383942}.
CC -!- SUBUNIT: Interacts with lmn-1 and baf-1. {ECO:0000269|PubMed:11870211,
CC ECO:0000269|PubMed:12684533}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211,
CC ECO:0000269|PubMed:12490171}; Single-pass membrane protein
CC {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211,
CC ECO:0000269|PubMed:12490171}; Nucleoplasmic side
CC {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211,
CC ECO:0000269|PubMed:12490171}. Nucleus envelope
CC {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:25653391}. Note=Lmn-1
CC and mel-28 are required for its localization to the nuclear envelope
CC (PubMed:11870211, PubMed:16950114). Remains in the nuclear envelope
CC until mid-late anaphase (PubMed:10982402). Recruited to the reforming
CC nuclear envelope from telophase and throughout interphase
CC (PubMed:25653391). {ECO:0000269|PubMed:10982402,
CC ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:16950114,
CC ECO:0000269|PubMed:25653391}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:11870211, PubMed:25653391).
CC Expressed in all cells, except in cells undergoing spermatogenesis
CC (PubMed:11870211). High expression in hypodermis, neurons, pharyngeal
CC muscle, body wall muscle and gonadal sheath (PubMed:25653391).
CC {ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:25653391}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the development and in
CC adults. {ECO:0000269|PubMed:11870211}.
CC -!- DISRUPTION PHENOTYPE: Mild increase in embryonic lethality of progeny
CC of X-ray-irradiated adults (PubMed:22383942). Slightly more spherical
CC nuclei (PubMed:25653391). Simultaneous knockout of emr-1 and lem-2
CC leads to embryonic lethality, 8.5% shorter animals in larval stage L2,
CC abnormal gonads and a developmental stop at late L2/early L3
CC (PubMed:22171324). Missing cell divisions in the postembryonic
CC mesodermal lineage and failure to produce any of the differentiated M
CC lineage cells (PubMed:22171324). Defects in the organization of
CC chromatin, nuclear intermediate filaments, and nuclear pore complexes
CC (NPCs), and defects in mitosis in cells that continue to divide after
CC embryogenesis (PubMed:22171324). In the mitotic zone of the gonad, lmn-
CC 1 and NPCs are mislocalized and nuclei are misshaped (PubMed:22171324).
CC Misshaped nuclei with large lmn-1 aggregates, clustered NPCs and
CC condensed chromatin in somatic hypodermal cells (PubMed:22171324).
CC Defects in motility, sarcomere organization, and muscle attachment to
CC hypodermis (PubMed:22171324). Decreased motility and near paralysis at
CC day 6 (PubMed:22171324). Disorganized thin and thick filaments of
CC sarcomeres and abnormally positioned muscles at day 3 and 6
CC (PubMed:22171324). Decreased pumping rate of the pharynx
CC (PubMed:22171324). RNAi-mediated knockdown causes an increase in the
CC number of nuclei with pha-4 bound to the pax-1 promoter; observed in
CC pharyngeal but not intestinal cells (PubMed:20714352). Simultaneous
CC RNAi-mediated knockdown of lem-2 and emr-1 causes anaphase chromatin
CC bridges and redistribution of baf-1 from the nuclear periphery to the
CC segregating chromatin during anaphase (PubMed:12684533).
CC {ECO:0000269|PubMed:12684533, ECO:0000269|PubMed:20714352,
CC ECO:0000269|PubMed:22171324, ECO:0000269|PubMed:22383942,
CC ECO:0000269|PubMed:25653391}.
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DR EMBL; FO080941; CCD67954.1; -; Genomic_DNA.
DR PIR; T15287; T15287.
DR RefSeq; NP_490907.1; NM_058506.5.
DR AlphaFoldDB; O01971; -.
DR SMR; O01971; -.
DR BioGRID; 37242; 3.
DR IntAct; O01971; 1.
DR STRING; 6239.M01D7.6.1; -.
DR iPTMnet; O01971; -.
DR EPD; O01971; -.
DR PaxDb; O01971; -.
DR PeptideAtlas; O01971; -.
DR EnsemblMetazoa; M01D7.6.1; M01D7.6.1; WBGene00001309.
DR EnsemblMetazoa; M01D7.6.2; M01D7.6.2; WBGene00001309.
DR GeneID; 171752; -.
DR KEGG; cel:CELE_M01D7.6; -.
DR UCSC; M01D7.6.1; c. elegans.
DR CTD; 171752; -.
DR WormBase; M01D7.6; CE12270; WBGene00001309; emr-1.
DR eggNOG; ENOG502QWCI; Eukaryota.
DR GeneTree; ENSGT00940000154098; -.
DR HOGENOM; CLU_1429189_0_0_1; -.
DR InParanoid; O01971; -.
DR OMA; DCEESMR; -.
DR OrthoDB; 886655at2759; -.
DR PRO; PR:O01971; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001309; Expressed in embryo and 4 other tissues.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IDA:WormBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005521; F:lamin binding; IPI:WormBase.
DR GO; GO:0007059; P:chromosome segregation; IGI:WormBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IGI:WormBase.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:UniProtKB.
DR GO; GO:0010165; P:response to X-ray; IMP:WormBase.
DR Gene3D; 1.10.720.40; -; 1.
DR InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR InterPro; IPR003887; LEM_dom.
DR Pfam; PF03020; LEM; 1.
DR SMART; SM00540; LEM; 1.
DR SUPFAM; SSF63451; SSF63451; 1.
DR PROSITE; PS50954; LEM; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Membrane; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..166
FT /note="Emerin homolog 1"
FT /id="PRO_0000206143"
FT TOPO_DOM 1..127
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..166
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT DOMAIN 1..44
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT REGION 62..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 166 AA; 18118 MW; 9D649883FFDEBE15 CRC64;
MDVSQLTDAE LRDSLKSHGV SVGPIVATTR KLYEKKLIKL SDGSINNQSN LNDSQFNEDS
LIISSSPKKS PPQRVFQNVS AATAAATTSP ESDSDDCEES MRYLTEEEMA ADRASARQAQ
SNKGGFLGST ITFTILFVFI AVFAYFLIEN AEQLKLVAET NPEDTI
