EMD_MOUSE
ID EMD_MOUSE Reviewed; 259 AA.
AC O08579; Q3TIH6; Q3UJP3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Emerin;
GN Name=Emd; Synonyms=Sta;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129;
RX PubMed=9107678; DOI=10.1007/s003359900435;
RA Small K., Wagener M., Warren S.T.;
RT "Isolation and characterization of the complete mouse emerin gene.";
RL Mamm. Genome 8:337-341(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RA Hawkes S.L.J., Neville L.A., Kennedy M.A.K., Love D.R.;
RT "cDNA sequence and analysis of the murine Emery-Dreifuss muscular dystrophy
RT gene.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=DBA/2J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10579712; DOI=10.1083/jcb.147.5.913;
RA Sullivan T., Escalante-Alcalde D., Bhatt H., Anver M., Bhat N.,
RA Nagashima K., Stewart C.L., Burke B.;
RT "Loss of A-type lamin expression compromises nuclear envelope integrity
RT leading to muscular dystrophy.";
RL J. Cell Biol. 147:913-920(1999).
RN [7]
RP INTERACTION WITH TMEM43, AND SUBCELLULAR LOCATION.
RX PubMed=18230648; DOI=10.1242/jcs.019281;
RA Bengtsson L., Otto H.;
RT "LUMA interacts with emerin and influences its distribution at the inner
RT nuclear membrane.";
RL J. Cell Sci. 121:536-548(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH SUN1 AND SUN2.
RX PubMed=19933576; DOI=10.1074/jbc.m109.071910;
RA Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M.,
RA Shackleton S.;
RT "Mammalian SUN protein interaction networks at the inner nuclear membrane
RT and their role in laminopathy disease processes.";
RL J. Biol. Chem. 285:3487-3498(2010).
CC -!- FUNCTION: Stabilizes and promotes the formation of a nuclear actin
CC cortical network. Stimulates actin polymerization in vitro by binding
CC and stabilizing the pointed end of growing filaments. Inhibits beta-
CC catenin activity by preventing its accumulation in the nucleus. Acts by
CC influencing the nuclear accumulation of beta-catenin through a CRM1-
CC dependent export pathway. Links centrosomes to the nuclear envelope via
CC a microtubule association. Required for proper localization of non-
CC farnesylated prelamin-A/C (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with lamins A and C, BANF1, GMCL, BCLAF1 and
CC YTHDC1/YT521. Interacts with TMEM43; the interaction retains emerin in
CC the inner nuclear membrane. Interacts with ACTB, SPTAN1, F-actin,
CC CTNNB1 and beta-tubulin (By similarity). Interacts with SUN1 and SUN2.
CC Interacts with TMEM201. {ECO:0000250, ECO:0000269|PubMed:18230648,
CC ECO:0000269|PubMed:19933576}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000250|UniProtKB:P50402}; Single-pass membrane protein;
CC Nucleoplasmic side {ECO:0000250|UniProtKB:P50402}. Nucleus outer
CC membrane. Note=Colocalized with BANF1 at the central region of the
CC assembling nuclear rim, near spindle-attachment sites. The accumulation
CC of different intermediates of prelamin-A/C (non-farnesylated or
CC carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its
CC localization in the nucleus (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic fibroblasts, skeletal muscle,
CC heart muscle and tongue epithelium (at protein level). Widely
CC expressed. {ECO:0000269|PubMed:10579712, ECO:0000269|PubMed:9107678}.
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DR EMBL; U79753; AAB51239.1; -; Genomic_DNA.
DR EMBL; U73902; AAD00238.1; -; mRNA.
DR EMBL; AK146361; BAE27112.1; -; mRNA.
DR EMBL; AK167852; BAE39870.1; -; mRNA.
DR EMBL; CH466650; EDL29837.1; -; Genomic_DNA.
DR EMBL; BC132131; AAI32132.1; -; mRNA.
DR EMBL; BC132133; AAI32134.1; -; mRNA.
DR CCDS; CCDS30222.1; -.
DR RefSeq; NP_031953.1; NM_007927.3.
DR AlphaFoldDB; O08579; -.
DR SMR; O08579; -.
DR BioGRID; 199436; 32.
DR IntAct; O08579; 5.
DR MINT; O08579; -.
DR STRING; 10090.ENSMUSP00000002029; -.
DR iPTMnet; O08579; -.
DR PhosphoSitePlus; O08579; -.
DR EPD; O08579; -.
DR jPOST; O08579; -.
DR PaxDb; O08579; -.
DR PeptideAtlas; O08579; -.
DR PRIDE; O08579; -.
DR ProteomicsDB; 275614; -.
DR TopDownProteomics; O08579; -.
DR Antibodypedia; 371; 493 antibodies from 40 providers.
DR Ensembl; ENSMUST00000002029; ENSMUSP00000002029; ENSMUSG00000001964.
DR GeneID; 13726; -.
DR KEGG; mmu:13726; -.
DR UCSC; uc009toa.2; mouse.
DR CTD; 2010; -.
DR MGI; MGI:108117; Emd.
DR VEuPathDB; HostDB:ENSMUSG00000001964; -.
DR eggNOG; ENOG502S5SJ; Eukaryota.
DR GeneTree; ENSGT00390000002034; -.
DR HOGENOM; CLU_095531_0_0_1; -.
DR InParanoid; O08579; -.
DR OMA; DRERPIY; -.
DR OrthoDB; 1219474at2759; -.
DR PhylomeDB; O08579; -.
DR TreeFam; TF337236; -.
DR Reactome; R-MMU-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR BioGRID-ORCS; 13726; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Emd; mouse.
DR PRO; PR:O08579; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O08579; protein.
DR Bgee; ENSMUSG00000001964; Expressed in undifferentiated genital tubercle and 247 other tissues.
DR ExpressionAtlas; O08579; baseline and differential.
DR Genevisible; O08579; MM.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
DR GO; GO:0005652; C:nuclear lamina; TAS:MGI.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0005640; C:nuclear outer membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0031616; C:spindle pole centrosome; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0071763; P:nuclear membrane organization; ISO:MGI.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:MGI.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR CDD; cd12939; LEM_emerin; 1.
DR Gene3D; 1.10.720.40; -; 1.
DR InterPro; IPR035004; Emerin.
DR InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR InterPro; IPR003887; LEM_dom.
DR InterPro; IPR034989; LEM_emerin.
DR PANTHER; PTHR15171; PTHR15171; 1.
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 Acetylation; Actin-binding; Membrane; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..259
FT /note="Emerin"
FT /id="PRO_0000206141"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..45
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT REGION 46..223
FT /note="Interaction with F-actin"
FT /evidence="ECO:0000250"
FT REGION 168..187
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63190"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63190"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63190"
FT MOD_RES 161
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 96
FT /note="Y -> C (in Ref. 3; BAE39870)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="P -> H (in Ref. 3; BAE39870)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 29436 MW; 645B021541063502 CRC64;
MDDYAVLSDT ELAAVLRQYN IPHGPIVGST RKLYEKKIFE YETQRRRLLP PNSSSSSFSY
QFSDLDSAAV DSDMYDLPKK EDALLYQSKD YNDDYYEESY LTTKTYGEPE SVGMSKSFRQ
PGTSLVDADT FHHQVRDDIF SSLEEEGKDR ERLIYGQDSA YQSIAHYRPI SNVSRSSLGL
SYYPTSSTSS VSSSSSSPSS WLTRRAIRPE KQAPAAALGQ DRQVPLWGQL LLFLVFAAFL
LFVYYSIQAE EGNPFWMDP
