EMD_RAT
ID EMD_RAT Reviewed; 260 AA.
AC Q63190;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Emerin;
GN Name=Emd;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Forebrain;
RX PubMed=9472006; DOI=10.1242/jcs.111.6.781;
RA Ellis J.A., Craxton M., Yates J.R.W., Kendrick-Jones J.;
RT "Aberrant intracellular targeting and cell cycle-dependent phosphorylation
RT of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype.";
RL J. Cell Sci. 111:781-792(1998).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-72; SER-142; SER-143
RP AND SER-144, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Interacts with SUN1 and SUN2. Interacts with
CC TMEM201 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000250|UniProtKB:P50402}; Single-pass membrane protein
CC {ECO:0000250}; Nucleoplasmic side {ECO:0000250|UniProtKB:P50402}.
CC Nucleus outer membrane {ECO:0000250}. Note=Colocalized with BANF1 at
CC the central region of the assembling nuclear rim, near spindle-
CC attachment sites. The accumulation of different intermediates of
CC prelamin-A/C (non-farnesylated or carboxymethylated farnesylated
CC prelamin-A/C) in fibroblasts modify its localization in the nucleus (By
CC similarity). {ECO:0000250}.
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DR EMBL; X98377; CAA67023.1; -; mRNA.
DR RefSeq; NP_037080.1; NM_012948.1.
DR AlphaFoldDB; Q63190; -.
DR SMR; Q63190; -.
DR STRING; 10116.ENSRNOP00000053121; -.
DR iPTMnet; Q63190; -.
DR PhosphoSitePlus; Q63190; -.
DR jPOST; Q63190; -.
DR PaxDb; Q63190; -.
DR PRIDE; Q63190; -.
DR GeneID; 25437; -.
DR KEGG; rno:25437; -.
DR CTD; 2010; -.
DR RGD; 2551; Emd.
DR eggNOG; ENOG502S5SJ; Eukaryota.
DR InParanoid; Q63190; -.
DR OrthoDB; 1219474at2759; -.
DR PhylomeDB; Q63190; -.
DR Reactome; R-RNO-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR PRO; PR:Q63190; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; ISO:RGD.
DR GO; GO:0005640; C:nuclear outer membrane; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005819; C:spindle; IDA:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0071763; P:nuclear membrane organization; ISO:RGD.
DR GO; GO:0031468; P:nuclear membrane reassembly; IEP:RGD.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:RGD.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
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..260
FT /note="Emerin"
FT /id="PRO_0000206142"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..45
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT REGION 46..224
FT /note="Interaction with F-actin"
FT /evidence="ECO:0000250"
FT REGION 169..188
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 184..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 49
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 162
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O08579"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50402"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08579"
SQ SEQUENCE 260 AA; 29676 MW; F7ACD132BF281FF4 CRC64;
MDDYAVLSDT ELAAVLRQYN IPHGPILGST RKLYEKKIFE YETQRRRLSP PSSSSSSFSY
RFSDLDSASV DSDMYDLPKK EDALLYQSKD YNDDYYEESY LTTRTYGEPE SVGMSKSFRR
PGTSLVDADD TFHHQVRDDI FSSSEEEGKD RERPIYGRDS AYQSIAEYRP ISNVSRSSLG
LSYYPRSSTS SVSSSSSSPS SWLTRRAIRP EKQAPTAALG QDRQVPLWGQ LLLFLAFATF
LLFVYYSIQA QEGNPFWMDP
