LAM0_DROME
ID LAM0_DROME Reviewed; 622 AA.
AC P08928; Q9VMQ0;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 4.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Lamin Dm0 {ECO:0000305};
DE Flags: Precursor;
GN Name=Lam {ECO:0000312|FlyBase:FBgn0002525};
GN ORFNames=CG6944 {ECO:0000312|FlyBase:FBgn0002525};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND PHOSPHORYLATION AT THR-10;
RP THR-12; THR-20; SER-25; SER-34; THR-39; SER-41; SER-42; SER-45; THR-47;
RP SER-235; TYR-249; SER-250; SER-311; THR-413; THR-435; SER-442; SER-455;
RP SER-459: SER-595 AND SER-615.
RC TISSUE=Embryo;
RX PubMed=3126192; DOI=10.1083/jcb.106.3.585;
RA Gruenbaum Y., Landesman Y., Drees B., Bare J.W., Saumweber H., Paddy M.R.,
RA Sedat J.W., Smith D.E., Benton B.M., Fisher P.A.;
RT "Drosophila nuclear lamin precursor Dm0 is translated from either of two
RT developmentally regulated mRNA species apparently encoded by a single
RT gene.";
RL J. Cell Biol. 106:585-596(1988).
RN [2]
RP SEQUENCE REVISION TO 24-39 AND 254-263.
RA Stuurman N., Maus N., Fisher P.A.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2123469; DOI=10.1016/0888-7543(90)90274-x;
RA Osman M., Paz M., Landesman Y., Fainsod A., Gruenbaum Y.;
RT "Molecular analysis of the Drosophila nuclear lamin gene.";
RL Genomics 8:217-224(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=7593280; DOI=10.1242/jcs.108.10.3189;
RA Riemer D., Stuurman N., Berrios M., Hunter C., Fisher P.A., Weber K.;
RT "Expression of Drosophila lamin C is developmentally regulated: analogies
RT with vertebrate A-type lamins.";
RL J. Cell Sci. 108:3189-3198(1995).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=8999964; DOI=10.1074/jbc.272.4.2493;
RA Ashery-Padan R., Weiss A.M., Feinstein N., Gruenbaum Y.;
RT "Distinct regions specify the targeting of otefin to the nucleoplasmic side
RT of the nuclear envelope.";
RL J. Biol. Chem. 272:2493-2499(1997).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9199347; DOI=10.1128/mcb.17.7.4114;
RA Ashery-Padan R., Ulitzur N., Arbel A., Goldberg M., Weiss A.M., Maus N.,
RA Fisher P.A., Gruenbaum Y.;
RT "Localization and posttranslational modifications of otefin, a protein
RT required for vesicle attachment to chromatin, during Drosophila
RT melanogaster development.";
RL Mol. Cell. Biol. 17:4114-4123(1997).
RN [10]
RP INTERACTION WITH OTE, AND SUBCELLULAR LOCATION.
RX PubMed=9632815; DOI=10.1128/mcb.18.7.4315;
RA Goldberg M., Lu H., Stuurman N., Ashery-Padan R., Weiss A.M., Yu J.,
RA Bhattacharyya D., Fisher P.A., Gruenbaum Y., Wolfner M.F.;
RT "Interactions among Drosophila nuclear envelope proteins lamin, otefin, and
RT YA.";
RL Mol. Cell. Biol. 18:4315-4323(1998).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15035436; DOI=10.1078/0171-9335-00350;
RA Wagner N., Schmitt J., Krohne G.;
RT "Two novel LEM-domain proteins are splice products of the annotated
RT Drosophila melanogaster gene CG9424 (Bocksbeutel).";
RL Eur. J. Cell Biol. 82:605-616(2004).
RN [12]
RP SUBUNIT, AND INTERACTION WITH LBR.
RX PubMed=15054108; DOI=10.1242/jcs.01052;
RA Wagner N., Weber D., Seitz S., Krohne G.;
RT "The lamin B receptor of Drosophila melanogaster.";
RL J. Cell Sci. 117:2015-2028(2004).
RN [13]
RP FUNCTION.
RX PubMed=14617811; DOI=10.1091/mbc.e03-06-0374;
RA Patterson K., Molofsky A.B., Robinson C., Acosta S., Cater C.,
RA Fischer J.A.;
RT "The functions of Klarsicht and nuclear lamin in developmentally regulated
RT nuclear migrations of photoreceptor cells in the Drosophila eye.";
RL Mol. Biol. Cell 15:600-610(2004).
RN [14]
RP FUNCTION, INTERACTION WITH MAN1, AND SUBCELLULAR LOCATION.
RX PubMed=16439308; DOI=10.1016/j.ejcb.2005.10.002;
RA Wagner N., Kagermeier B., Loserth S., Krohne G.;
RT "The Drosophila melanogaster LEM-domain protein MAN1.";
RL Eur. J. Cell Biol. 85:91-105(2006).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=18723885; DOI=10.1534/genetics.108.091371;
RA Pinto B.S., Wilmington S.R., Hornick E.E., Wallrath L.L., Geyer P.K.;
RT "Tissue-specific defects are caused by loss of the Drosophila MAN1 LEM
RT domain protein.";
RL Genetics 180:133-145(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; THR-12; THR-20; SER-25;
RP SER-34; THR-39; SER-41; SER-42; SER-45; THR-47; SER-235; TYR-249; SER-250;
RP SER-311; THR-413; THR-435; SER-442; SER-455; SER-459; SER-595; THR-597 AND
RP SER-615, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [17]
RP INTERACTION WITH OTE.
RX PubMed=22751930; DOI=10.1128/mcb.00814-12;
RA Habermann K., Mirgorodskaya E., Gobom J., Lehmann V., Mueller H.,
RA Bluemlein K., Deery M.J., Czogiel I., Erdmann C., Ralser M.,
RA von Kries J.P., Lange B.M.;
RT "Functional analysis of centrosomal kinase substrates in Drosophila
RT melanogaster reveals a new function of the nuclear envelope component
RT otefin in cell cycle progression.";
RL Mol. Cell. Biol. 32:3554-3569(2012).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27402967; DOI=10.1242/bio.017566;
RA Hayashi D., Tanabe K., Katsube H., Inoue Y.H.;
RT "B-type nuclear lamin and the nuclear pore complex Nup107-160 influences
RT maintenance of the spindle envelope required for cytokinesis in Drosophila
RT male meiosis.";
RL Biol. Open 5:1011-1021(2016).
CC -!- FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer
CC on the nucleoplasmic side of the inner nuclear membrane, which is
CC thought to provide a framework for the nuclear envelope and may also
CC interact with chromatin (PubMed:3126192, PubMed:15035436). May have a
CC role in the localization of the LEM domain proteins Ote, bocks and MAN1
CC to the nuclear membrane (PubMed:15035436, PubMed:16439308). In
CC spermatocytes, plays a role in maintaining type-A lamin LamC nuclear
CC localization; regulates meiotic cytokinesis by maintaining the
CC structure of the spindle envelope, and by contributing to the formation
CC of the contractile ring and central spindle (PubMed:27402967). Required
CC for nuclear migration and to link the microtubule organizing center
CC (MTOC) to the nucleus (PubMed:14617811). In addition, is required for
CC nuclear envelope localization of klar (PubMed:14617811).
CC {ECO:0000269|PubMed:14617811, ECO:0000269|PubMed:15035436,
CC ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:27402967,
CC ECO:0000269|PubMed:3126192}.
CC -!- SUBUNIT: Interacts directly with LBR (PubMed:15054108). Interacts with
CC MAN1 (PubMed:16439308). Interacts with Ote (PubMed:9632815,
CC PubMed:22751930). {ECO:0000269|PubMed:15054108,
CC ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:22751930,
CC ECO:0000269|PubMed:9632815}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7593280,
CC ECO:0000269|PubMed:9199347}. Nucleus inner membrane
CC {ECO:0000269|PubMed:16439308}. Nucleus envelope
CC {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308,
CC ECO:0000269|PubMed:8999964, ECO:0000269|PubMed:9199347,
CC ECO:0000269|PubMed:9632815}. Nucleus lamina
CC {ECO:0000269|PubMed:18723885}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:27402967}. Cytoplasm
CC {ECO:0000269|PubMed:9199347}. Note=Nuclear periphery (PubMed:7593280).
CC At metaphase and anaphase, weakly expressed in the nuclear envelope and
CC spindle poles (PubMed:16439308). Expression in oocyte cytoplasm
CC increases after stages 6 to 7 of egg development (PubMed:9199347). In
CC spermatocytes detected at the spindle envelope, spindle poles and
CC astral membrane throughout meiosis I, whereas mostly depleted in
CC meiosis II (PubMed:27402967). Colocalizes with nuclear pore complex
CC component Nup107 throughout meiosis I (PubMed:27402967).
CC {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:27402967,
CC ECO:0000269|PubMed:7593280, ECO:0000269|PubMed:9199347}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in all tissues (at protein
CC level) (PubMed:7593280). Expressed in spermatocytes (at protein level)
CC (PubMed:27402967). {ECO:0000269|PubMed:27402967,
CC ECO:0000269|PubMed:7593280}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed in all developmental
CC stages, especially during the first 6-9 hours.
CC {ECO:0000269|PubMed:7593280}.
CC -!- PTM: Three forms of lamin have been identified in D.melanogaster, lamin
CC Dm0 is rapidly processed to lamin Dm1 in the cytoplasm, Dm1 is then
CC assembled in the nuclear envelope and is then phosphorylated, forming
CC lamin Dm2. {ECO:0000269|PubMed:18327897, ECO:0000269|PubMed:3126192}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in spermatocytes results
CC in spindle envelope disintegration, failure to form contractile rings
CC and central spindle microtubules during meiosis I resulting in abnormal
CC cytokinesis and multinuclear cell formation.
CC {ECO:0000269|PubMed:27402967}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X07278; CAA30259.1; -; mRNA.
DR EMBL; X16275; CAA34351.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52262.1; -; Genomic_DNA.
DR EMBL; BT001506; AAN71261.1; -; mRNA.
DR PIR; A29965; A29965.
DR PIR; A37103; A37103.
DR RefSeq; NP_001245892.1; NM_001258963.2.
DR RefSeq; NP_001245893.1; NM_001258964.2.
DR RefSeq; NP_001285629.1; NM_001298700.1.
DR RefSeq; NP_476616.1; NM_057268.5.
DR AlphaFoldDB; P08928; -.
DR SMR; P08928; -.
DR BioGRID; 59950; 43.
DR DIP; DIP-2663N; -.
DR IntAct; P08928; 15.
DR MINT; P08928; -.
DR STRING; 7227.FBpp0078733; -.
DR iPTMnet; P08928; -.
DR PaxDb; P08928; -.
DR PRIDE; P08928; -.
DR EnsemblMetazoa; FBtr0079100; FBpp0078733; FBgn0002525.
DR EnsemblMetazoa; FBtr0307058; FBpp0297901; FBgn0002525.
DR EnsemblMetazoa; FBtr0307059; FBpp0297902; FBgn0002525.
DR EnsemblMetazoa; FBtr0346460; FBpp0312110; FBgn0002525.
DR GeneID; 33782; -.
DR KEGG; dme:Dmel_CG6944; -.
DR CTD; 33782; -.
DR FlyBase; FBgn0002525; Lam.
DR VEuPathDB; VectorBase:FBgn0002525; -.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000168319; -.
DR HOGENOM; CLU_012560_9_2_1; -.
DR InParanoid; P08928; -.
DR OMA; TTYKFHR; -.
DR OrthoDB; 701388at2759; -.
DR PhylomeDB; P08928; -.
DR Reactome; R-DME-352238; Breakdown of the nuclear lamina.
DR Reactome; R-DME-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR Reactome; R-DME-9035034; RHOF GTPase cycle.
DR SignaLink; P08928; -.
DR BioGRID-ORCS; 33782; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Lam; fly.
DR GenomeRNAi; 33782; -.
DR PRO; PR:P08928; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0002525; Expressed in eye disc (Drosophila) and 30 other tissues.
DR ExpressionAtlas; P08928; baseline and differential.
DR Genevisible; P08928; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005638; C:lamin filament; IDA:FlyBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0005641; C:nuclear envelope lumen; IDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005652; C:nuclear lamina; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:FlyBase.
DR GO; GO:0007417; P:central nervous system development; IMP:FlyBase.
DR GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:FlyBase.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:FlyBase.
DR GO; GO:0070828; P:heterochromatin organization; IMP:FlyBase.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:UniProtKB.
DR GO; GO:0007110; P:meiosis I cytokinesis; IMP:UniProtKB.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; IDA:FlyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0050777; P:negative regulation of immune response; IMP:FlyBase.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:FlyBase.
DR GO; GO:0071763; P:nuclear membrane organization; IDA:FlyBase.
DR GO; GO:0007097; P:nuclear migration; IMP:FlyBase.
DR GO; GO:0051664; P:nuclear pore localization; IMP:FlyBase.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:2000433; P:positive regulation of cytokinesis, actomyosin contractile ring assembly; IMP:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IMP:UniProtKB.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IMP:FlyBase.
DR GO; GO:0048137; P:spermatocyte division; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
DR Gene3D; 2.60.40.1260; -; 1.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF00932; LTD; 1.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF74853; SSF74853; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
DR PROSITE; PS51841; LTD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Intermediate filament;
KW Lipoprotein; Membrane; Methylation; Nucleus; Phosphoprotein; Prenylation;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..619
FT /note="Lamin Dm0"
FT /id="PRO_0000063828"
FT PROPEP 620..622
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396785"
FT DOMAIN 54..410
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 461..588
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..56
FT /note="Head"
FT REGION 55..91
FT /note="Coil 1A"
FT REGION 92..103
FT /note="Linker 1"
FT REGION 104..241
FT /note="Coil 1B"
FT REGION 242..265
FT /note="Linker 2"
FT REGION 266..408
FT /note="Coil 2"
FT REGION 409..619
FT /note="Tail"
FT REGION 429..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 446..451
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 289
FT /note="Heptad change of phase"
FT SITE 353
FT /note="Heptad change of phase"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 249
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 413
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 597
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:3126192"
FT MOD_RES 619
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 619
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 135
FT /note="E -> R (in Ref. 1; CAA30259)"
FT /evidence="ECO:0000305"
FT CONFLICT 270..271
FT /note="EL -> DV (in Ref. 1; CAA30259)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="Y -> I (in Ref. 1; CAA30259/CAA34351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 71300 MW; B77E48AA5CD9A8BD CRC64;
MSSKSRRAGT ATPQPGNTST PRPPSAGPQP PPPSTHSQTA SSPLSPTRHS RVAEKVELQN
LNDRLATYID RVRNLETENS RLTIEVQTTR DTVTRETTNI KNIFEAELLE TRRLLDDTAR
DRARAEIDIK RLWEENEELK NKLDKKTKEC TTAEGNVRMY ESRANELNNK YNQANADRKK
LNEDLNEALK ELERLRKQFE ETRKNLEQET LSRVDLENTI QSLREELSFK DQIHSQEINE
SRRIKQTEYS EIDGRLSSEY DAKLKQSLQE LRAQYEEQMQ INRDEIQSLY EDKIQRLQEA
AARTSNSTHK SIEELRSTRV RIDALNANIN ELEQANADLN ARIRDLERQL DNDRERHGQE
IDLLEKELIR LREEMTQQLK EYQDLMDIKV SLDLEIAAYD KLLVGEEARL NITPATNTAT
VQSFSQSLRN STRATPSRRT PSAAVKRKRA VVDESEDHSV ADYYVSASAK GNVEIKEIDP
EGKFVRLFNK GSEEVAIGGW QLQRLINEKG PSTTYKFHRS VRIEPNGVIT VWSADTKASH
EPPSSLVMKS QKWVSADNTR TILLNSEGEA VANLDRIKRI VSQHTSSSRL SRRRSVTAVD
GNEQLYHQQG DPQQSNEKCA IM
