LAMC_DROME
ID LAMC_DROME Reviewed; 621 AA.
AC Q03427; Q24374; Q9V729;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Lamin-C;
DE AltName: Full=pG-IF;
GN Name=LamC; ORFNames=CG10119;
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].
RC TISSUE=Embryo;
RX PubMed=8314904; DOI=10.1242/jcs.104.4.1263;
RA Bossie C.A., Sanders M.M.;
RT "A cDNA from Drosophila melanogaster encodes a lamin C-like intermediate
RT filament protein.";
RL J. Cell Sci. 104:1263-1272(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Embryo;
RX PubMed=8082654;
RA Riemer D., Weber K.;
RT "The organization of the gene for Drosophila lamin C: limited homology with
RT vertebrate lamin genes and lack of homology versus the Drosophila lamin Dmo
RT gene.";
RL Eur. J. Cell Biol. 63:299-306(1994).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP INTERACTION WITH MAN1.
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-406; SER-441 AND
RP THR-443, 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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 (By similarity). In spermatocytes, regulates
CC cytokinesis during meiosis (PubMed:27402967).
CC {ECO:0000250|UniProtKB:P08928, ECO:0000269|PubMed:27402967}.
CC -!- SUBUNIT: Interacts with MAN1. {ECO:0000269|PubMed:16439308}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7593280}. Nucleus
CC lamina {ECO:0000269|PubMed:18723885, ECO:0000269|PubMed:27402967}.
CC Note=Nuclear periphery (PubMed:7593280). In premeiotic nuclei of
CC primary spermatocytes, localization to the nuclear lamina depends on
CC type-B lamin Lam. In spermatocytes, temporarily depleted between
CC anaphase I and telophase I, and anaphase II and telophase II.
CC {ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:7593280}.
CC -!- TISSUE SPECIFICITY: First detected from late stage 12 in the oenocytes,
CC abdominal segments, hindgut and posterior spiracles, with expression
CC increasing in stage 13 (PubMed:7593280) (at protein level). In stage
CC 14, also becomes detectable in the foregut (PubMed:7593280) (at protein
CC level). Stage 15 shows expression in the epidermis, dorsal longitudinal
CC trunk, pharynx, esophagus and proventriculus, with the dorsal
CC pharyngeal musculature showing expression in late stage 15
CC (PubMed:7593280) (at protein level). In stage 16 embryos, also detected
CC in the exit glia with increasing expression in the somatic musculature
CC (PubMed:7593280) (at protein level). Also detected in the visceral
CC mesoderm but not in the midgut or central nervous system until the end
CC of embryogenesis (PubMed:7593280) (at protein level). In third instar
CC larvae, detectable at varying levels in all cell types (PubMed:7593280)
CC (at protein level). Expressed in spermatocytes (at protein level)
CC (PubMed:27402967). {ECO:0000269|PubMed:27402967,
CC ECO:0000269|PubMed:7593280}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 12-22 hours embryos. Expression peaks
CC in larvae and declines in pupae and adults.
CC {ECO:0000269|PubMed:7593280}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; L07933; AAA28666.1; -; mRNA.
DR EMBL; X75886; CAA53480.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58237.1; -; Genomic_DNA.
DR EMBL; AY095046; AAM11374.1; -; mRNA.
DR PIR; S49020; S49020.
DR RefSeq; NP_523742.2; NM_079018.3.
DR AlphaFoldDB; Q03427; -.
DR SMR; Q03427; -.
DR BioGRID; 62363; 14.
DR STRING; 7227.FBpp0305369; -.
DR iPTMnet; Q03427; -.
DR PaxDb; Q03427; -.
DR PRIDE; Q03427; -.
DR DNASU; 36615; -.
DR EnsemblMetazoa; FBtr0087512; FBpp0086641; FBgn0010397.
DR GeneID; 36615; -.
DR KEGG; dme:Dmel_CG10119; -.
DR CTD; 36615; -.
DR FlyBase; FBgn0010397; LamC.
DR VEuPathDB; VectorBase:FBgn0010397; -.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000168319; -.
DR HOGENOM; CLU_012560_9_2_1; -.
DR InParanoid; Q03427; -.
DR OMA; MSIHHRH; -.
DR PhylomeDB; Q03427; -.
DR BioGRID-ORCS; 36615; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36615; -.
DR PRO; PR:Q03427; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010397; Expressed in crop (Drosophila) and 41 other tissues.
DR ExpressionAtlas; Q03427; baseline and differential.
DR Genevisible; Q03427; DM.
DR GO; GO:0005638; C:lamin filament; IDA:FlyBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0005652; C:nuclear lamina; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:FlyBase.
DR GO; GO:0070732; C:spindle envelope; IDA:FlyBase.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:FlyBase.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:UniProtKB.
DR GO; GO:0060415; P:muscle tissue morphogenesis; IMP:FlyBase.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0051664; P:nuclear pore localization; IMP:FlyBase.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IBA:GO_Central.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:FlyBase.
DR GO; GO:0035989; P:tendon development; 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 Coiled coil; Intermediate filament; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..621
FT /note="Lamin-C"
FT /id="PRO_0000063827"
FT DOMAIN 46..402
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 468..582
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..47
FT /note="Head"
FT REGION 47..85
FT /note="Coil 1A"
FT REGION 86..95
FT /note="Linker 1"
FT REGION 96..233
FT /note="Coil 1B"
FT REGION 234..257
FT /note="Linker 2"
FT REGION 258..403
FT /note="Coil 2"
FT REGION 404..621
FT /note="Tail"
FT REGION 404..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 453..458
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 281
FT /note="Heptad change of phase"
FT SITE 345
FT /note="Heptad change of phase"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 166
FT /note="S -> A (in Ref. 2; CAA53480)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="M -> I (in Ref. 1; AAA28666)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..440
FT /note="RR -> HH (in Ref. 2; CAA53480)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="V -> I (in Ref. 1; AAA28666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 621 AA; 69860 MW; E6C0F173D022C04D CRC64;
MSARRVTLNT RVSRASTSTP VGGASTSSRV GATSPTSPTR TSRQQEKEEL QHLNDRLACY
IDRMRNLENE NSRLTQELNL AQDTVNRETS NLKAVYEKEL AAARKLLDET AKEKAKLEID
IKRLWEENDD LKPRLDKKTK EATVAENNAR LYENRYNEVN GKYNQSLADR KKFEDQAKEL
ALENERLRRQ LDDLRKQLEA ETLARVDLEN QNQSLREELA FKDQVHTQEL TETRSRRQIE
ISEIDGRLSR QYEAKLQQSL QELRDQYEGQ MRINREEIEL LYDNEIQNLK AAANRAAQGS
ALATEEVRLM RTKIDGLNAK LQNLEDTNAG LNARIRELEN LLDTERQRHN QYIASLEAEL
QRMRDEMAHQ LQEYQGLMDI KVSLDLEIAA YDKLLCGEER RLNIESPGRP TTDSGISSNG
SHLTASASSR SGRVTPSGRR SATPGISGSS AVKRRRTVID ESEDRTLSEY SVNAAAKGDL
EIIEADVEGR FIKLHNKGTE EINLTGWQLT RIAGDEELAF KFSRGSKVLG GASVTIWSVD
AGTAHDPPNN LVMKKKWPVA NSMRSVLANA DKEDVASYDR VRANVSSHTS RHRSSGTPST
GFTLGSGAGS TGVRSLFSLL F
