LMN1_CAEEL
ID LMN1_CAEEL Reviewed; 566 AA.
AC Q21443; O62127;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Lamin-1;
DE AltName: Full=Ce-lamin;
DE AltName: Full=CeLam-1;
DE Flags: Precursor;
GN Name=lmn-1 {ECO:0000312|WormBase:DY3.2};
GN Synonyms=lam-1 {ECO:0000312|WormBase:DY3.2};
GN ORFNames=DY3.2 {ECO:0000312|WormBase:DY3.2};
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 [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7925480;
RA Riemer D., Dodemont H., Weber K.;
RT "A nuclear lamin protein of the nematode Caenorhabditis elegans with
RT unusual structural features: cDNA cloning and gene organization.";
RL Eur. J. Cell Biol. 62:214-223(1993).
RN [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11071918; DOI=10.1091/mbc.11.11.3937;
RA Liu J., Ben-Shahar T.R., Riemer D., Treinin M., Spann P., Weber K.,
RA Fire A., Gruenbaum Y.;
RT "Essential roles for Caenorhabditis elegans lamin gene in nuclear
RT organization, cell cycle progression, and spatial organization of nuclear
RT pore complexes.";
RL Mol. Biol. Cell 11:3937-3947(2000).
RN [4]
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 [5]
RP INTERACTION WITH EMR-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 [6]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11907270; DOI=10.1091/mbc.01-06-0294;
RA Lee K.K., Starr D.A., Cohen M., Liu J., Han M., Wilson K.L., Gruenbaum Y.;
RT "Lamin-dependent localization of UNC-84, a protein required for nuclear
RT migration in Caenorhabditis elegans.";
RL Mol. Biol. Cell 13:892-901(2002).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=12064941; DOI=10.1006/jsbi.2002.4452;
RA Tzur Y.B., Hersh B.M., Horvitz H.R., Gruenbaum Y.;
RT "Fate of the nuclear lamina during Caenorhabditis elegans apoptosis.";
RL J. Struct. Biol. 137:146-153(2002).
RN [9]
RP INTERACTION WITH LEM-2 AND EMR-1.
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 [10]
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 [11]
RP FUNCTION, INTERACTION WITH UNC-84, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25057012; DOI=10.1091/mbc.e14-05-0971;
RA Bone C.R., Tapley E.C., Gorjanacz M., Starr D.A.;
RT "The Caenorhabditis elegans SUN protein UNC-84 interacts with lamin to
RT transfer forces from the cytoplasm to the nucleoskeleton during nuclear
RT migration.";
RL Mol. Biol. Cell 25:2853-2865(2014).
CC -!- FUNCTION: Major component of the nuclear lamina, a fibrous layer on the
CC nucleoplasmic side of the inner nuclear membrane (PubMed:11071918,
CC PubMed:25057012). Provides a framework for the nuclear envelope and
CC probably also interacts with chromatin (PubMed:11071918,
CC PubMed:25057012). Essential to maintain the shape and integrity of the
CC nucleus, and for DNA replication (PubMed:11071918). Involved in spatial
CC organization of nuclear pore complexes (PubMed:11071918). It is not a
CC target for ced-3 during apoptosis, suggesting that lamin cleavage is
CC not essential for apoptosis in C.elegans (PubMed:12064941).
CC {ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:12064941,
CC ECO:0000269|PubMed:25057012}.
CC -!- SUBUNIT: Interacts with LEM domain proteins lem-2 and emr-1
CC (PubMed:11870211, PubMed:12684533). May interact with unc-84; this
CC interaction may be required to complete the connection between the
CC nuclear lamina and the cytoskeleton (PubMed:25057012).
CC {ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12684533,
CC ECO:0000269|PubMed:25057012}.
CC -!- INTERACTION:
CC Q21443; Q9XTB5: lem-2; NbExp=3; IntAct=EBI-314110, EBI-2535391;
CC Q21443; Q21443: lmn-1; NbExp=3; IntAct=EBI-314110, EBI-314110;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:16950114}.
CC Nucleus inner membrane {ECO:0000269|PubMed:10982402,
CC ECO:0000269|PubMed:11071918, ECO:0000269|PubMed:11907270,
CC ECO:0000269|PubMed:12490171, ECO:0000269|PubMed:25057012}; Lipid-anchor
CC {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11071918,
CC ECO:0000269|PubMed:12490171}; Nucleoplasmic side
CC {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11071918,
CC ECO:0000269|PubMed:12490171}. Note=Remains in the nuclear envelope
CC until late anaphase in early embryos. Depends on mel-28 for nuclear
CC envelope localization after mitosis. {ECO:0000269|PubMed:10982402,
CC ECO:0000269|PubMed:16950114}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in all cells, except in cells
CC undergoing spermatogenesis. {ECO:0000269|PubMed:11071918}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the development and in
CC adults. {ECO:0000269|PubMed:11071918}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in the irregular
CC localization of nuclear envelope associated proteins such as unc-84
CC (PubMed:11870211). RNAi-mediated knockdown results in nuclear migration
CC defects in hyp7 hypodermal precursor cells (PubMed:25057012).
CC {ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:25057012}.
CC -!- MISCELLANEOUS: It is the only lamin protein in C.elegans.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X74027; CAA52188.1; -; Genomic_DNA.
DR EMBL; BX284601; CAB09411.1; -; Genomic_DNA.
DR PIR; S42257; S42257.
DR PIR; T20390; T20390.
DR RefSeq; NP_492371.1; NM_059970.4.
DR AlphaFoldDB; Q21443; -.
DR SMR; Q21443; -.
DR BioGRID; 38120; 65.
DR DIP; DIP-29640N; -.
DR IntAct; Q21443; 43.
DR STRING; 6239.DY3.2.2; -.
DR EPD; Q21443; -.
DR PaxDb; Q21443; -.
DR PeptideAtlas; Q21443; -.
DR EnsemblMetazoa; DY3.2.1; DY3.2.1; WBGene00003052.
DR GeneID; 172687; -.
DR KEGG; cel:CELE_DY3.2; -.
DR UCSC; DY3.2.1; c. elegans.
DR CTD; 172687; -.
DR WormBase; DY3.2; CE15746; WBGene00003052; lmn-1.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000168319; -.
DR HOGENOM; CLU_012560_9_2_1; -.
DR InParanoid; Q21443; -.
DR OMA; IGQWAIK; -.
DR OrthoDB; 701388at2759; -.
DR PhylomeDB; Q21443; -.
DR Reactome; R-CEL-352238; Breakdown of the nuclear lamina.
DR Reactome; R-CEL-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-CEL-9013405; RHOD GTPase cycle.
DR Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR SignaLink; Q21443; -.
DR PRO; PR:Q21443; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003052; Expressed in embryo and 4 other tissues.
DR GO; GO:0005638; C:lamin filament; ISS:WormBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005652; C:nuclear lamina; IBA:GO_Central.
DR GO; GO:0034399; C:nuclear periphery; IDA:WormBase.
DR GO; GO:0042393; F:histone binding; IDA:WormBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0007281; P:germ cell development; IMP:WormBase.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:WormBase.
DR GO; GO:0051664; P:nuclear pore localization; IMP:WormBase.
DR GO; GO:0006997; P:nucleus organization; IMP:WormBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IBA:GO_Central.
DR GO; GO:0051983; P:regulation of chromosome segregation; IMP:WormBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:WormBase.
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; Intermediate filament; Lipoprotein; Membrane;
KW Methylation; Nucleus; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..563
FT /note="Lamin-1"
FT /id="PRO_0000063826"
FT PROPEP 564..566
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403473"
FT DOMAIN 45..387
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 435..550
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 13..47
FT /note="Head"
FT REGION 48..82
FT /note="Coil 1A"
FT REGION 83..94
FT /note="Linker 1"
FT REGION 95..228
FT /note="Coil 1B"
FT REGION 229..256
FT /note="Linker 2"
FT REGION 257..385
FT /note="Coil 2"
FT REGION 386..566
FT /note="Tail"
FT REGION 528..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT MOD_RES 563
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 563
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 499
FT /note="A -> R (in Ref. 1; CAA52188)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 64084 MW; F9AF3B720EF9A984 CRC64;
MSSRKGTRSS RIVTLERSAN SSLSNNGGGD DSFGSTLLET SRLQEKDHLT SLNSRLATYI
DKVRQLEQEN NRLQVQIRDI EVVEKKEKSN LADRFEAEKA RLRRALDSAQ DELAKYRIEY
DAAKVEVKKL KPQVEKLERE LAGAEEQALH AQSIADQSQA KQKTLQARND KLVVENDDLK
KQNITLRDTV EGLKKAVEDE TLLRTAANNK IKALEEDLAF ALQQHKGELE EVRHKRQVDM
TTYAKQINDE YQSKLQDQIE EMRAQFKNNL HQNKTAFEDA YKNKLNAARE RQEEAVSEAI
HLRARVRDLE TSSSGNASLI ERLRSELDTL KRSFQEKLDD KDARIAELNQ EIERMMSEFH
DLLDVKIQLD AELKTYQALL EGEEERLNLT QEAPQNTSVH HVSFSSGGAS AQRGVKRRRV
VDVNGEDQDI DYLNRRSKLN KETVGPVGID EVDEEGKWVR VANNSEEEQS IGGYKLVVKA
GNKEASFQFS SRMKLAPHAS ATVWSADAGA VHHPPEVYVM KKQQWPIGDN PSARLEDSEG
DTVSSITVEF SESSDPSDPA DRCSIM
