LAML1_XENLA
ID LAML1_XENLA Reviewed; 583 AA.
AC P09010;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Lamin-L(I);
DE Flags: Precursor;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3428276; DOI=10.1002/j.1460-2075.1987.tb02716.x;
RA Krohne G., Wolin S.L., McKeon F.D., Franke W.W., Kirschner M.W.;
RT "Nuclear lamin LI of Xenopus laevis: cDNA cloning, amino acid sequence and
RT binding specificity of a member of the lamin B subfamily.";
RL EMBO J. 6:3801-3808(1987).
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.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Lipid-anchor;
CC Nucleoplasmic side.
CC -!- PTM: B-type lamins undergo a series of modifications, such as
CC farnesylation and phosphorylation. Increased phosphorylation of the
CC lamins occurs before envelope disintegration and probably plays a role
CC in regulating lamin associations.
CC -!- MISCELLANEOUS: The structural integrity of the lamina is strictly
CC controlled by the cell cycle, as seen by the disintegration and
CC formation of the nuclear envelope in prophase and telophase,
CC respectively.
CC -!- MISCELLANEOUS: There are at least five different lamins in Xenopus: the
CC somatic lamins L(I), L(II), and A; the oocyte germinal vesicle lamin
CC L(III); and the male germ cells lamin l(IV).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X06344; CAA29651.1; -; mRNA.
DR PIR; S01496; S01496.
DR RefSeq; NP_001081547.1; NM_001088078.1.
DR AlphaFoldDB; P09010; -.
DR SMR; P09010; -.
DR PRIDE; P09010; -.
DR DNASU; 397911; -.
DR GeneID; 397911; -.
DR KEGG; xla:397911; -.
DR CTD; 397911; -.
DR Xenbase; XB-GENE-17340188; lmnb1.S.
DR OrthoDB; 701388at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 397911; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.1260; -; 1.
DR InterPro; IPR018039; IF_conserved.
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; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
DR PROSITE; PS51841; LTD; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Intermediate filament; Lipoprotein; Membrane;
KW Methylation; Nucleus; Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..580
FT /note="Lamin-L(I)"
FT /id="PRO_0000063823"
FT PROPEP 581..583
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396782"
FT DOMAIN 32..388
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 429..547
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..34
FT /note="Head"
FT REGION 35..69
FT /note="Coil 1A"
FT REGION 70..81
FT /note="Linker 1"
FT REGION 82..215
FT /note="Coil 1B"
FT REGION 216..243
FT /note="Linker 2"
FT REGION 244..386
FT /note="Coil 2"
FT REGION 387..580
FT /note="Tail"
FT REGION 387..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 414..419
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 393..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 268
FT /note="Heptad change of phase"
FT SITE 332
FT /note="Heptad change of phase"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT MOD_RES 580
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 580
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 583 AA; 66451 MW; 26C4FE9CDE97E81E CRC64;
MATATPSGPR SSGRRSSMST PLSPTRITRL QEKVDLQELN DRLALYIDTV RSLESENSLL
HVQVTEREEV RSREVSGIKE LYETELADAR RSLDDTAREK ARLQLELSKV SVEHQDLQAS
FSKRESELES TQARFRETEA LLNSKNAALA TAQSENKSLQ GEVEDLKAEI GQLGSALALA
KKQLEEEILM KVDLENRCQS LIEELNFRKN IYEEEIKETS RRHETRLVEV DSGRQVDYEY
KLSQALSEMR EQQESQIGLY KEELEQTYQS KLENARLASE MNSSAVNSTR EELMESRIRI
DSLTSQLSEL QKESRAWHDR MQELEDMLAK EKDNSRKMLA EREREMADIR DQMQQQLNDY
EQLLDVKLAL DMEISAYRKL LEGEEERLKL SPSPSRVTVS RASSSRAVRT TKGKRKRIDV
EESEASSSVS IDHSAAATGD VSIEEVDVDG KYIRLKNNSE KDHPLGGWEL TRTIGEASVN
FKFTSRYVLK AEQTVTIWAA DAGVKASPPS DLIWKNQNSW GTGEDVKATL KNSQGEEVAQ
RTTIYTTNIP EEEFEEGEEI FEETAKEFHY PQQKSGNKNC AIM
