ID   LMNA_XENLA              Reviewed;         665 AA.
AC   P11048;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-SEP-2026, entry version 123.
DE   RecName: Full=Lamin-A;
DE   Flags: Precursor;
GN   Name=lmna;
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=3428277; DOI=10.1002/j.1460-2075.1987.tb02717.x;
RA   Wolin S.L., Krohne G., Kirschner M.W.;
RT   "A new lamin in Xenopus somatic tissues displays strong homology to human
RT   lamin A.";
RL   EMBO J. 6:3809-3818(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1521501; DOI=10.1007/bf00660316;
RA   Stick R.;
RT   "The gene structure of Xenopus nuclear lamin A: a model for the evolution
RT   of A-type from B-type lamins by exon shuffling.";
RL   Chromosoma 101:566-574(1992).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25157132; DOI=10.1073/pnas.1414437111;
RA   Komiya Y., Mandrekar N., Sato A., Dawid I.B., Habas R.;
RT   "Custos controls beta-catenin to regulate head development during
RT   vertebrate embryogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:13099-13104(2014).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=3762708; DOI=10.1038/323560a0;
RA   Aebi U., Cohn J., Buhle L., Gerace L.;
RT   "The nuclear lamina is a meshwork of intermediate-type filaments.";
RL   Nature 323:560-564(1986).
CC   -!- FUNCTION: Lamins are intermediate filament proteins that assemble into
CC       a filamentous meshwork, and which constitute the major components of
CC       the nuclear lamina, a fibrous layer on the nucleoplasmic side of the
CC       inner nuclear membrane (PubMed:3762708). Lamins provide a framework for
CC       the nuclear envelope, bridging the nuclear envelope and chromatin,
CC       thereby playing an important role in nuclear assembly, chromatin
CC       organization, nuclear membrane and telomere dynamics (By similarity).
CC       The structural integrity of the lamina is strictly controlled by the
CC       cell cycle, as seen by the disintegration and formation of the nuclear
CC       envelope in prophase and telophase, respectively (By similarity).
CC       {ECO:0000250|UniProtKB:P02545, ECO:0000269|PubMed:3762708}.
CC   -!- SUBUNIT: Homodimer. Lamin dimers then assemble into dimeric head-to-
CC       tail polymers. Ultimately, two head-to-tail polymers assemble laterally
CC       into a protofilament with a uniformly shaped rod of 3.5 nm in diameter.
CC       {ECO:0000250|UniProtKB:P02545}.
CC   -!- SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000269|PubMed:3762708}.
CC       Nucleus envelope {ECO:0000269|PubMed:25157132}. Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:25157132}. Nucleus matrix
CC       {ECO:0000250|UniProtKB:P02545}.
CC   -!- PTM: Phosphorylation plays a key role in lamin organization,
CC       subcellular localization and nuclear envelope disintegration.
CC       Phosphorylation by CDK1 at Ser-18 at the onset of mitosis drives lamin
CC       disassembly and nuclear envelope breakdown.
CC       {ECO:0000250|UniProtKB:P14732}.
CC   -!- MISCELLANEOUS: There are at least five different lamins in Xenopus: the
CC       somatic lamins L(I)/lmnb1.S, L(II)/lmnb2.L, and A/lmna.L; the oocyte
CC       germinal vesicle lamin L(III)/lmnb3.L; and the male germ cells lamin
CC       l(IV).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; X06345; CAA29652.1; -; mRNA.
DR   PIR; S02358; S02358.
DR   RefSeq; NP_001095210.1; NM_001101740.1.
DR   AlphaFoldDB; P11048; -.
DR   SMR; P11048; -.
DR   GeneID; 373673; -.
DR   KEGG; xla:373673; -.
DR   AGR; Xenbase:XB-GENE-920728; -.
DR   CTD; 373673; -.
DR   Xenbase; XB-GENE-920728; lmna.L.
DR   OrthoDB; 102442at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 373673; Expressed in stomach and 16 other cell types or tissues.
DR   GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR   GO; GO:0005652; C:nuclear lamina; IDA:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0031507; P:heterochromatin formation; IBA:GO_Central.
DR   GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR   GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR   GO; GO:0051664; P:nuclear pore localization; IBA:GO_Central.
DR   GO; GO:0090435; P:protein localization to nuclear envelope; IBA:GO_Central.
DR   FunFam; 1.20.5.170:FF:000033; Lamin A/C; 1.
DR   FunFam; 1.20.5.500:FF:000002; Lamin A/C; 1.
DR   FunFam; 2.60.40.1260:FF:000001; Lamin A/C; 1.
DR   FunFam; 1.20.5.1160:FF:000007; Lamin B1; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 2.60.40.1260; Lamin Tail domain; 1.
DR   Gene3D; 1.20.5.500; Single helix bin; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 2.
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   PANTHER; PTHR45721; LAMIN DM0-RELATED; 1.
DR   PANTHER; PTHR45721:SF5; PRELAMIN-A_C; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF00932; LTD; 1.
DR   SMART; SM01391; Filament; 1.
DR   SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR   SUPFAM; SSF74853; Lamin A/C globular tail domain; 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; Methylation;
KW   Nucleus; Phosphoprotein; Prenylation; Reference proteome.
FT   CHAIN           1..662
FT                   /note="Lamin-A"
FT                   /id="PRO_0000063815"
FT   PROPEP          663..665
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P02545"
FT                   /id="PRO_0000403466"
FT   DOMAIN          27..383
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   DOMAIN          425..542
FT                   /note="LTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT   REGION          1..29
FT                   /note="Head"
FT   REGION          30..66
FT                   /note="Coil 1A"
FT   REGION          67..76
FT                   /note="Linker 1"
FT   REGION          77..214
FT                   /note="Coil 1B"
FT   REGION          215..238
FT                   /note="Linker 2"
FT   REGION          239..383
FT                   /note="Coil 2"
FT   REGION          381..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..664
FT                   /note="Tail"
FT   REGION          550..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           413..418
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        399..411
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..630
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P02545"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14732"
FT   MOD_RES         388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02545"
FT   MOD_RES         662
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P02545"
FT   LIPID           662
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P02545"
SQ   SEQUENCE   665 AA;  74919 MW;  9FA64F2F1AF99293 CRC64;
     METPGQKRAT RSTHTPLSPT RITRLQEKED LQGLNDRLAV YIDKVRSLEL ENARLRLRIT
     ESEDVISREV TGIKSAYETE LADARKTLDS VAKERARLQL ELSKIREEHK ELKARNAKKE
     SDLLTAQARL KDLEALLNSK DAALTTALGE KRNLENEIRE LKAHIAKLEA SLADTKKQLQ
     DEMLRRVDTE NRNQTLKEEL EFQKSIYNEE MRETKRRHET RLVEVDNGRQ REFESKLADA
     LHELRAQHEG QIGLYKEELG KTYNAKLENA KQSAERNSSL VGEAQEEIQQ SRIRIDSLSA
     QLSQLQKQLA AREAKLRDLE DAYARERDSS RRLLADKDRE MAEMRARMQQ QLDEYQELLD
     IKLALDMEIN AYRKLLEGEE ERLRLSPSPN TQKRSARTIA SHSGAHISSS ASKRRRLEEG
     ESRSSSFTQH ARTTGKVSVE EVDPEGKYVR LRNKSNEDQS LGNWQIKRQI GDETPIVYKF
     PPRLTLKAGQ TVTIWASGAG ATNSPPSDLV WKAQSSWGTG DSIRTALLTS SNEEVAMRKL
     VRTVVINDED DEDNDDMEHH HHHHHHHHDG QNSSGDPGEY NLRSRTIVCT SCGRPAEKSV
     LASQGSGLVT GSSGSSSSSV TLTRTYRSTG GTSGGSGLGE SPVTRNFIVG NGQRAQVAPQ
     NCSIM
//