LMNA_XENLA
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 03-AUG-2022, entry version 112.
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).
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. Nucleus envelope
CC {ECO:0000269|PubMed:25157132}.
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; X06345; CAA29652.1; -; mRNA.
DR PIR; S02358; S02358.
DR RefSeq; NP_001095210.1; NM_001101740.1.
DR AlphaFoldDB; P11048; -.
DR SMR; P11048; -.
DR PRIDE; P11048; -.
DR GeneID; 373673; -.
DR KEGG; xla:373673; -.
DR CTD; 373673; -.
DR Xenbase; XB-GENE-920728; lmna.L.
DR OrthoDB; 701388at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 373673; Expressed in stomach and 16 other tissues.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
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; Methylation;
KW Nucleus; 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"
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 388..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250"
FT MOD_RES 662
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 662
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
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
