LAML3_XENLA
ID LAML3_XENLA Reviewed; 583 AA.
AC P10999; P23420; Q6AZG7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Lamin-L(III);
DE AltName: Full=Lamin-B3;
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] (ISOFORMS 1 AND 2).
RX PubMed=2249665; DOI=10.1002/j.1460-2075.1990.tb07629.x;
RA Doering V., Stick R.;
RT "Gene structure of nuclear lamin LIII of Xenopus laevis; a model for the
RT evolution of IF proteins from a lamin-like ancestor.";
RL EMBO J. 9:4073-4081(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
RX PubMed=3181134; DOI=10.1002/j.1460-2075.1988.tb03186.x;
RA Stick R.;
RT "cDNA cloning of the developmentally regulated lamin LIII of Xenopus
RT laevis.";
RL EMBO J. 7:3189-3197(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=B3A;
CC IsoId=P10999-1; Sequence=Displayed;
CC Name=2; Synonyms=B3B;
CC IsoId=P10999-2; Sequence=VSP_002473;
CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes.
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; X13169; CAA31567.1; -; mRNA.
DR EMBL; BC078034; AAH78034.1; -; mRNA.
DR PIR; S01301; S01301.
DR RefSeq; NP_001081545.1; NM_001088076.1.
DR AlphaFoldDB; P10999; -.
DR SMR; P10999; -.
DR BioGRID; 99247; 2.
DR PRIDE; P10999; -.
DR GeneID; 397910; -.
DR KEGG; xla:397910; -.
DR CTD; 397910; -.
DR Xenbase; XB-GENE-920628; lmnb3.L.
DR OMA; YHSKLEN; -.
DR OrthoDB; 701388at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 397910; Expressed in egg cell and 17 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; Alternative splicing; Coiled coil; Intermediate filament;
KW Lipoprotein; Membrane; Methylation; Nucleus; Phosphoprotein; Prenylation;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..580
FT /note="Lamin-L(III)"
FT /id="PRO_0000063825"
FT PROPEP 581..583
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396784"
FT DOMAIN 30..386
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 429..546
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..32
FT /note="Head"
FT REGION 33..67
FT /note="Coil 1A"
FT REGION 68..79
FT /note="Linker 1"
FT REGION 80..215
FT /note="Coil 1B"
FT REGION 216..242
FT /note="Linker 2"
FT REGION 243..384
FT /note="Coil 2"
FT REGION 383..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..580
FT /note="Tail"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..408
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 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"
FT VAR_SEQ 572..583
FT /note="SHQSVDPSCSIM -> TKRRKKKCCSVS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2249665"
FT /id="VSP_002473"
FT CONFLICT 349
FT /note="Q -> H (in Ref. 2; CAA31567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 67291 MW; 6BDBD1CF25ACEE92 CRC64;
MATSTPSRAR EHASAAQSPG SPTRISRMQE KEDLRHLNDR LAAYIERVRS LEADKSLLKI
QLEEREEVSS REVTNLRQLY ETELADARKL LDQTANERAR LQVELGKVRE EYRQLQARNS
KKENDLSLAQ NQLRDLESKL NTKEAELATA LSGKRGLEEQ LQEQRAQIAG LESSLRDTTK
QLHDEMLWRV DLENKMQTIR EQLDFQKNIH TQEVKEIKKR HDTRIVEIDS GRRVEFESKL
AEALQELRRD HEQQILEYKE HLEKNFSAKL ENAQLAAAKN SDYASATREE IMATKLRVDT
LSSQLNHYQK QNSALEAKVR DLQDMLDRAH DMHRRQMTEK DREVTEIRQT LQGQLEEYEQ
LLDVKLALDM EINAYRKMLE GEEQRLKLSP SPSQRSTVSR ASTSQTSRLL RGKKRKLDET
GRSVTKRSYK VVQQASSTGP VSVEDIDPEG NYVRLLNNTE EDFSLHGWVV KRMHMSLPEI
AFKLPCRFIL KSSQRVTIWA AGAGAVHSPP TDLVWKSQKT WGTGDNIKIT LLDSTGEECA
ERTLYRVIGE EGETDEDFVE EEELERQFRS QSHQSVDPSC SIM
