LAML2_XENLA
ID LAML2_XENLA Reviewed; 623 AA.
AC P21910;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Lamin-L(II);
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=2102682; DOI=10.1007/bf01726689;
RA Hoeger T.H., Zatloukal K., Waizenegger I., Krohne G.;
RT "Characterization of a second highly conserved B-type lamin present in
RT cells previously thought to contain only a single B-type lamin.";
RL Chromosoma 99:379-390(1990).
RN [2]
RP ERRATUM OF PUBMED:2102682.
RX PubMed=2102440; DOI=10.1007/bf00337604;
RA Hoeger T.H., Zatloukal K., Waizenegger I., Krohne G.;
RL Chromosoma 100:67-69(1990).
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; X54099; CAA38033.1; -; mRNA.
DR PIR; A48315; A48315.
DR RefSeq; NP_001095239.1; NM_001101769.1.
DR AlphaFoldDB; P21910; -.
DR SMR; P21910; -.
DR GeneID; 397912; -.
DR KEGG; xla:397912; -.
DR CTD; 397912; -.
DR Xenbase; XB-GENE-865968; lmnb2.L.
DR OrthoDB; 701388at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 397912; Expressed in gastrula and 18 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..620
FT /note="Lamin-L(II)"
FT /id="PRO_0000063824"
FT PROPEP 621..623
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396783"
FT DOMAIN 35..391
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 468..585
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..27
FT /note="Head"
FT REGION 28..64
FT /note="Coil 1A"
FT REGION 64..74
FT /note="Linker 1"
FT REGION 75..211
FT /note="Coil 1B"
FT REGION 212..235
FT /note="Linker 2"
FT REGION 236..378
FT /note="Coil 2"
FT REGION 380..592
FT /note="Tail"
FT REGION 388..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 420..425
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 397..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT MOD_RES 620
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 620
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 623 AA; 71470 MW; A7E874548B81ED0E CRC64;
MATTTPSRST RSSMQSPARG TSTPLSPTRI SRLQEKEELR HLNDRLAVYI DRVRALELEN
DRLMVKISEK EEVTTREVSG IKNLYESELA DARKVLDETA RERARLQIEL GKFRSDLDEL
NKNYKKKDAD LSTAQGRIKD LEALFHRSEA ELGTALGEKR SLEAEVADLR AQLSKTEDAH
RVAKKQLEKE TLMRVDFENR MQSLQEEMDF RKNIYEEESR ETRKRHERRI VEVDRGHHYD
YESKLAQALD ELRKQHDEQV KMYKEELEQT YQAKLDNIKR SSDHNDKAAN TALEELTERR
MRIETLGYQL SGLQKQANAA EERIRELEEL LSSDRDKYRK LLDSKEREMA EMRDQMQQQL
NEYQELLDVK LALDLEINAY RKLLEGEEER LKLSPSPESR VTVSRATSSS SSATRTSRSK
RRRVEEEYEE GGASTGFGAG HSLGSSRITA SEGSSRTITS GQSSTTRFHL SQQASATGSI
SIEEIDLEGK YVHLKNNSDK DQSLGNWRLK RKIGEEEEIV YKFTPKYVLK AGQSVKIYSA
DAGVAHSPPS ILVWKNQSSW GTGSNIRTYL VNTEEEEVAV RTVTKSVLRN VEEEEDEDAD
FGEEDLFHQQ GDPRTTSRGC SVM
