ID A0A2Y9M085_DELLE Unreviewed; 664 AA.
AC A0A2Y9M085;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Lamin isoform X1 {ECO:0000313|RefSeq:XP_022415115.1};
GN Name=LMNA {ECO:0000313|RefSeq:XP_022415115.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022415115.1};
RN [1] {ECO:0000313|RefSeq:XP_022415115.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022415115.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000256|ARBA:ARBA00024186}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000256|RuleBase:RU000685}.
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DR RefSeq; XP_022415115.1; XM_022559407.2.
DR AlphaFoldDB; A0A2Y9M085; -.
DR STRING; 9749.A0A2Y9M085; -.
DR Ensembl; ENSDLET00000030031; ENSDLEP00000027322; ENSDLEG00000019723.
DR KEGG; dle:111167038; -.
DR InParanoid; A0A2Y9M085; -.
DR OrthoDB; 72418at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005638; C:lamin filament; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; IEA:Ensembl.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:Ensembl.
DR GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0072201; P:negative regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
DR GO; GO:0006998; P:nuclear envelope organization; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
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; 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 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Intermediate filament {ECO:0000256|ARBA:ARBA00022754,
KW ECO:0000256|RuleBase:RU000685};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023289};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT DOMAIN 31..387
FT /note="IF rod"
FT /evidence="ECO:0000259|PROSITE:PS51842"
FT DOMAIN 428..545
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..369
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 391..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 74137 MW; 31A88A3EFF9369E8 CRC64;
METPSQRRAT RGGAQGSSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR SLETENAGLR
LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA RLQLELSKVR EEFKDLKARN
TKKEGDLMAA QARLKDLEAL LNSKEAALST ALSEKRTLEG ELHDLRGQVA KLEAALSEAK
KQLQDEMLRR VDAENRLQTL KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR
LADALQELRA QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLMGAAHE ELQQSRVRID
SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAD KEREMAEMRA RMQQQLDEYQ
ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG RASSHSSQTQ SGGSITKKRK
LESTESRSSF SQHARTSGRV AVEEVDEEGK FVRLRNKSNE DQSMGNWQIK RQNGDDPLLT
YRFPPKFTLK AGQVVTIWAA GAGATHSPPT DLVWKAQSTW GCGNSLRTAL INSTGEEVAM
RKLVRSVTMV EDDEDEDGDD LLHHHHGSHG SSSGDPAEYN LRSRTVLCGT CGQPADKASA
SSSGAQVGGS ISSGSSASSV AVTRSYRGVG GSGGGSFGDS LVTRSYLLGN SRLRTQSPQN
CSIM
//
