LMNB2_CHICK
ID LMNB2_CHICK Reviewed; 600 AA.
AC P14732;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Lamin-B2;
DE Flags: Precursor;
GN Name=LMNB2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2477550; DOI=10.1016/0022-2836(89)90505-6;
RA Vorburger K., Lehner C.F., Kitten G.T., Eppenberger H.M., Nigg E.A.;
RT "A second higher vertebrate B-type lamin. cDNA sequence determination and
RT in vitro processing of chicken lamin B2.";
RL J. Mol. Biol. 208:405-415(1989).
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. {ECO:0000250|UniProtKB:Q03252}.
CC -!- SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000250|UniProtKB:Q03252}.
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 -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X16880; CAA34763.1; -; mRNA.
DR PIR; S05519; S05519.
DR RefSeq; NP_990616.1; NM_205285.1.
DR AlphaFoldDB; P14732; -.
DR SMR; P14732; -.
DR BioGRID; 676482; 1.
DR IntAct; P14732; 1.
DR STRING; 9031.ENSGALP00000000639; -.
DR iPTMnet; P14732; -.
DR PaxDb; P14732; -.
DR PRIDE; P14732; -.
DR GeneID; 396222; -.
DR KEGG; gga:396222; -.
DR CTD; 84823; -.
DR VEuPathDB; HostDB:geneid_396222; -.
DR eggNOG; KOG0977; Eukaryota.
DR InParanoid; P14732; -.
DR OrthoDB; 701388at2759; -.
DR PhylomeDB; P14732; -.
DR PRO; PR:P14732; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005652; C:nuclear lamina; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
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 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; Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..597
FT /note="Lamin-B2"
FT /id="PRO_0000063822"
FT PROPEP 598..600
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403472"
FT DOMAIN 25..381
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 445..562
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 2..27
FT /note="Head"
FT REGION 28..64
FT /note="Coil 1A"
FT REGION 75..212
FT /note="Coil 1B"
FT REGION 237..379
FT /note="Coil 2"
FT REGION 377..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..600
FT /note="Tail"
FT REGION 568..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 414..419
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 385..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT MOD_RES 597
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 597
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 600 AA; 67941 MW; 670E2985202211C0 CRC64;
MSGTPIRGTP GGTPLSPTRI SRLQEKEELR QLNDRLAVYI DRVRALELEN DRLLVKISEK
EEVTTREVSG IKNLYESELA DARRVLDETA KERARLQIEI GKLRAELEEF NKSYKKKDAD
LSVAQGRIKD LEVLFHRSEA ELNTVLNEKR SLEAEVADLR AQLAKAEDGH AVAKKQLEKE
TLMRVDLENR CQSLQEDLDF RKNVFEEEIR ETRKRHEHRL VEVDTSRQQE YENKMAQALE
DLRNQHDEQV KLYKMELEQT YQAKLENAIL ASDQNDKAAG AAREELKEAR MRIESLSHQL
SGLQKQASAT EDRIRELKET MAGERDKFRK MLDAKEREMT EMRDQMQLQL TEYQELLDVK
LALDMEISAY RKLLEGEEER LKLSPSPSSR VTVSRATSSS SSSSTSLVRS SRGKRRRIEA
EELSGSGTSG IGTGSISGSS SSSSFQMSQQ ASATGSISIE EIDLEGKYVQ LKNNSEKDQS
LGNWRLKRQI GDGEEIAYKF TPKYVLRAGQ TVTIWGADAG VSHSPPSVLV WKNQGSWGTG
GNIRTYLVNS DGEEVAVRTV TKSVVVRENE EEEDEADFGE EDLFNQQGDP RTTSRGCLVM
