LMNB1_CHICK
ID LMNB1_CHICK Reviewed; 584 AA.
AC P14731;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Lamin-B1;
DE Flags: Precursor;
GN Name=LMNB1;
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=2795656; DOI=10.1016/0022-2836(89)90504-4;
RA Peter M., Kitten G.T., Lehner C.F., Vorburger K., Bailer S.M., Maridor G.,
RA Nigg E.A.;
RT "Cloning and sequencing of cDNA clones encoding chicken lamins A and B1 and
RT comparison of the primary structures of vertebrate A- and B-type lamins.";
RL J. Mol. Biol. 208:393-404(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:P20700}.
CC -!- SUBUNIT: Homodimer. Interacts with lamin-associated polypeptides IA, IB
CC and 2. {ECO:0000250|UniProtKB:P20700}.
CC -!- SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000250|UniProtKB:P20700}.
CC -!- PTM: Phosphorylated. Phosphorylation is increased before envelope
CC disintegration and probably plays a role in regulating lamin
CC associations (By similarity). {ECO:0000250}.
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; X16878; CAA34761.1; -; mRNA.
DR PIR; S05518; S05518.
DR RefSeq; NP_990617.1; NM_205286.1.
DR AlphaFoldDB; P14731; -.
DR SMR; P14731; -.
DR BioGRID; 676483; 1.
DR STRING; 9031.ENSGALP00000023635; -.
DR PaxDb; P14731; -.
DR GeneID; 396223; -.
DR KEGG; gga:396223; -.
DR CTD; 4001; -.
DR VEuPathDB; HostDB:geneid_396223; -.
DR eggNOG; KOG0977; Eukaryota.
DR InParanoid; P14731; -.
DR OrthoDB; 701388at2759; -.
DR PhylomeDB; P14731; -.
DR PRO; PR:P14731; -.
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; ISS:UniProtKB.
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; ISS:UniProtKB.
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..581
FT /note="Lamin-B1"
FT /id="PRO_0000063819"
FT PROPEP 582..584
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403469"
FT DOMAIN 31..387
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 429..545
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..33
FT /note="Head"
FT REGION 34..70
FT /note="Coil 1A"
FT REGION 81..218
FT /note="Coil 1B"
FT REGION 243..385
FT /note="Coil 2"
FT REGION 386..584
FT /note="Tail"
FT REGION 388..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..584
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 393..407
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 581
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 581
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 584 AA; 66530 MW; 1DEB97EE65B66EA2 CRC64;
MAAAVAPLSP QPRGAAASAA LSPTRISRLQ EKEELRQLND RLAVYIDKVR SLETENSALQ
RRVSEREQVC GREISGLKEL FETELADARK TLDDTARERA KLQIELGKLR AEHEQVLSSY
AKKDSDLNAA QVKLREFEAA LNAKEAALAT ALGDKRSQEE ELEDLRDQIA QLEVSLAAAK
KELADETLQK VDLENRCQSL IEDLEFRKNV YEEEIKETRR KHETRLVEVD SGRQIEYEYK
LAQALKEIRE QHDAQVKLYK EELEQTYSSK LENIRQSSEM HSCTANTVRE ELHESRMRIE
TLSSHIADIQ KESRAWQDRV HELEDTLSKE RENYRKILAE NEREVAEMRN QMQQQFSDYE
QLLDVKLALD MEISAYRKLL ESEEERLRLS PGPSSRVTVS RASSSRSVRT TRGKRKRIDV
EESEASSSVS ISHSASATGN ISIEEIDVDG KFIRLKNTSE QDQPMGGWEM IRKIGDTSAS
YRYTSRYVLK AGQTVTIWAA NAGVTASPPT DLIWKNQNSW GTGEDVKVVL KNSQGEEVAQ
RSTVFKTTVN EGEEEEEEGE EEILEDVIHQ QGSPRKPERS CVVM
