LMNA_CHICK
ID LMNA_CHICK Reviewed; 657 AA.
AC P13648;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Lamin-A;
DE Flags: Precursor;
GN Name=LMNA;
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.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P02545}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X16879; CAA34762.1; -; mRNA.
DR PIR; S05517; S05517.
DR RefSeq; NP_990618.1; NM_205287.1.
DR AlphaFoldDB; P13648; -.
DR SMR; P13648; -.
DR BioGRID; 676484; 1.
DR IntAct; P13648; 1.
DR PRIDE; P13648; -.
DR GeneID; 396224; -.
DR KEGG; gga:396224; -.
DR CTD; 4000; -.
DR VEuPathDB; HostDB:geneid_396224; -.
DR InParanoid; P13648; -.
DR OrthoDB; 701388at2759; -.
DR PhylomeDB; P13648; -.
DR PRO; PR:P13648; -.
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..654
FT /note="Lamin-A"
FT /id="PRO_0000063814"
FT PROPEP 655..657
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403465"
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..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..32
FT /note="Head"
FT REGION 33..69
FT /note="Coil 1A"
FT REGION 70..79
FT /note="Linker 1"
FT REGION 80..217
FT /note="Coil 1B"
FT REGION 218..241
FT /note="Linker 2"
FT REGION 242..382
FT /note="Coil 2"
FT REGION 383..657
FT /note="Tail"
FT REGION 383..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..621
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 654
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 654
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 657 AA; 73164 MW; FD0B31828A77AF08 CRC64;
MSTPSQRRSG RGGGPSGTPL SPTRITRLQE KEDLQELNDR LAVYIDKVRS LELENAGLRL
RITESEEVVS REVSGIKAAY EAELADARKT LDSVAKERAR LQLELSKVRE EHKELKARNA
KKEADLLAAQ ARLKDLEALL NSKEAALSTA LGEKRNLENE VRDLRAQVAK LEGALSEAKK
QLQDEMLRRV DAENRLQTLK EELEFQKNIY SEELRETKRR HETRLVEIDN GRQQEFESKL
AEALQDLRRQ HEDQIRHYRD ELEKTYGAKL ENAKQSAERN SSMAGAAHEE LQQTHIRIDS
LSAELSQLQK QLAAKEAKLR EVEEALSRER EGGRRLLAEK EREMAEMRAR MQQQLDEYQE
LLDIKLALDM EINAYRKLLE GEEERLRLSP SPSSQRGARS SGLQHSGAGS AKKRRLEDGE
GREGREGRTS FSHHARTSGR VGVEEVDLEG RFVRLRNKSN EDQALGNWQV KRQNGDDPPL
TYRFPPKFTL KAGQAVTIWA SGAGATHSPP SDVVWKAQSS WGSGDSLRTA LINSNGEEVA
MRKLVRTVII NDDDEDEEDD EVSIHHRHHH SGCSGSADPA EYNLRSRTVL CGTCGQPADK
GSAAAASSAS SASTVTVSRG YRSSGGGIGE GLLGRSYVLG GAGPRRQAPA PQGCSIM
