ID   LMN2_HYPDU              Reviewed;         614 AA.
AC   A0A125S9M5;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Lamin-2 {ECO:0000303|PubMed:26840051};
DE   Flags: Precursor;
OS   Hypsibius dujardini (Water bear) (Macrobiotus dujardini).
OC   Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC   Hypsibioidea; Hypsibiidae; Hypsibius.
OX   NCBI_TaxID=232323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, SUBCELLULAR LOCATION,
RP   ISOPRENYLATION AT CYS-611, AND DOMAIN.
RX   PubMed=26840051; DOI=10.7554/elife.11117;
RA   Hering L., Bouameur J.E., Reichelt J., Magin T.M., Mayer G.;
RT   "Novel origin of lamin-derived cytoplasmic intermediate filaments in
RT   tardigrades.";
RL   Elife 5:E11117-E11117(2016).
CC   -!- FUNCTION: Intermediate filament (IF) protein, component of the nuclear
CC       lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear
CC       membrane, which is thought to provide a framework for the nuclear
CC       envelope (PubMed:26840051). {ECO:0000305|PubMed:26840051}.
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Lipid-anchor;
CC       Nucleoplasmic side {ECO:0000269|PubMed:26840051}. Note=Localization is
CC       restricted to the nuclear periphery which is consistent with the
CC       presence of a C-terminal isoprenylation motif (PubMed:26840051).
CC       {ECO:0000269|PubMed:26840051}.
CC   -!- DOMAIN: Contains an alpha-helical IF rod domain organization with three
CC       coiled coil-forming segments (coil 1A, coil 1B, and coil 2)
CC       (PubMed:26840051). {ECO:0000305|PubMed:26840051}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; KU295461; AME17871.1; -; mRNA.
DR   AlphaFoldDB; A0A125S9M5; -.
DR   SMR; A0A125S9M5; -.
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; 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; PS51842; IF_ROD_2; 1.
DR   PROSITE; PS51841; LTD; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Intermediate filament; Lipoprotein; Membrane; Nucleus;
KW   Prenylation.
FT   CHAIN           1..611
FT                   /note="Lamin-2"
FT                   /id="PRO_0000440215"
FT   PROPEP          612..614
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT                   /id="PRO_0000440216"
FT   DOMAIN          81..433
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188,
FT                   ECO:0000305|PubMed:26840051"
FT   DOMAIN          462..581
FT                   /note="LTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT   REGION          1..76
FT                   /note="Head"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..117
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          118..128
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          129..268
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          269..286
FT                   /note="Linker 2"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          287..426
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          427..611
FT                   /note="Tail"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   REGION          433..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           449..458
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000305|PubMed:26840051"
FT   COMPBIAS        1..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           611
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:26840051"
SQ   SEQUENCE   614 AA;  69565 MW;  9F92BC162350F528 CRC64;
     MSAQVSKKRG GSNPPKTGQH AASSTTSRTE SSATSQTIYE RQEVETRTQR TPGGLLLAAS
     SAEVSSGTAG LAGSPLSRHQ EKEEFKLLNN RFANYIDTIR AQQEEISVLR RKVETVSSKE
     VVENQKIKER YNLEIANLRR ALDEVSRDLA AAIIERDSLR PERDARLLLD NEKKTLQKRS
     KDAEAALKDA KNQLAALRDQ AKDHDNEIHG LTTENSSLKL QIENLKKDLS QETNLRVDAE
     NRLQSEREKN ALLEGIHNEE IVSLRNQRRT EITEVETRMG EEYQSKIVEQ LNDLRADLEA
     VAHEMRLDLE RSYQNQLEDS QDLANRYRDE ARALLADLSA AQDRIKETQT RSEKQLQELR
     LQLQRLQAEL NGKDDEVQRL QKLLADRQAE LQNTHHELSR QIASYQELLD EKIHLDAELA
     TYNALLRTEE ERLNMKSPPF PSTPDSQRRG TKRRIADSYT RTRFRNEASA TGDIHISEID
     AEGQFVRLEN KSGQDVVIGG WKLLMVSDNG EDNKTDYKIH SNQVIKAHSS TTIWSANTNV
     VHEPPADIVM EGRWLVGDHT SVTLSTSDGV EVARREMTQS STRDDSYLGP SGLPKRSRLV
     VADSSDHQKN CVIM