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Database: UniProt
Entry: W5M5I2_LEPOC
LinkDB: W5M5I2_LEPOC
Original site: W5M5I2_LEPOC 
ID   W5M5I2_LEPOC            Unreviewed;       609 AA.
AC   W5M5I2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Lamin B2 {ECO:0000313|Ensembl:ENSLOCP00000003640.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000003640.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000003640.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AHAT01011189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01011190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5M5I2; -.
DR   STRING; 7918.ENSLOCP00000003640; -.
DR   Ensembl; ENSLOCT00000003647.1; ENSLOCP00000003640.1; ENSLOCG00000003086.1.
DR   eggNOG; KOG0977; Eukaryota.
DR   GeneTree; ENSGT00940000160274; -.
DR   HOGENOM; CLU_012560_9_2_1; -.
DR   InParanoid; W5M5I2; -.
DR   OMA; EMTQMRD; -.
DR   Proteomes; UP000018468; Linkage group LG19.
DR   Bgee; ENSLOCG00000003086; Expressed in embryo and 13 other cell types or tissues.
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 formation; 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; 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; 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:SF2; LAMIN-B2; 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   SUPFAM; SSF90257; Myosin rod fragments; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
DR   PROSITE; PS51841; LTD; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Intermediate filament {ECO:0000256|ARBA:ARBA00022754};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT   DOMAIN          52..408
FT                   /note="IF rod"
FT                   /evidence="ECO:0000259|PROSITE:PS51842"
FT   DOMAIN          457..574
FT                   /note="LTD"
FT                   /evidence="ECO:0000259|PROSITE:PS51841"
FT   REGION          25..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          56..224
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          320..390
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        26..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  68980 MW;  62B54D5848D99300 CRC64;
     KPRSPSTNSN VSRPIVCVCE MATATPSRSA AGTPRQSADT PLSPTRISRL QEKEELRHLN
     DRLAVYIDRV RALELENDRL MVKVSEKEEV TTREVTGIKS LYEVELADAR RVLDETARDR
     ARLQIDLGKA NAELEEVTRN YKKKDGDLAA AQARIKELEA QCNKSGADLN TALSENRALL
     AEVNELKAQL AKAEDAHTVA KKQLEAETLM RVDLENRCQS LQEDLNFRKN IYDEEVQETR
     RRHERRMVEV DSGRQQEYEY KLSAALQDLR RQHDEQVAIY KQELENTFQA KLENAKVSSD
     MNDKAVSTAR EELQEAHMRI ESLGYQLTAL QKQASAAEER IRELEDLLAS DRDKYRRQLD
     AKEREMAEMR DQMQQQLNEY QELLDVKLAL DMEISAYNKL LEGEESRLKL SPSPSSRVTV
     SRVTSSSLAS ASVTRSSRAK RKRVEMEESG TVGQPRFQIS QQAETTGSIT IEEIDLEGKS
     VTLKNNAEKD QSLGNWRLKR RIGDGDEIAY KFTPKYLLKA GQTVTVWSAD AGVTHAPPSN
     LLWKTQSSWG TGDDIVTFLV NSDGEEVAKR TVTKSLVEVE EEEDADFGEE DLFHQQGDPK
     AASRECLIM
//
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