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Database: UniProt
Entry: W5N2L1_LEPOC
LinkDB: W5N2L1_LEPOC
Original site: W5N2L1_LEPOC 
ID   W5N2L1_LEPOC            Unreviewed;       987 AA.
AC   W5N2L1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Nuclear factor kappa B subunit 1 {ECO:0000313|Ensembl:ENSLOCP00000014870.1};
GN   Name=NFKB1 {ECO:0000313|Ensembl:ENSLOCP00000014870.1};
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:ENSLOCP00000014870.1, 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:ENSLOCP00000014870.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AHAT01017793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01017794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015200704.1; XM_015345218.1.
DR   RefSeq; XP_015200705.1; XM_015345219.1.
DR   RefSeq; XP_015200706.1; XM_015345220.1.
DR   RefSeq; XP_015200707.1; XM_015345221.1.
DR   AlphaFoldDB; W5N2L1; -.
DR   STRING; 7918.ENSLOCP00000014870; -.
DR   Ensembl; ENSLOCT00000014899.1; ENSLOCP00000014870.1; ENSLOCG00000012080.1.
DR   GeneID; 102693746; -.
DR   KEGG; loc:102693746; -.
DR   CTD; 4790; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00940000158625; -.
DR   InParanoid; W5N2L1; -.
DR   OMA; GCSPNQQ; -.
DR   OrthoDB; 1059550at2759; -.
DR   Proteomes; UP000018468; Linkage group LG4.
DR   Bgee; ENSLOCG00000012080; Expressed in bone element and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0007249; P:canonical NF-kappaB signal transduction; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR   CDD; cd01177; IPT_NFkappaB; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.40.340; Rel homology domain (RHD), DNA-binding domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_dom.
DR   InterPro; IPR033926; IPT_NFkappaB.
DR   InterPro; IPR000451; NFkB/Dor.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR   InterPro; IPR030492; RHD_CS.
DR   InterPro; IPR032397; RHD_dimer.
DR   InterPro; IPR011539; RHD_DNA_bind_dom.
DR   InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR   PANTHER; PTHR24169:SF9; NUCLEAR FACTOR NF-KAPPA-B P105 SUBUNIT; 1.
DR   PANTHER; PTHR24169; NUCLEAR FACTOR NF-KAPPA-B PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF16179; RHD_dimer; 1.
DR   Pfam; PF00554; RHD_DNA_bind; 1.
DR   PRINTS; PR00057; NFKBTNSCPFCT.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00429; IPT; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49417; p53-like transcription factors; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS01204; REL_1; 1.
DR   PROSITE; PS50254; REL_2; 1.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          41..248
FT                   /note="RHD"
FT                   /evidence="ECO:0000259|PROSITE:PS50254"
FT   REPEAT          586..618
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          619..651
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          655..687
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          689..722
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          723..755
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          369..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        954..968
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   987 AA;  106936 MW;  9FEBCD490F9584EC CRC64;
     MAEEDPYLQG GIFDMETFTP LMGMETFNFT AMPPTNSLRV ADGPYLQIIE QPKQRGFRFR
     YGCEGPSHGG LPGASSEKNR KSYPQVKICN YQGPARVVVQ LVTFSKNVNL HAHSLVGKQC
     DKGICVADQQ PKDTSISFPN LGILHVTKKN VNKTLEERMT EAYRMGYNYG ISIHPEIDCL
     QSEGRIPREL TEHQKSLITN AATSQAKEMD LSVVRLMFTA FLPDSDGGFT RRLEPVISDP
     IYDSKAPNAS NLKIVRMDRT AGCVTGGEEV YLLCDKVQKD DIQVRFYEDD ETGLAWEAYG
     DFSPTDVHRQ FAIVFKTPKY RDLNLQKPTS VFVQLKRKSD NETSEPKPFT YHPQVIDKEE
     VQRKRQKTLP NFQDFGPPGA GGGMYRGGGP GTGGGPSTGG GQCNFQGYQG YNNFGGGYPF
     SHGPGGPGAG MKHASKGPTD DAEDDSDSDT DEDPATAGIV QICGQQASEE IKLPPKVEQS
     SSTEDSSPTE DPASAEEEEI TADLLFGEKA MQLAQRHAEA LFNYAVTGDV KMLLAVLRPL
     LAVQDENGDT GLHLGVIHSR TDAVKSLAEV ISALPGDDVL SMRNDLYQTP LHLAVITKQA
     EAVEALLKAG ANMSLTDRHG NTALHLAAKE GEGKILNLLL EHKDAAELID LPNAAGFHAI
     HLAVLANSIL CLRQLIEFGA NVDACEQSSG RTALHLAVEL ENVSLAGCLL LEGNAHVDAC
     TYNGSTALHI AAGKGSMKLT ALLMAAGADP HKENSEPLYD VDDECHLEEE EEDEGFVPGT
     TPLDMAMSSE IYDLLNGKQY QPDSKTVVSL PQGDMKHLDE QTKLELCKVL EQPANNWEAL
     AQNLGLGILS SAFRLSPSPA KTLLDSYKVS GGTMKELLEG LKAMGNDKAV DIVQKAMSSE
     REDTSGPVST QVTHQQTGAL LSQHLQGLEN YSQDESSVCD SGVETSFRKL SLLSSESLSS
     SQEQAEQAGD HKLPTASPHS YVVKGEV
//
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