ID A0A1S3J667_LINUN Unreviewed; 1071 AA.
AC A0A1S3J667;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Nuclear factor NF-kappa-B p105 subunit isoform X1 {ECO:0000313|RefSeq:XP_013405334.1};
GN Name=LOC106170138 {ECO:0000313|RefSeq:XP_013405334.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013405334.1};
RN [1] {ECO:0000313|RefSeq:XP_013405334.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013405334.1};
RG RefSeq;
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 RefSeq; XP_013405334.1; XM_013549880.1.
DR AlphaFoldDB; A0A1S3J667; -.
DR EnsemblMetazoa; XM_013549880.1; XP_013405334.1; LOC106170138.
DR GeneID; 106170138; -.
DR KEGG; lak:106170138; -.
DR OrthoDB; 1059550at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08310; Death_NFkB-like; 1.
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:SF28; NUCLEAR FACTOR NF-KAPPA-B P110 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; 4.
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}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 67..263
FT /note="RHD"
FT /evidence="ECO:0000259|PROSITE:PS50254"
FT REPEAT 671..703
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 747..779
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 781..814
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 815..847
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 845..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..860
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 116356 MW; BA0B9799E8CC8F2E CRC64;
MVDESEDSLD LTGHYSAEED HDVRIAMAVG EAGPKQNGNN NLYPTTMNGV AAEVTPVING
FGSNTVGDEP YLEIVEEPQS RGFRFRYKCE GGSHGGLQGE NSEKGKKTYP TVRINNWTGA
ARIVVSLVTD EEVPKTHAHE LVGKNCQNGI CLVELKGGSN NTATFPNMGV QHITRRNLVN
VLSERIQESI RLNHVLVTGN PNAGLTEAEK NQAKEQAEEQ AKGMHLSTVR LCFQAYLMDE
NGTYSRMLPS VISKQIYDCK APGAAALKIC RLDRQAGSVR GNDEVFLLCD KVQKDDIAVR
FFEEDEDGRL KWEAYGNFGP PDVHRQYAIV FRTPPYWNVN IAKAVVVRMQ LMRRSDRAIS
DPKPFTYFPE VADMDEISKK RKKTVGFPFS RYGGSGGSSG GYSSGGSGGG GSGLVGPAGG
TGAGGSATYN FAGTSQGVNR PVNPPMMKGS GYVQQPSLST QPISNLNGNM SRANQHPIKM
QNIGGSMAAP SFPHYGPTDS EDLVTDSAPD FDDMNMFSPP YDSSSNQPYY GYPQKGLLAR
GTISVGKENN WKSDMENITS KTKQMGLDEV PIPTKGTSAP EPQPDSLSQQ NNDLVMRLAA
RTAEALQDYA ATGDTKALLA VQRHLVGVQD EAGDNCVHIA VIHKRVEACK NLLSVAVTIP
NSNIVNQLNK RRQTPLHLAV LTQQPLVVDL LLKSGADPYI VDLHGNTATH LAAELGSKGC
LEVLLKYMRL NTSPSNPFPE LAMYNYEGFA PVHLAALCGS LQALKVILRV QTDVNIQDGK
SGRTALHHAV EKEDLALVGC LLLEAGADVN ATTYDGNTAL HLACGRECTG MVALLMAAGA
DPNIENSELL EEEKDDEGDG VDEEEKKKND PEEDLIGHTA FDLAWRNAKI QKILNGEPYS
TFRDVEDHSA HLIKSGGKVY TLSQDSGLGS SSVTGDLDKL DYMSRVSLAK LLDPCKTDQD
WEAVAKYLDL GHLVSTFRPQ KSPTLSLLDN YEVLDGTISQ LTQCLKELGR TDAIAIIEEL
QELASEVKKT GIHSSVKQLI PPRRGQEPEK CDSGVESFFT PDDTRQEIVT H
//