ID   IKBL1_PIG               Reviewed;         380 AA.
AC   Q9TSV7; A5D9N1;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=NF-kappa-B inhibitor-like protein 1;
DE   AltName: Full=Inhibitor of kappa B-like protein;
DE            Short=I-kappa-B-like protein;
DE            Short=IkappaBL;
DE   AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 1;
GN   Name=NFKBIL1; Synonyms=IKBL;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Large white; TISSUE=Fibroblast;
RX   PubMed=11169259; DOI=10.1034/j.1399-0039.2001.057001055.x;
RA   Chardon P., Rogel-Gaillard C., Cattolico L., Duprat S., Vaiman M.,
RA   Renard C.;
RT   "Sequence of the swine major histocompatibility complex region containing
RT   all non-classical class I genes.";
RL   Tissue Antigens 57:55-65(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Porcine genome sequencing project;
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the regulation of innate immune response. Acts as
CC       negative regulator of Toll-like receptor and interferon-regulatory
CC       factor (IRF) signaling pathways. Contributes to the negative regulation
CC       of transcriptional activation of NF-kappa-B target genes in response to
CC       endogenous pro-inflammatory stimuli (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CACTIN (via N-terminal domain); the interaction
CC       occurs in a pro-inflammatory-independent manner. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Nuclear localization
CC       with a speckled expression pattern in some cells. Colocalizes with
CC       CACTIN in the nucleus (By similarity). {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ251914; CAB63854.1; -; Genomic_DNA.
DR   EMBL; BX548169; CAN59681.1; -; Genomic_DNA.
DR   EMBL; AJ251914; CAN59681.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q9TSV7; -.
DR   SMR; Q9TSV7; -.
DR   STRING; 9823.ENSSSCP00000001489; -.
DR   PaxDb; Q9TSV7; -.
DR   Ensembl; ENSSSCT00045065897; ENSSSCP00045046666; ENSSSCG00045038092.
DR   Ensembl; ENSSSCT00070048183; ENSSSCP00070040676; ENSSSCG00070024131.
DR   eggNOG; ENOG502QTMZ; Eukaryota.
DR   InParanoid; Q9TSV7; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 7.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR   GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR   GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR038753; NFKBIL1.
DR   PANTHER; PTHR15263; PTHR15263; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
PE   3: Inferred from homology;
KW   ANK repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..380
FT                   /note="NF-kappa-B inhibitor-like protein 1"
FT                   /id="PRO_0000067013"
FT   REPEAT          64..93
FT                   /note="ANK 1"
FT   REPEAT          97..133
FT                   /note="ANK 2"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         150
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBC1"
SQ   SEQUENCE   380 AA;  43031 MW;  361E0D9DBAD34103 CRC64;
     MSNPSPQVPE GEASTSVCRP KSSMASTSRR QRRERRFRRY LSAGRLVRAQ ALLQRHPGLD
     VDAGQPPPLH RACARHDAPA LCLLLRLGAD PAHQDRHGDT ALHAAARQGP DAYTDFFLPL
     LSRCPSAMGI KNKDGETPGQ ILGWGPPWDS AEEEEEDEAS KEREWRQKLQ GELEDEWQEV
     IGRFEDDASH ETQEPESFSA WSDRMAREHA QKRQQQRETE GACRPPRAEG SSHSWRQQEE
     EQRLFRERAR AKEEELRESQ ARRAQEAPRD PVPEPARAGP RAEHPRGAGR GSLWRFGDVP
     WPCPGGGDPE AMAAALVARG PPLEEQGALR RYLRVQQVRW HPDRFLQRFR SQIETWELGR
     VMGAVTALSQ ALNRHAEALK