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IKBL1_MACMU
ID   IKBL1_MACMU             Reviewed;         381 AA.
AC   Q5TM19;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
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;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15269276; DOI=10.1093/molbev/msh216;
RA   Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT   "Rhesus macaque class I duplicon structures, organization, and evolution
RT   within the alpha block of the major histocompatibility complex.";
RL   Mol. Biol. Evol. 21:2079-2091(2004).
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}.
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DR   EMBL; AB128049; BAD69726.1; -; Genomic_DNA.
DR   RefSeq; NP_001040609.1; NM_001047144.1.
DR   AlphaFoldDB; Q5TM19; -.
DR   SMR; Q5TM19; -.
DR   STRING; 9544.ENSMMUP00000011586; -.
DR   GeneID; 715283; -.
DR   KEGG; mcc:715283; -.
DR   CTD; 4795; -.
DR   eggNOG; ENOG502QTMZ; Eukaryota.
DR   HOGENOM; CLU_054217_0_0_1; -.
DR   InParanoid; Q5TM19; -.
DR   OMA; DEFCETF; -.
DR   TreeFam; TF333242; -.
DR   Proteomes; UP000006718; Unplaced.
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..381
FT                   /note="NF-kappa-B inhibitor-like protein 1"
FT                   /id="PRO_0000067010"
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          186..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..294
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..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..285
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   381 AA;  43144 MW;  1E2E04AF44054484 CRC64;
     MSNPSPQVPE EEASTSVCRP KSSMASTSRR QRRERRFRRY LSAGRLVRAQ ALLQRHPGLD
     VDAGQPPPLH RACARHDAPA LCLLLRLGAD PAHQDRHGDT ALHAAARQGP DAYTDFFLPL
     LSRCPSAMGI KNKDGETPGQ ILGWGPPWDS AEEEEEDDAS KEREWRQKLQ GELEDEWQEV
     MGRFEGDASH ETQEPESFSA WSDRLAREHA QKCQQQQREA EGSCRPPRAE GSSQSWRQQE
     EEQRLFRERA RVKEEELRES RARRAQEALG DREPKPARAG PRAEHPRGAG RGSLWRFGDV
     PWPCPGGGDP EAMAAALVAR GPPLEEQGAL RRYLRVQQVR WHPDRFLQRF RSQIETWELG
     RVMGAVTALS QALNRHAEAL K
 
 
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