ID A0A2Y9NB16_DELLE Unreviewed; 314 AA.
AC A0A2Y9NB16;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=NF-kappa-B inhibitor alpha {ECO:0000256|ARBA:ARBA00041123};
DE AltName: Full=I-kappa-B-alpha {ECO:0000256|ARBA:ARBA00041987};
GN Name=NFKBIA {ECO:0000313|RefSeq:XP_022426423.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022426423.1};
RN [1] {ECO:0000313|RefSeq:XP_022426423.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022426423.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the NF-kappa-B inhibitor family.
CC {ECO:0000256|ARBA:ARBA00038439}.
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DR RefSeq; XP_022426423.1; XM_022570715.2.
DR AlphaFoldDB; A0A2Y9NB16; -.
DR STRING; 9749.A0A2Y9NB16; -.
DR Ensembl; ENSDLET00000018560; ENSDLEP00000016822; ENSDLEG00000012342.
DR KEGG; dle:111173225; -.
DR InParanoid; A0A2Y9NB16; -.
DR OrthoDB; 621606at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR GO; GO:0008139; F:nuclear localization sequence binding; IEA:Ensembl.
DR GO; GO:0140311; F:protein sequestering activity; IEA:Ensembl.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0010888; P:negative regulation of lipid storage; IEA:Ensembl.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0070427; P:nucleotide-binding oligomerization domain containing 1 signaling pathway; IEA:Ensembl.
DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; IEA:Ensembl.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IEA:Ensembl.
DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
DR GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
DR GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR PANTHER; PTHR46680; NF-KAPPA-B INHIBITOR ALPHA; 1.
DR PANTHER; PTHR46680:SF1; NF-KAPPA-B INHIBITOR ALPHA; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 110..142
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 182..214
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 216..248
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 314 AA; 35245 MW; 214B296E92E5E919 CRC64;
MFQPAEPGQE WAMEGPRDAL KKERLLDDRH DSGLDSMKDE EYEQMVKELR EIRLEPQEAP
RGAEPWKQQV TEDGDSFLHL AIIHEEKVLT MEVVRQVKGD LAFLNFQNNL QQTPLHLAVI
TNQPEIAEAL LEAGCDPELR DFRGNTPLHL ACEQGCLASV GVLTQPRGTQ HLHSILQATN
YNGHTCLHLA SIHGYLGIVE LLVSLGADVN AQEPCNGRTA LHLAVDLQNP DLVSLLLKCG
ADVNRVTYQG YSPYQLTWGR PSTRIQQQLG QLTLENLQML PESEDEESYD TESEFTEDEL
PYDDCVLGGQ RLTL
//
