ID   IKBA_CHICK              Reviewed;         318 AA.
AC   Q91974;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=NF-kappa-B inhibitor alpha;
DE   AltName: Full=I-kappa-B-alpha;
DE            Short=IkB-alpha;
DE            Short=IkappaBalpha;
DE   AltName: Full=REL-associated protein pp40;
GN   Name=NFKBIA; Synonyms=IKBA;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=1891714; DOI=10.1126/science.1891714;
RA   Davis N., Ghosh S., Simmons D.L., Tempst P., Liou H.-C., Baltimore D.,
RA   Bose H.R. Jr.;
RT   "Rel-associated pp40: an inhibitor of the rel family of transcription
RT   factors.";
RL   Science 253:1268-1271(1991).
CC   -!- FUNCTION: Inhibits NF-kappa-B by complexing with and trapping it in the
CC       cytoplasm. May be involved in regulation of transcriptional responses
CC       to NF-kappa-B, including cell adhesion, immune and pro-inflammatory
CC       responses, apoptosis, differentiation and growth. Controlled by
CC       sequential serine-phosphorylation, ubiquitination and degradation.
CC       Tyrosine-phosphorylation could only lead to dissociation from NF-kappa-
CC       B (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RELA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Highly expressed in lymph node, thymus followed by
CC       liver, brain, muscle, kidney, gastrointestinal and reproductive tract.
CC   -!- PTM: Ubiquitinated; subsequent to stimulus-dependent phosphorylation on
CC       serines, polyubiquitination targets the protein for rapid degradation
CC       via the ubiquitin system. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NF-kappa-B inhibitor family. {ECO:0000305}.
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; S55765; AAB19758.1; -; mRNA.
DR   EMBL; M74544; AAA49030.1; -; mRNA.
DR   PIR; I51192; I51192.
DR   AlphaFoldDB; Q91974; -.
DR   SMR; Q91974; -.
DR   IntAct; Q91974; 1.
DR   STRING; 9031.ENSGALP00000041417; -.
DR   PaxDb; Q91974; -.
DR   VEuPathDB; HostDB:geneid_396093; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   InParanoid; Q91974; -.
DR   OrthoDB; 1341288at2759; -.
DR   PhylomeDB; Q91974; -.
DR   Reactome; R-GGA-1227892; TRAF6 mediated NF-kB activation.
DR   Reactome; R-GGA-434001; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
DR   Reactome; R-GGA-434131; NFkB activation mediated by RIP1 complexed with activated TLR3.
DR   PRO; PR:Q91974; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0051059; F:NF-kappaB binding; IBA:GO_Central.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
DR   GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IBA:GO_Central.
DR   GO; GO:0048145; P:regulation of fibroblast proliferation; NAS:UniProtKB.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   2: Evidence at transcript level;
KW   ANK repeat; Cytoplasm; Isopeptide bond; Phosphoprotein; Reference proteome;
KW   Repeat; Ubl conjugation.
FT   CHAIN           1..318
FT                   /note="NF-kappa-B inhibitor alpha"
FT                   /id="PRO_0000067003"
FT   REPEAT          114..143
FT                   /note="ANK 1"
FT   REPEAT          147..176
FT                   /note="ANK 2"
FT   REPEAT          186..215
FT                   /note="ANK 3"
FT   REPEAT          220..249
FT                   /note="ANK 4"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Phosphoserine; by IKKA and IKKB"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         40
FT                   /note="Phosphoserine; by IKKA, IKKB and IKKE"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         46
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        21
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  35399 MW;  2EF1BFB21B54E29F CRC64;
     MLSAHRPAEP PAVEGCEPPR KERQGGLLPP DDRHDSGLDS MKEEEYRQLV RELEDIRLQP
     REPPARPHAW AQQLTEDGDT FLHLAIIHEE KALSLEVIRQ AAGDAAFLNF QNNLSQTPLH
     LAVITDQAEI AEHLLKAGCD LDVRDFRGNT PLHIACQQGS LRSVSVLTQH CQPHHLLAVL
     QATNYNGHTC LHLASIQGYL AVVEYLLSLG ADVNAQEPCN GRTALHLAVD LQNSDLVSLL
     VKHGPDVNKV TYQGYSPYQL TWGRDNASIQ EQLKLLTTAD LQILPESEDE ESSESEPEFT
     EDELMYDDCC IGGRQLTF