ID   AZI2_RAT                Reviewed;         404 AA.
AC   Q4KMA0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=5-azacytidine-induced protein 2;
GN   Name=Azi2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Adapter protein which binds TBK1 and IKBKE playing a role in
CC       antiviral innate immunity (By similarity). Activates serine/threonine-
CC       protein kinase TBK1 and facilitates its oligomerization (By
CC       similarity). Enhances the phosphorylation of NF-kappa-B p65 subunit
CC       RELA by TBK1 (By similarity). Promotes TBK1-induced as well as TNF-
CC       alpha or PMA-induced activation of NF-kappa-B (By similarity).
CC       Participates in IFNB promoter activation via TICAM1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9H6S1}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with IKBKE, TBK1 and
CC       TICAM1 (By similarity). {ECO:0000250|UniProtKB:Q9H6S1,
CC       ECO:0000250|UniProtKB:Q9QYP6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H6S1}.
CC   -!- PTM: Ubiquitinated via 'Lys-48'-linked polyubiquitination by TRIM38,
CC       leading to its degradation. {ECO:0000250|UniProtKB:Q9QYP6}.
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DR   EMBL; BC098680; AAH98680.1; -; mRNA.
DR   RefSeq; NP_001020876.1; NM_001025705.1.
DR   AlphaFoldDB; Q4KMA0; -.
DR   SMR; Q4KMA0; -.
DR   STRING; 10116.ENSRNOP00000013449; -.
DR   iPTMnet; Q4KMA0; -.
DR   PhosphoSitePlus; Q4KMA0; -.
DR   jPOST; Q4KMA0; -.
DR   PaxDb; Q4KMA0; -.
DR   PRIDE; Q4KMA0; -.
DR   GeneID; 316051; -.
DR   KEGG; rno:316051; -.
DR   UCSC; RGD:1310530; rat.
DR   CTD; 64343; -.
DR   RGD; 1310530; Azi2.
DR   eggNOG; ENOG502QV07; Eukaryota.
DR   InParanoid; Q4KMA0; -.
DR   PhylomeDB; Q4KMA0; -.
DR   PRO; PR:Q4KMA0; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0097028; P:dendritic cell differentiation; ISO:RGD.
DR   GO; GO:0044565; P:dendritic cell proliferation; ISO:RGD.
DR   GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR   GO; GO:0000278; P:mitotic cell cycle; ISO:RGD.
DR   GO; GO:0042110; P:T cell activation; ISO:RGD.
DR   InterPro; IPR024581; TBD.
DR   Pfam; PF12845; TBD; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..404
FT                   /note="5-azacytidine-induced protein 2"
FT                   /id="PRO_0000280606"
FT   REGION          1..198
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QYP6"
FT   REGION          229..269
FT                   /note="Interaction with TBK1 and IKBKE"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6S1"
FT   REGION          332..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          40..198
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        356..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         330
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         365
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6S1"
SQ   SEQUENCE   404 AA;  45986 MW;  7F438E9E15BAC1DB CRC64;
     MDTLVEDDIC ILNHEKAHKR EAVTPLSAYP GDESVASHFA LVTAYEDIKK RLKDSEKENS
     FLKKRIRALE EKLVGARVEE ETSSVGREQV NKAYHAYREV CIDRDNLKSR LEKISKDNSE
     SLRALTEQLQ CKEVELLQLR TEVETQQVMR NLNPPSSNWE VEKLSCDLKI HGLEQELELL
     RKECSDLRTE LQKARQTGPS QEDILQDRDV IRPSLPREEH VPHQGPHHSD HMQHAYWELR
     REMANLHLVT RVQAELLRQL KTAAAGKACT QVGCVEDLGR DSAKLHLANC TAAYKRHPPL
     SPHGKATCYA PPSTLPGDRK AFSDKAVLQS WTDNERLTPN DGADFQEHNS YGRNSLEDNS
     WVFPSPPKSS ETAFGESKSK ILPSPNLPPL HYLDQHNQNC LYKS