ID   TOIPB_ONCMY             Reviewed;         275 AA.
AC   Q4LBC7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Toll-interacting protein B;
DE   AltName: Full=Toll-interacting protein 2;
GN   Name=tollipb; Synonyms=tollip2;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=18502148; DOI=10.1016/j.fsi.2008.04.002;
RA   Rebl A., Hoyheim B., Fischer U., Kollner B., Siegl E., Seyfert H.M.;
RT   "Tollip, a negative regulator of TLR-signalling, is encoded by twin genes
RT   in salmonid fish.";
RL   Fish Shellfish Immunol. 25:153-162(2008).
CC   -!- FUNCTION: Component of the signaling pathway of IL-1 and Toll-like
CC       receptors. Inhibits cell activation by microbial products. Connects the
CC       ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8
CC       family adapter and thus mediating autophagic clearance of ubiquitin
CC       conjugates. The TOLLIP-dependent selective autophagy pathway plays an
CC       important role in clearance of cytotoxic polyQ proteins aggregates (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ATG8 family proteins (via AIM motifs), and
CC       ubiquitin (via CUE domain). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18502148}.
CC   -!- DOMAIN: Both ATG8-interaction motifs (AIM1 and AIM2) are required for
CC       the association with ATG8 family proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tollip family. {ECO:0000305}.
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DR   EMBL; AJ878917; CAI48086.1; -; mRNA.
DR   AlphaFoldDB; Q4LBC7; -.
DR   SMR; Q4LBC7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR   CDD; cd04016; C2_Tollip; 1.
DR   CDD; cd14363; CUE_TOLIP; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR003892; CUE.
DR   InterPro; IPR041799; TOLIP_CUE.
DR   InterPro; IPR037301; Tollip_C2.
DR   InterPro; IPR009060; UBA-like_sf.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF02845; CUE; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00546; CUE; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51140; CUE; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Cytoplasm; Immunity; Inflammatory response; Innate immunity;
KW   Repeat.
FT   CHAIN           1..275
FT                   /note="Toll-interacting protein B"
FT                   /id="PRO_0000384937"
FT   DOMAIN          35..152
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          230..273
FT                   /note="CUE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT   MOTIF           133..136
FT                   /note="AIM1"
FT   MOTIF           151..154
FT                   /note="AIM2"
SQ   SEQUENCE   275 AA;  30592 MW;  4FDED8443C4FBCCD CRC64;
     MSTTISTQRG QVYIGELPQD FLRITPPQQQ QQVQLDAQAA QQLQYGESLG TVRRLSITVV
     QAKLAKNYGM TRMDPYCRVR LGYAVYETPT AHNGAKNPRW NKVIQCTVPP GVDSFYLEIF
     DERAFSMDDR IAWTHVTIPE GLREGSVVDE WYSLSGRQGD DKEGMINLVM SYANMTAGMH
     MSPPVVLMPT VYQQGVGYIP IAGVPTVYNQ GMVPMGMPAA PTVAPQEAPC SEEDLKALQD
     MFPNLDREVI RTVIEAQQGN KDAAINTLLQ MTEEL