TOLIP_ESOLU
ID TOLIP_ESOLU Reviewed; 275 AA.
AC C1BZR1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Toll-interacting protein;
GN Name=tollip;
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
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 -!- 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; BT080090; ACO14514.1; -; mRNA.
DR RefSeq; NP_001290730.1; NM_001303801.1.
DR AlphaFoldDB; C1BZR1; -.
DR SMR; C1BZR1; -.
DR STRING; 8010.XP_010897794.1; -.
DR GeneID; 105027394; -.
DR KEGG; els:105027394; -.
DR CTD; 54472; -.
DR OrthoDB; 1219350at2759; -.
DR Proteomes; UP000265140; LG25.
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 Reference proteome; Repeat.
FT CHAIN 1..275
FT /note="Toll-interacting protein"
FT /id="PRO_0000384935"
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; 30319 MW; C8D22DB4D711DA49 CRC64;
MATTISTQRG QVYIGELPQD FLRITPTQQQ QQVQLDAQAA QQLQYGGSLG TVGRLSITVV
QAKLAKNYGM TRMDPYCRVR LGYAVYETPT AHNGAKNPRW NKVIQCTVPP GVGSFYLEIF
DERAFSMDDR IAWTHVTIPE GLREGSVVDE WYSLSDRQGD DKEGMINLVM SFANMPAGMH
MSPPVVLMPT VYQQGVGYIP IAGVPTAYSP GMVPMGMPAA PTVTPQEAPC SEEDLKALQD
MFPNLDREVI RTVIEAQQGN KDAAINSLLQ MTEEL