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Database: UniProt
Entry: C1BZR1
LinkDB: C1BZR1
Original site: C1BZR1 
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   01-OCT-2014, entry version 16.
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;
OC   Esociformes; 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.,
RA   Messmer A.M., Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J.,
RA   Davidson W.S., Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes
RT   in 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.
CC       Connects the ubiquitin pathway to autophagy by functioning as a
CC       ubiquitin-ATG8 family adapter and thus mediating autophagic
CC       clearance of ubiquitin conjugates. The TOLLIP-dependent selective
CC       autophagy pathway plays an important role in clearance of
CC       cytotoxic polyQ proteins aggregates (By similarity).
CC       {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
CC       for the association with ATG8 family proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tollip family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 C2 domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 CUE domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00468}.
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DR   EMBL; BT080090; ACO14514.1; -; mRNA.
DR   ProteinModelPortal; C1BZR1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR003892; CUE.
DR   InterPro; IPR009060; UBA-like.
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; PS51140; CUE; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Cytoplasm; Immunity; Inflammatory response;
KW   Innate immunity; Repeat.
FT   CHAIN         1    275       Toll-interacting protein.
FT                                /FTId=PRO_0000384935.
FT   DOMAIN       40    135       C2.
FT   DOMAIN      230    273       CUE. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00468}.
FT   MOTIF       133    136       AIM1.
FT   MOTIF       151    154       AIM2.
FT   COMPBIAS     28     34       Poly-Gln.
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
//
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