TOLIP_DANRE
ID TOLIP_DANRE Reviewed; 276 AA.
AC Q7ZV43; Q6NYL4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Toll-interacting protein;
GN Name=tollip; ORFNames=zgc:76985;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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; BC046009; AAH46009.1; -; mRNA.
DR EMBL; BC066544; AAH66544.1; -; mRNA.
DR AlphaFoldDB; Q7ZV43; -.
DR SMR; Q7ZV43; -.
DR STRING; 7955.ENSDARP00000112313; -.
DR PaxDb; Q7ZV43; -.
DR ZFIN; ZDB-GENE-030131-8820; tollip.
DR eggNOG; ENOG502QWQA; Eukaryota.
DR InParanoid; Q7ZV43; -.
DR PhylomeDB; Q7ZV43; -.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-9020702; Interleukin-1 signaling.
DR PRO; PR:Q7ZV43; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
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:0030178; P:negative regulation of Wnt signaling pathway; IMP:ZFIN.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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..276
FT /note="Toll-interacting protein"
FT /id="PRO_0000384933"
FT DOMAIN 35..152
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 231..274
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT MOTIF 133..136
FT /note="AIM1"
FT MOTIF 151..154
FT /note="AIM2"
FT CONFLICT 222
FT /note="A -> P (in Ref. 1; AAH66544)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="A -> G (in Ref. 1; AAH66544)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 276 AA; 30424 MW; 1C61E5B737513D1E CRC64;
MATTISTQRG QVYIGELPQD FLRIMPTQQQ QQVQLDAQAA RQLQYGGSLG TAGRLSITVV
QAKLAKNYGM TRMDPYCRIR LGYAVYETPT AHNGAKNPRW NKVIQCTVPP GVDSFYLEIF
DERAFSMDDR IAWTHVTIPE NLREGTVVDE WYSLSGRQGD DKEGMINLVM SFATIPAGMM
MQPQPVVLMP TVYQQGVGYV PIAGVPGMYN QGVVPMGMPA AAPVASQSAP CSEEDLKALQ
DMFPNLDKEV IRTVLEAQQG NKDAAINSLL QMAEEL