TID_DROVI
ID TID_DROVI Reviewed; 529 AA.
AC Q24331;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein tumorous imaginal discs, mitochondrial;
DE AltName: Full=Protein lethal(2)tumorous imaginal discs;
DE AltName: Full=TID58;
DE Flags: Precursor;
GN Name=l(2)tid; Synonyms=tid;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RX PubMed=9434170; DOI=10.1016/s0378-1119(97)00528-3;
RA Kaymer M., Debes A., Kress H., Kurzik-Dumke U.;
RT "Sequence, molecular organization and products of the Drosophila virilis
RT homologs of the D. melanogaster nested genes lethal(2) tumorous imaginal
RT discs [l(2)tid] and lethal(2) neighbour of tid [l(2)not].";
RL Gene 204:91-103(1997).
CC -!- FUNCTION: May act as a tumor suppressor in larval imaginal disks.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, highest
CC expression is seen during larval development.
CC {ECO:0000269|PubMed:9434170}.
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DR EMBL; Y07700; CAA68962.1; -; Genomic_DNA.
DR AlphaFoldDB; Q24331; -.
DR SMR; Q24331; -.
DR STRING; 7244.FBpp0232421; -.
DR eggNOG; KOG0715; Eukaryota.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005113; F:patched binding; IEA:EnsemblMetazoa.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 1.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Developmental protein; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Repeat; Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..529
FT /note="Protein tumorous imaginal discs, mitochondrial"
FT /id="PRO_0000007259"
FT DOMAIN 80..145
FT /note="J"
FT REPEAT 243..250
FT /note="CXXCXGXG motif; approximate"
FT REPEAT 260..267
FT /note="CXXCXGXG motif"
FT REPEAT 282..289
FT /note="CXXCXGXG motif; approximate"
FT REPEAT 296..303
FT /note="CXXCXGXG motif"
FT ZN_FING 230..308
FT /note="CR-type"
FT REGION 441..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 529 AA; 58120 MW; 2A0631FF26F791CF CRC64;
MISCKNLCVL RQLPLKNCRR HYSAIQSSAA LLSVRPTKWT PKPAAAGGAV SAWQQRTTAK
QHQQQQRRSL FSSSRMQAKD YYATLGVAKN ANAKDIKKAY YELAKKYHPD TNKDDPDASK
KFQDVSEAYE VLSDDQKRRE YDTYGQTTEN MNRQGAGGAG GFGGGPFGPD GFSQNWQFRS
TIDPEELFRK IFGEGNFRSN SFDDFADSKF GFGQAQELVM DLTFAQAARG VNKDVNVNVV
DQCPKCAGSK CEPGTKPGRC QYCNGTGFET ISTGPFVMRS TCRYCQGTRQ YIKYPCAECE
GKGQTVQRRK VTVPVPAGIE NGQTVRMQVG SKELFVTFRV ERSDYFRRDG ADVHTDAPIS
LAQAVLGGTV RVQGVYEDQW LNIEPGTSSH RKIALRGKGL KRVNAHGHGD HYVHIKIEVP
KKLSQEQRAL LEAYAELEED TPGQIHGMAQ RKDGSKKATA GASETKTDAQ PAGRTADSGS
QGTSRAGAET ESAKGQQSEK SETRRKDQQT GGESGSGGGF LNKIKSMFN
