ID TID_DROME Reviewed; 520 AA.
AC Q27237; O02528; O02529; O02549; Q24554; Q27259; Q7KVH8; Q8T9A7; Q9W1K7;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 24-JAN-2024, entry version 169.
DE RecName: Full=Protein tumorous imaginal discs, mitochondrial;
DE AltName: Full=Protein lethal(2)tumorous imaginal discs;
DE AltName: Full=TID50;
DE AltName: Full=TID56;
DE Flags: Precursor;
GN ORFNames=CG5504 {ECO:0000312|FlyBase:FBgn0002174};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Apxo, bIf, Harvich, and Oregon-R;
RX PubMed=9373138; DOI=10.1016/s0378-1119(97)00373-9;
RA Kurzik-Dumke U., Kaymer M., Gundacker D., Debes A., Labitzke K.;
RT "Gene within gene configuration and expression of the Drosophila
RT melanogaster genes lethal(2) neighbour of tid [l(2)not] and lethal(2)
RT relative of tid.";
RL Gene 200:45-58(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=7758246; DOI=10.1002/dvg.1020160110;
RA Kurzik-Dumke U., Gundacker D., Rentrop M., Gateff E.;
RT "Tumor suppression in Drosophila is causally related to the function of the
RT lethal(2) tumorous imaginal discs gene, a dnaJ homolog.";
RL Dev. Genet. 16:64-76(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM A).
RC STRAIN=Oregon-2;
RA Gundacker S., Neubhuer M., Kurzik-Dumke U.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP CHARACTERIZATION.
RX PubMed=9585178; DOI=10.1379/1466-1268(1998)003<0012:mlateo>2.3.co;2;
RA Kurzik-Dumke U., Debes A., Kaymer M., Dienes P.;
RT "Mitochondrial localization and temporal expression of the Drosophila
RT melanogaster DnaJ homologous tumor suppressor Tid50.";
RL Cell Stress Chaperones 3:12-27(1998).
CC -!- FUNCTION: May act as a tumor suppressor in larval imaginal disks.
CC {ECO:0000269|PubMed:7758246}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q27237-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q27237-2; Sequence=VSP_008308, VSP_008309;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed throughout embryonic
CC development. In larvae, expression is seen in sensory organs, gopplet
CC cells, gonads, imaginal disks, proventriculus, fat body, hematopoietic
CC organ, midgut, Malpighian tubules and ring gland.
CC {ECO:0000269|PubMed:7758246, ECO:0000269|PubMed:9373138}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, highest
CC expression in first and second instar larvae and adults.
CC {ECO:0000269|PubMed:7758246, ECO:0000269|PubMed:9373138}.
CC -!- MISCELLANEOUS: In strains Harvich and Apxo, there are 2 identical genes
CC which code for l(2)tid protein.
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DR EMBL; X95241; CAA64528.1; -; Genomic_DNA.
DR EMBL; X95242; CAA64531.1; -; Genomic_DNA.
DR EMBL; X95247; CAA64536.1; -; Genomic_DNA.
DR EMBL; X95249; CAA64538.1; -; Genomic_DNA.
DR EMBL; X95251; CAA64540.1; -; Genomic_DNA.
DR EMBL; Y10074; CAA71163.1; -; Genomic_DNA.
DR EMBL; Y10074; CAA71164.1; -; Genomic_DNA.
DR EMBL; X77822; CAA54837.1; -; Genomic_DNA.
DR EMBL; X98094; CAA66720.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF47051.3; -; Genomic_DNA.
DR EMBL; AE013599; AAS64764.1; -; Genomic_DNA.
DR EMBL; AY069853; AAL39998.1; -; mRNA.
DR PIR; S42091; S42091.
DR RefSeq; NP_524932.2; NM_080193.5. [Q27237-2]
DR RefSeq; NP_995932.1; NM_206210.3.
DR AlphaFoldDB; Q27237; -.
DR SMR; Q27237; -.
DR BioGRID; 71741; 9.
DR IntAct; Q27237; 2.
DR STRING; 7227.FBpp0088955; -.
DR PaxDb; 7227-FBpp0088955; -.
DR EnsemblMetazoa; FBtr0089503; FBpp0088498; FBgn0002174. [Q27237-2]
DR GeneID; 48844; -.
DR KEGG; dme:Dmel_CG5504; -.
DR AGR; FB:FBgn0002174; -.
DR FlyBase; FBgn0002174; CG5504.
DR VEuPathDB; VectorBase:FBgn0002174; -.
DR eggNOG; KOG0715; Eukaryota.
DR GeneTree; ENSGT00940000155280; -.
DR InParanoid; Q27237; -.
DR OrthoDB; 276132at2759; -.
DR PhylomeDB; Q27237; -.
DR SignaLink; Q27237; -.
DR BioGRID-ORCS; 48844; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 48844; -.
DR PRO; PR:Q27237; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0002174; Expressed in testis and 31 other cell types or tissues.
DR ExpressionAtlas; Q27237; baseline and differential.
DR Genevisible; Q27237; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
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; IPI:FlyBase.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:FlyBase.
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; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
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 PANTHER; PTHR44145; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1.
DR PANTHER; PTHR44145:SF3; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1.
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; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Developmental protein; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Repeat; Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..520
FT /note="Protein tumorous imaginal discs, mitochondrial"
FT /id="PRO_0000007258"
FT DOMAIN 65..130
FT /note="J"
FT REPEAT 227..234
FT /note="CXXCXGXG motif; approximate"
FT REPEAT 244..251
FT /note="CXXCXGXG motif"
FT REPEAT 266..273
FT /note="CXXCXGXG motif; approximate"
FT REPEAT 280..287
FT /note="CXXCXGXG motif"
FT ZN_FING 214..292
FT /note="CR-type"
FT REGION 430..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT VAR_SEQ 446..447
FT /note="AG -> SE (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_008308"
FT VAR_SEQ 448..520
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_008309"
FT VARIANT 28
FT /note="T -> A (in strain: Apxo)"
FT VARIANT 47..48
FT /note="Missing (in strain: Oregon-2 and Oregon-R)"
FT VARIANT 222
FT /note="N -> I (in strain: Apxo)"
FT VARIANT 286..287
FT /note="Missing (in strain: Apxo)"
FT VARIANT 286
FT /note="K -> R (in strain: Oregon-2 and Oregon-R)"
FT VARIANT 415
FT /note="A -> D (in strain: Apxo)"
FT VARIANT 478
FT /note="E -> K (in strain: bIf and Berkeley)"
FT VARIANT 489
FT /note="K -> E (in strain: bIf and Berkeley)"
FT CONFLICT 286
FT /note="K -> M (in Ref. 1, 2, 3; CAA64528 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="A -> V (in Ref. 1, 2, 3; CAA64528 and 6)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 56137 MW; 1904B878F386FB1A CRC64;
MMISCKKLFV FRQLPAVRRC LAAAAFSTPR ATSYRILSSA GSGSTRADAP QVRRLHTTRD
LLAKDYYATL GVAKNANGKD IKKAYYQLAK KYHPDTNKED PDAGRKFQEV SEAYEVLSDE
QKRREYDTYG QTAENIGRQG GGFPGGGAGG FGPEGFSQSW QFRSSIDPEE LFRKIFGEGN
FRTNSFDDFA DSKFGFGQAQ EMVMDLTFAQ AARGVNKDVN VNVVDQCPKC AGTKCEPGTK
PGRCQYCNGT GFETVSTGPF VMRSTCRYCQ GTRQHIKYPC SECEGKGRTV QRRKVTVPVP
AGIENGQTVR MQVGSKELFV TFRVERSDYF RREGADVHTD AAISLAQAVL GGTVRVQGVY
EDQWINVEPG TSSHHKIMLR GKGLKRVNAH GHGDHYVHVK ITVPSAKKLD KKRLALIEAY
AELEEDTPGQ IHGIANRKDG SKQATAGASE EPGAGAAAKA SAAAAGSGAS KPGPGAEESE
GKDQWTDNKK TKAKEGGGSG SGQGDGGGGG FISKIKSMFN
//
