RDX_DROME
ID RDX_DROME Reviewed; 829 AA.
AC Q9VFP2; A4V2V6; Q15BT8; Q5BIA3; Q7KSK6; Q8ING4; Q8MRB4; Q9VFP3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein roadkill;
DE AltName: Full=Hh-induced MATH and BTB domain-containing protein;
GN Name=rdx; Synonyms=HIB; ORFNames=CG12537;
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 [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, INDUCTION, AND
RP FUNCTION.
RX PubMed=16651542; DOI=10.1242/dev.02370;
RA Kent D., Bush E.W., Hooper J.E.;
RT "Roadkill attenuates Hedgehog responses through degradation of Cubitus
RT interruptus.";
RL Development 133:2001-2010(2006).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
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 [5]
RP INTERACTION WITH CI AND GFT, TISSUE SPECIFICITY, INDUCTION, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16740475; DOI=10.1016/j.devcel.2006.05.004;
RA Zhang Q., Zhang L., Wang B., Ou C.-Y., Chien C.-T., Jiang J.;
RT "A hedgehog-induced BTB protein modulates hedgehog signaling by degrading
RT Ci/Gli transcription factor.";
RL Dev. Cell 10:719-729(2006).
CC -!- FUNCTION: Involved in segment polarity. In complex with gft/CUL3,
CC promotes ubiquitination of ci and its subsequent degradation by the
CC proteasome, which results in hh signaling attenuation. This regulation
CC may be important during eye formation for proper packing of ommatidia
CC into a hexagonal array. {ECO:0000269|PubMed:16651542,
CC ECO:0000269|PubMed:16740475}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with ci and gft/CUL3. {ECO:0000269|PubMed:16740475}.
CC -!- INTERACTION:
CC Q9VFP2; Q9VCI7: RanBP3; NbExp=3; IntAct=EBI-132658, EBI-191917;
CC Q9VFP2-2; P19538: ci; NbExp=8; IntAct=EBI-15659276, EBI-94976;
CC Q9VFP2-2; Q9V475: Cul3; NbExp=2; IntAct=EBI-15659276, EBI-109873;
CC Q9VFP2-2; Q9VHV8: puc; NbExp=2; IntAct=EBI-15659276, EBI-193532;
CC Q9VFP2-2; Q9VFP2-2: rdx; NbExp=3; IntAct=EBI-15659276, EBI-15659276;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16740475}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000305}; Synonyms=E {ECO:0000312|FlyBase:FBgn0264493};
CC IsoId=Q9VFP2-1; Sequence=Displayed;
CC Name=2 {ECO:0000305}; Synonyms=B {ECO:0000312|FlyBase:FBgn0264493};
CC IsoId=Q9VFP2-2; Sequence=VSP_022825;
CC Name=3 {ECO:0000305}; Synonyms=C {ECO:0000312|FlyBase:FBgn0264493};
CC IsoId=Q9VFP2-3; Sequence=VSP_022826, VSP_022829;
CC Name=4 {ECO:0000305}; Synonyms=A {ECO:0000312|FlyBase:FBgn0264493}, F
CC {ECO:0000312|FlyBase:FBgn0264493};
CC IsoId=Q9VFP2-4; Sequence=VSP_022827, VSP_022828;
CC -!- TISSUE SPECIFICITY: Expressed near the anterio-posterior compartment
CC boundary of antenna, leg and wing disks. {ECO:0000269|PubMed:16740475}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally in stage 1 embryos. Isoform 1
CC and isoform 4 are expressed zygotically in stage 4 in pole cells. By
CC stage 8, expressed in 14 segmentally repeating stripes. During stage 9
CC and 10, expression appears in neuroblasts. After stage 14, expression
CC is restricted to clypeolabrum, anal plate and salivary glands.
CC {ECO:0000269|PubMed:16651542}.
CC -!- INDUCTION: By hh during segmentation. {ECO:0000269|PubMed:16651542,
CC ECO:0000269|PubMed:16740475}.
CC -!- DOMAIN: The MATH domain interacts with ci.
CC -!- DOMAIN: The BTB (POZ) domain interacts with gft/CUL3.
CC -!- SIMILARITY: Belongs to the Tdpoz family. {ECO:0000305}.
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DR EMBL; DQ507278; ABG24573.1; -; mRNA.
DR EMBL; AE014297; AAF55007.3; -; Genomic_DNA.
DR EMBL; AE014297; AAF55008.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN14346.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14347.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN14348.1; -; Genomic_DNA.
DR EMBL; AY121682; AAM52009.1; -; mRNA.
DR EMBL; BT012443; AAS93714.1; -; mRNA.
DR EMBL; BT021321; AAX33469.1; -; mRNA.
DR RefSeq; NP_650325.1; NM_142068.2. [Q9VFP2-3]
DR RefSeq; NP_650326.3; NM_142069.4. [Q9VFP2-1]
DR RefSeq; NP_731875.2; NM_169564.2. [Q9VFP2-4]
DR RefSeq; NP_731876.2; NM_169565.2. [Q9VFP2-4]
DR RefSeq; NP_731877.1; NM_169566.2. [Q9VFP2-2]
DR AlphaFoldDB; Q9VFP2; -.
DR SMR; Q9VFP2; -.
DR BioGRID; 66781; 48.
DR DIP; DIP-29550N; -.
DR IntAct; Q9VFP2; 11.
DR STRING; 7227.FBpp0099767; -.
DR PaxDb; Q9VFP2; -.
DR DNASU; 41704; -.
DR EnsemblMetazoa; FBtr0100361; FBpp0099767; FBgn0264493. [Q9VFP2-1]
DR EnsemblMetazoa; FBtr0301632; FBpp0290846; FBgn0264493. [Q9VFP2-4]
DR EnsemblMetazoa; FBtr0301633; FBpp0290847; FBgn0264493. [Q9VFP2-2]
DR EnsemblMetazoa; FBtr0301634; FBpp0290848; FBgn0264493. [Q9VFP2-3]
DR EnsemblMetazoa; FBtr0334298; FBpp0306413; FBgn0264493. [Q9VFP2-4]
DR GeneID; 41704; -.
DR KEGG; dme:Dmel_CG12537; -.
DR CTD; 5962; -.
DR FlyBase; FBgn0264493; rdx.
DR VEuPathDB; VectorBase:FBgn0264493; -.
DR eggNOG; KOG1987; Eukaryota.
DR HOGENOM; CLU_320366_0_0_1; -.
DR InParanoid; Q9VFP2; -.
DR PhylomeDB; Q9VFP2; -.
DR Reactome; R-DME-216167; Nuclear CI is degraded.
DR Reactome; R-DME-5632684; Hedgehog 'on' state.
DR SignaLink; Q9VFP2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 41704; 0 hits in 3 CRISPR screens.
DR ChiTaRS; rdx; fly.
DR GenomeRNAi; 41704; -.
DR PRO; PR:Q9VFP2; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0264493; Expressed in cleaving embryo and 63 other tissues.
DR ExpressionAtlas; Q9VFP2; baseline and differential.
DR Genevisible; Q9VFP2; DM.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:FlyBase.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:FlyBase.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:FlyBase.
DR GO; GO:0031648; P:protein destabilization; IMP:FlyBase.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:FlyBase.
DR GO; GO:1901044; P:protein polyubiquitination involved in nucleus-associated proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR GO; GO:0030162; P:regulation of proteolysis; IMP:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IMP:UniProtKB.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR008974; TRAF-like.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00917; MATH; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50144; MATH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Nucleus; Reference proteome;
KW Segmentation polarity protein; Ubl conjugation pathway.
FT CHAIN 1..829
FT /note="Protein roadkill"
FT /id="PRO_0000274593"
FT DOMAIN 486..616
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 655..722
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 24..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..455
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_022825"
FT VAR_SEQ 1..426
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_022826"
FT VAR_SEQ 1..423
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_022827"
FT VAR_SEQ 424..430
FT /note="AANFCDK -> MDLIQEP (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_022828"
FT VAR_SEQ 427..430
FT /note="FCDK -> MALA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_022829"
FT CONFLICT 536
FT /note="K -> T (in Ref. 1; ABG24573)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="G -> D (in Ref. 1; ABG24573)"
FT /evidence="ECO:0000305"
FT CONFLICT 749..750
FT /note="CV -> WL (in Ref. 1; ABG24573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 829 AA; 89667 MW; 608D32B45859280E CRC64;
MFEPYVKIKK KRSVNEIYEN ENLEQQQHHL QQQQQQPATS DNCCCENGEP QNAPEVATAT
VAATSVAATS AAATVATGAA ASSSSSGNCS RLQQLISTPP VLLRRSSLQQ QQHQQQQHHP
HTPAATATPP QQQQQQQAAP SVLQQHLGHL NYESGATAAA AATAAAAAAT VATSRSGSAT
LAQHLATPSN ILQAAFGSSN LQHILTRSAP SPSSSAISSN NCSSACAGNT HYNGGNSNSG
SSSSNSNHHS NSIIASRLFG AASSSSSSSS SSASASSSSV AASSSSSSHH LHSHHSALTN
SITNRINQSI RRHLNQQQHH HPLSASSSSA SASPSASTSS SSSYQQSSVQ QQHYNCAHPA
QQQQHHHHHH SSSSSSSSSS SSSHHHHNSS SSSNSNNQQQ PQQSPLCLVL LVKCPNSKEF
CNAAANFCDK RLPVNECQAS QTARVTSNLH ASSSTMAVSR VPSPPLPEVN TPVAENWCYT
QVKVVKFSYM WTINNFSFCR EEMGEVLKSS TFSAGANDKL KWCLRVNPKG LDEESKDYLS
LYLLLVSCNK SEVRAKFKFS ILNAKREETK AMESQRAYRF VQGKDWGFKK FIRRDFLLDE
ANGLLPEDKL TIFCEVSVVA DSVNISGQSN IVQFKVPECK LSEDLGNLFD NEKFSDVTLS
VGGREFQAHK AILAARSDVF AAMFEHEMEE RKLNRVAITD VDHEVLKEML RFIYTGKAPN
LEKMADDLLA AADKYALEKL KVMCEEALCV NLSVETAAET LILADLHSAD QLKAQTIDFI
NTHATDVMET SGWQNMITTH SHLIAEAFRA LATQQIPPIG PPRKRVKMS
