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Protein

Protein roadkill

Gene

rdx

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in segment polarity. In complex with gft/CUL3, promotes ubiquitination of ci and its subsequent degradation by the proteasome, which results in hh signaling attenuation. This regulation may be important during eye formation for proper packing of ommatidia into a hexagonal array.2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • protein homodimerization activity Source: FlyBase

GO - Biological processi

  • cellularization Source: FlyBase
  • establishment of ommatidial planar polarity Source: FlyBase
  • eye development Source: UniProtKB
  • eye morphogenesis Source: FlyBase
  • lateral inhibition Source: FlyBase
  • negative regulation of protein import into nucleus Source: FlyBase
  • negative regulation of smoothened signaling pathway Source: FlyBase
  • positive regulation of apoptotic process Source: FlyBase
  • positive regulation of JNK cascade Source: FlyBase
  • protein destabilization Source: FlyBase
  • protein ubiquitination Source: UniProtKB
  • regulation of proteolysis Source: FlyBase
  • segment polarity determination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Segmentation polarity protein

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-DME-5632684. Hedgehog 'on' state.
SignaLinkiQ9VFP2.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein roadkill
Alternative name(s):
Hh-induced MATH and BTB domain-containing protein
Gene namesi
Name:rdx
Synonyms:HIB
ORF Names:CG12537
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0264493. rdx.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 829829Protein roadkillPRO_0000274593Add
BLAST

Proteomic databases

PaxDbiQ9VFP2.

Expressioni

Tissue specificityi

Expressed near the anterio-posterior compartment boundary of antenna, leg and wing disks.1 Publication

Developmental stagei

Expressed maternally in stage 1 embryos. Isoform 1 and isoform 4 are expressed zygotically in stage 4 in pole cells. By stage 8, expressed in 14 segmentally repeating stripes. During stage 9 and 10, expression appears in neuroblasts. After stage 14, expression is restricted to clypeolabrum, anal plate and salivary glands.1 Publication

Inductioni

By hh during segmentation.2 Publications

Gene expression databases

BgeeiQ9VFP2.
ExpressionAtlasiQ9VFP2. differential.
GenevisibleiQ9VFP2. DM.

Interactioni

Subunit structurei

Interacts with ci and gft/CUL3.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi66781. 43 interactions.
DIPiDIP-29550N.
IntActiQ9VFP2. 6 interactions.
MINTiMINT-288765.
STRINGi7227.FBpp0099767.

Structurei

3D structure databases

ProteinModelPortaliQ9VFP2.
SMRiQ9VFP2. Positions 483-811.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini486 – 616131MATHPROSITE-ProRule annotationAdd
BLAST
Domaini655 – 72268BTBPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi31 – 366Poly-Gln
Compositional biasi82 – 865Poly-Ser
Compositional biasi109 – 14537Gln-richAdd
BLAST
Compositional biasi156 – 19540Ala-richAdd
BLAST
Compositional biasi208 – 395188Ser-richAdd
BLAST
Compositional biasi289 – 38799His-richAdd
BLAST

Domaini

The MATH domain interacts with ci.
The BTB (POZ) domain interacts with gft/CUL3.

Sequence similaritiesi

Belongs to the Tdpoz family.Curated
Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 1 MATH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1987. Eukaryota.
ENOG410XQV8. LUCA.
GeneTreeiENSGT00390000000361.
InParanoidiQ9VFP2.
KOiK10523.
OMAiCDKRLPV.
OrthoDBiEOG73NG3G.
PhylomeDBiQ9VFP2.

Family and domain databases

Gene3Di2.60.210.10. 1 hit.
InterProiIPR000210. BTB/POZ_dom.
IPR002083. MATH/TRAF_dom.
IPR011333. SKP1/BTB/POZ.
IPR008974. TRAF-like.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
PF00917. MATH. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00061. MATH. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
SSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS50144. MATH. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1Curated (identifier: Q9VFP2-1) [UniParc]FASTAAdd to basket

Also known as: EImported

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFEPYVKIKK KRSVNEIYEN ENLEQQQHHL QQQQQQPATS DNCCCENGEP
60 70 80 90 100
QNAPEVATAT VAATSVAATS AAATVATGAA ASSSSSGNCS RLQQLISTPP
110 120 130 140 150
VLLRRSSLQQ QQHQQQQHHP HTPAATATPP QQQQQQQAAP SVLQQHLGHL
160 170 180 190 200
NYESGATAAA AATAAAAAAT VATSRSGSAT LAQHLATPSN ILQAAFGSSN
210 220 230 240 250
LQHILTRSAP SPSSSAISSN NCSSACAGNT HYNGGNSNSG SSSSNSNHHS
260 270 280 290 300
NSIIASRLFG AASSSSSSSS SSASASSSSV AASSSSSSHH LHSHHSALTN
310 320 330 340 350
SITNRINQSI RRHLNQQQHH HPLSASSSSA SASPSASTSS SSSYQQSSVQ
360 370 380 390 400
QQHYNCAHPA QQQQHHHHHH SSSSSSSSSS SSSHHHHNSS SSSNSNNQQQ
410 420 430 440 450
PQQSPLCLVL LVKCPNSKEF CNAAANFCDK RLPVNECQAS QTARVTSNLH
460 470 480 490 500
ASSSTMAVSR VPSPPLPEVN TPVAENWCYT QVKVVKFSYM WTINNFSFCR
510 520 530 540 550
EEMGEVLKSS TFSAGANDKL KWCLRVNPKG LDEESKDYLS LYLLLVSCNK
560 570 580 590 600
SEVRAKFKFS ILNAKREETK AMESQRAYRF VQGKDWGFKK FIRRDFLLDE
610 620 630 640 650
ANGLLPEDKL TIFCEVSVVA DSVNISGQSN IVQFKVPECK LSEDLGNLFD
660 670 680 690 700
NEKFSDVTLS VGGREFQAHK AILAARSDVF AAMFEHEMEE RKLNRVAITD
710 720 730 740 750
VDHEVLKEML RFIYTGKAPN LEKMADDLLA AADKYALEKL KVMCEEALCV
760 770 780 790 800
NLSVETAAET LILADLHSAD QLKAQTIDFI NTHATDVMET SGWQNMITTH
810 820
SHLIAEAFRA LATQQIPPIG PPRKRVKMS
Length:829
Mass (Da):89,667
Last modified:February 7, 2006 - v2
Checksum:i608D32B45859280E
GO
Isoform 2Curated (identifier: Q9VFP2-2) [UniParc]FASTAAdd to basket

Also known as: BImported

The sequence of this isoform differs from the canonical sequence as follows:
     1-455: Missing.

Show »
Length:374
Mass (Da):42,284
Checksum:i2116548EE64F04C0
GO
Isoform 3Curated (identifier: Q9VFP2-3) [UniParc]FASTAAdd to basket

Also known as: CImported

The sequence of this isoform differs from the canonical sequence as follows:
     1-426: Missing.
     427-430: FCDK → MALA

Show »
Length:403
Mass (Da):45,310
Checksum:i190BB5EC3B108CD8
GO
Isoform 4Curated (identifier: Q9VFP2-4) [UniParc]FASTAAdd to basket

Also known as: AImported

, FImported

The sequence of this isoform differs from the canonical sequence as follows:
     1-423: Missing.
     424-430: AANFCDK → MDLIQEP

Show »
Length:406
Mass (Da):45,750
Checksum:i344A5EA7A271D404
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti536 – 5361K → T in ABG24573 (PubMed:16651542).Curated
Sequence conflicti716 – 7161G → D in ABG24573 (PubMed:16651542).Curated
Sequence conflicti749 – 7502CV → WL in ABG24573 (PubMed:16651542).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 455455Missing in isoform 2. 1 PublicationVSP_022825Add
BLAST
Alternative sequencei1 – 426426Missing in isoform 3. 1 PublicationVSP_022826Add
BLAST
Alternative sequencei1 – 423423Missing in isoform 4. CuratedVSP_022827Add
BLAST
Alternative sequencei424 – 4307AANFCDK → MDLIQEP in isoform 4. CuratedVSP_022828
Alternative sequencei427 – 4304FCDK → MALA in isoform 3. 1 PublicationVSP_022829

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ507278 mRNA. Translation: ABG24573.1.
AE014297 Genomic DNA. Translation: AAF55007.3.
AE014297 Genomic DNA. Translation: AAF55008.2.
AE014297 Genomic DNA. Translation: AAN14346.1.
AE014297 Genomic DNA. Translation: AAN14347.2.
AE014297 Genomic DNA. Translation: AAN14348.1.
AY121682 mRNA. Translation: AAM52009.1.
BT012443 mRNA. Translation: AAS93714.1.
BT021321 mRNA. Translation: AAX33469.1.
RefSeqiNP_650325.1. NM_142068.2. [Q9VFP2-3]
NP_650326.3. NM_142069.4. [Q9VFP2-1]
NP_731875.2. NM_169564.2. [Q9VFP2-4]
NP_731876.2. NM_169565.2. [Q9VFP2-4]
NP_731877.1. NM_169566.2. [Q9VFP2-2]
UniGeneiDm.10784.

Genome annotation databases

EnsemblMetazoaiFBtr0100361; FBpp0099767; FBgn0264493. [Q9VFP2-1]
GeneIDi41704.
KEGGidme:Dmel_CG12537.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ507278 mRNA. Translation: ABG24573.1.
AE014297 Genomic DNA. Translation: AAF55007.3.
AE014297 Genomic DNA. Translation: AAF55008.2.
AE014297 Genomic DNA. Translation: AAN14346.1.
AE014297 Genomic DNA. Translation: AAN14347.2.
AE014297 Genomic DNA. Translation: AAN14348.1.
AY121682 mRNA. Translation: AAM52009.1.
BT012443 mRNA. Translation: AAS93714.1.
BT021321 mRNA. Translation: AAX33469.1.
RefSeqiNP_650325.1. NM_142068.2. [Q9VFP2-3]
NP_650326.3. NM_142069.4. [Q9VFP2-1]
NP_731875.2. NM_169564.2. [Q9VFP2-4]
NP_731876.2. NM_169565.2. [Q9VFP2-4]
NP_731877.1. NM_169566.2. [Q9VFP2-2]
UniGeneiDm.10784.

3D structure databases

ProteinModelPortaliQ9VFP2.
SMRiQ9VFP2. Positions 483-811.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66781. 43 interactions.
DIPiDIP-29550N.
IntActiQ9VFP2. 6 interactions.
MINTiMINT-288765.
STRINGi7227.FBpp0099767.

Proteomic databases

PaxDbiQ9VFP2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0100361; FBpp0099767; FBgn0264493. [Q9VFP2-1]
GeneIDi41704.
KEGGidme:Dmel_CG12537.

Organism-specific databases

CTDi5962.
FlyBaseiFBgn0264493. rdx.

Phylogenomic databases

eggNOGiKOG1987. Eukaryota.
ENOG410XQV8. LUCA.
GeneTreeiENSGT00390000000361.
InParanoidiQ9VFP2.
KOiK10523.
OMAiCDKRLPV.
OrthoDBiEOG73NG3G.
PhylomeDBiQ9VFP2.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-DME-5632684. Hedgehog 'on' state.
SignaLinkiQ9VFP2.

Miscellaneous databases

ChiTaRSirdx. fly.
GenomeRNAii41704.
PROiQ9VFP2.

Gene expression databases

BgeeiQ9VFP2.
ExpressionAtlasiQ9VFP2. differential.
GenevisibleiQ9VFP2. DM.

Family and domain databases

Gene3Di2.60.210.10. 1 hit.
InterProiIPR000210. BTB/POZ_dom.
IPR002083. MATH/TRAF_dom.
IPR011333. SKP1/BTB/POZ.
IPR008974. TRAF-like.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
PF00917. MATH. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00061. MATH. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
SSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS50144. MATH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Roadkill attenuates Hedgehog responses through degradation of Cubitus interruptus."
    Kent D., Bush E.W., Hooper J.E.
    Development 133:2001-2010(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, INDUCTION, FUNCTION.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Strain: Berkeley.
    Tissue: Embryo.
  5. "A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor."
    Zhang Q., Zhang L., Wang B., Ou C.-Y., Chien C.-T., Jiang J.
    Dev. Cell 10:719-729(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CI AND GFT, TISSUE SPECIFICITY, INDUCTION, FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRDX_DROME
AccessioniPrimary (citable) accession number: Q9VFP2
Secondary accession number(s): A4V2V6
, Q15BT8, Q5BIA3, Q7KSK6, Q8ING4, Q8MRB4, Q9VFP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 7, 2006
Last modified: July 6, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.