TOPRS_DROME
ID TOPRS_DROME Reviewed; 1038 AA.
AC Q9V8P9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=E3 ubiquitin-protein ligase Topors;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase Topors {ECO:0000305};
DE AltName: Full=SUMO1-protein E3 ligase Topors;
DE AltName: Full=Topoisomerase I-binding RING finger protein;
DE AltName: Full=Topoisomerase I-binding arginine/serine-rich protein;
DE AltName: Full=dTopors;
GN Name=Topors; ORFNames=CG15104;
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 [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 [2]
RP GENOME REANNOTATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION, INTERACTION WITH H; P53 AND TOP1, AND MUTAGENESIS OF CYS-102.
RX PubMed=14871887; DOI=10.1074/jbc.m310097200;
RA Secombe J., Parkhurst S.M.;
RT "Drosophila Topors is a RING finger-containing protein that functions as a
RT ubiquitin-protein isopeptide ligase for the hairy basic helix-loop-helix
RT repressor protein.";
RL J. Biol. Chem. 279:17126-17133(2004).
RN [5]
RP FUNCTION, INTERACTION WITH CP190; LAM; MOD(MDG4) AND SU(HW), SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF CYS-118.
RX PubMed=16209949; DOI=10.1016/j.molcel.2005.08.031;
RA Capelson M., Corces V.G.;
RT "The ubiquitin ligase dTopors directs the nuclear organization of a
RT chromatin insulator.";
RL Mol. Cell 20:105-116(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-820 AND SER-822, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Functions as a ubiquitin-protein E3 ligase. Negatively
CC regulates the transcriptional repressor h/hairy by promoting its
CC ubiquitination and subsequent degradation. Also directs the nuclear
CC organization of the gypsy chromatin insulator. Chromatin insulators are
CC regulatory elements which establish independent domains of
CC transcriptional activity within eukaryotic genomes. Insulators have two
CC defining properties; they can block the communication between an
CC enhancer and a promoter when placed between them, and can also buffer
CC transgenes from position effect variegation (PEV). Insulators are
CC proposed to structure the chromatin fiber into independent domains of
CC differing transcriptional potential by promoting the formation of
CC distinct chromatin loops. This chromatin looping may require the
CC formation of insulator bodies, where homotypic interactions between
CC individual subunits of the insulator complex could promote the
CC clustering of widely spaced insulators at the nuclear periphery. Within
CC the gypsy insulator complex, this protein may promote formation of
CC nuclear insulator bodies by recruiting individual insulator complexes
CC to the nuclear lamina. {ECO:0000269|PubMed:14871887,
CC ECO:0000269|PubMed:16209949}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- SUBUNIT: Interacts with h/hairy, p53 and Top1. Interacts with the gypsy
CC chromatin insulator complex, composed of Cp190, mod(mdg4) and su(Hw);
CC interacts directly with mod(mdg4) and su(Hw). Interacts with Lam/lamin.
CC {ECO:0000269|PubMed:14871887, ECO:0000269|PubMed:16209949}.
CC -!- INTERACTION:
CC Q9V8P9; P14003: h; NbExp=4; IntAct=EBI-147805, EBI-123011;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16209949}. Chromosome
CC {ECO:0000269|PubMed:16209949}. Note=Colocalizes with the gypsy
CC chromatin insulator complex on polytene chromosomes and to nuclear
CC insulator bodies. Also localizes to the nuclear lamina.
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DR EMBL; AE013599; AAF57614.1; -; Genomic_DNA.
DR EMBL; AY122186; AAM52698.1; -; mRNA.
DR RefSeq; NP_001261083.1; NM_001274154.1.
DR RefSeq; NP_611388.1; NM_137544.3.
DR AlphaFoldDB; Q9V8P9; -.
DR SMR; Q9V8P9; -.
DR BioGRID; 62854; 10.
DR IntAct; Q9V8P9; 3.
DR STRING; 7227.FBpp0304302; -.
DR iPTMnet; Q9V8P9; -.
DR PaxDb; Q9V8P9; -.
DR PRIDE; Q9V8P9; -.
DR EnsemblMetazoa; FBtr0086570; FBpp0085754; FBgn0267351.
DR EnsemblMetazoa; FBtr0331977; FBpp0304302; FBgn0267351.
DR GeneID; 37188; -.
DR KEGG; dme:Dmel_CG15104; -.
DR CTD; 10210; -.
DR FlyBase; FBgn0267351; Topors.
DR VEuPathDB; VectorBase:FBgn0267351; -.
DR eggNOG; KOG4430; Eukaryota.
DR GeneTree; ENSGT00530000064170; -.
DR HOGENOM; CLU_009654_0_0_1; -.
DR InParanoid; Q9V8P9; -.
DR OMA; MINFRRE; -.
DR OrthoDB; 322085at2759; -.
DR PhylomeDB; Q9V8P9; -.
DR SignaLink; Q9V8P9; -.
DR BioGRID-ORCS; 37188; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Topors; fly.
DR GenomeRNAi; 37188; -.
DR PRO; PR:Q9V8P9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0267351; Expressed in egg cell and 23 other tissues.
DR ExpressionAtlas; Q9V8P9; baseline and differential.
DR Genevisible; Q9V8P9; DM.
DR GO; GO:0005652; C:nuclear lamina; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
DR GO; GO:0005521; F:lamin binding; IDA:UniProtKB.
DR GO; GO:0019789; F:SUMO transferase activity; ISS:FlyBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0051299; P:centrosome separation; IMP:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007060; P:male meiosis chromosome segregation; IMP:FlyBase.
DR GO; GO:0010032; P:meiotic chromosome condensation; IMP:FlyBase.
DR GO; GO:0071763; P:nuclear membrane organization; IMP:FlyBase.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IGI:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1038
FT /note="E3 ubiquitin-protein ligase Topors"
FT /id="PRO_0000232628"
FT ZN_FING 102..141
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 53..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..682
FT /note="Interaction with h/hairy"
FT REGION 627..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..711
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1028
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 820
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 102
FT /note="C->A: Abrogates ubiquitin-protein E3 ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:14871887"
FT MUTAGEN 118
FT /note="C->S: Abrogates enhancement of gypsy chromatin
FT insulator activity."
FT /evidence="ECO:0000269|PubMed:16209949"
SQ SEQUENCE 1038 AA; 113313 MW; BEB3E63AA131E9E8 CRC64;
MAEENPGALA ANVPYLGVDE LGASVIVEPG LEGSNAGGRT LPAAAIKFAD LTESGSESGD
NEAEEPVSAG PDNANAIGEP GTSASAAEEN GTVERNSPPP NCAICLSRCR RKCFTDSCMH
QFCFKCLCEW SKIKPECPLC KQPFRTIIHN VRTLDDYDRY PVQTTSPVPT ENPSLRYHIV
RRPRYTPLVQ NQAVIVNDIE AAIAAGAAGE DVLSAAEVAA GRRSYSRFEP YRSELMNYYQ
HDQDASTSGS LSQLWRRYVY DRKLYALPVS DSVTGHFREW SARFYRNNPA QIHRLMPWIH
RDIMCLLRNA AHSVNTVMTL MSDLLPMTSL LGPTFRRRLS PYLGERTSHF IHELFNFARS
PYDINGYDHV VQYSARVAEE VEVDLLDMVE TQSSNGDDLN LEVGDSDADA INAGFSPDWS
PPRVRPSTSV IVTNPGATHS FSVTMASDGS ELPGISIRRT TNVGSQTVAI NLSMRRPAAV
ASEEPEVIEI DDGDAAANAE VAAINDGSNT SRRHAGATLP VTAHIELESS SSSGDEDECV
FVLELKPPHM RTPEQVSLDS NSDSDVVFVN EQHEAAPDAI AENRSTQSPL DLASRDQGLF
MGPSTSGAAA NRGKNWKLVM AQTRRLDQLR TLRSIRSKKS RRSSMPARSD SGSSPSSCSS
SSFHFSSSSD EDSSDSSTTN SEPPKKKSRK RVANNKRSKK ESIGKRTSRK RKAKDQNMEM
LEQQQISQKK PQRQPESSSD SPSSSDDESG GDSSESSGQP NTNNNKSSSD SDDDSAVNMQ
LSALRATLKA EATLEDRKPV KLELQLPDDD QAGPLHSRMT PSPREDNEPG CSAPKRRRSC
SHSNQSSQSA SLASSSTATS SSAPLSSFAW GAAGFSGDPL MRGHPAMEEH DIANSLIELS
TLTQPVNIGL FNEHYNSAEN SMGMLSNTLC DSPQTLAADD ANLENYFDTD ADPEASRERD
AYSLEAAIDV VGESELQIAE DTATATEEQD EEDEEDEDQE EDDQEEEKAA EEEEEEEEDD
DDSDNHDEND ENQGLLPY
