RN_DROME
ID RN_DROME Reviewed; 946 AA.
AC Q9VI93; Q4V6Z5; Q8WRV3; Q9VI90;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Zinc finger protein rotund;
DE AltName: Full=Zinc finger protein roughened eye;
GN Name=rn {ECO:0000312|FlyBase:FBgn0267337}; Synonyms=roe;
GN ORFNames=CG32466 {ECO:0000312|FlyBase:FBgn0267337};
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] (ISOFORMS RN AND ROE), ALTERNATIVE PROMOTER
RP USAGE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11874922; DOI=10.1242/dev.129.5.1273;
RA St Pierre S.E., Galindo M.I., Couso J.P., Thor S.;
RT "Control of Drosophila imaginal disc development by rotund and roughened
RT eye: differentially expressed transcripts of the same gene encoding
RT functionally distinct zinc finger proteins.";
RL Development 129:1273-1281(2002).
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] (ISOFORM 3).
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12163403; DOI=10.1242/dev.129.17.3995;
RA Rodriguez Dd Ddel A., Terriente J., Galindo M.I., Couso J.P.,
RA Diaz-Benjumea F.J.;
RT "Different mechanisms initiate and maintain wingless expression in the
RT Drosophila wing hinge.";
RL Development 129:3995-4004(2002).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH NAB.
RX PubMed=17428824; DOI=10.1242/dev.003830;
RA Terriente Felix J., Magarinos M., Diaz-Benjumea F.J.;
RT "Nab controls the activity of the zinc-finger transcription factors Squeeze
RT and Rotund in Drosophila development.";
RL Development 134:1845-1852(2007).
RN [7]
RP FUNCTION.
RX PubMed=18571155; DOI=10.1016/j.ydbio.2008.04.028;
RA Terriente J., Perea D., Suzanne M., Diaz-Benjumea F.J.;
RT "The Drosophila gene zfh2 is required to establish proximal-distal domains
RT in the wing disc.";
RL Dev. Biol. 320:102-112(2008).
RN [8]
RP FUNCTION.
RX PubMed=18430928; DOI=10.1534/genetics.108.086983;
RA Zhao M., Szafranski P., Hall C.A., Goode S.;
RT "Basolateral junctions utilize warts signaling to control epithelial-
RT mesenchymal transition and proliferation crucial for migration and invasion
RT of Drosophila ovarian epithelial cells.";
RL Genetics 178:1947-1971(2008).
CC -!- FUNCTION: Transcription factor involved in imaginal disks development.
CC Isoform rn is required in the wings, antenna, haltere, proboscis and
CC legs disks, while isoform roe is required in the eye disk. Together
CC with nab corepressor, it is involved in the initiation and maintenance
CC of wingless (wg) expression in the wing hinge, by limiting the
CC expression of wg to this compartment. Also required for the epithelial-
CC mesenchymal transition branch of basolateral junctions signaling.
CC {ECO:0000269|PubMed:11874922, ECO:0000269|PubMed:12163403,
CC ECO:0000269|PubMed:17428824, ECO:0000269|PubMed:18430928,
CC ECO:0000269|PubMed:18571155}.
CC -!- SUBUNIT: Interacts with nab; which acts as a corepressor.
CC {ECO:0000269|PubMed:17428824}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=rn; Synonyms=E, Rotund;
CC IsoId=Q9VI93-1; Sequence=Displayed;
CC Name=roe; Synonyms=C, Roughened eye;
CC IsoId=Q9VI93-2; Sequence=VSP_037179;
CC Name=3;
CC IsoId=Q9VI93-3; Sequence=VSP_037180;
CC -!- TISSUE SPECIFICITY: Isoform rn and isoform roe are expressed in non-
CC overlapping domains in the larval imaginal disks. Isoform rn is first
CC expressed during the early third larval instar in the leg, wing,
CC haltere and antennal part of the eye-antennal imaginal disk. It is
CC observed as a ring in the leg and antenna disks and in the presumptive
CC wing pouch and capitellum of wing and haltere disks respectively. In
CC wing disk it isexpressed in 3 concentric domains in the wing pouch. In
CC late third instar, expression of isoform rn in the leg disk is no
CC longer evident, but is maintained in the other disks. Isoform roe
CC appears in the third instar and is confined to the eye part of the eye-
CC antennal imaginal disk in a band of 4-6 cells at the morphogenetic
CC furrow. There is no evidence of roe expression in other imaginal disks.
CC {ECO:0000269|PubMed:11874922, ECO:0000269|PubMed:12163403,
CC ECO:0000269|PubMed:17428824}.
CC -!- MISCELLANEOUS: [Isoform roe]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL59599.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF395904; AAL59598.1; -; mRNA.
DR EMBL; AF395905; AAL59599.1; ALT_INIT; mRNA.
DR EMBL; AE014297; AAF54032.3; -; Genomic_DNA.
DR EMBL; AE014297; AAS65102.1; -; Genomic_DNA.
DR EMBL; BT022161; AAY51555.1; -; mRNA.
DR RefSeq; NP_649715.2; NM_141458.3. [Q9VI93-1]
DR RefSeq; NP_996178.1; NM_206456.2. [Q9VI93-2]
DR AlphaFoldDB; Q9VI93; -.
DR SMR; Q9VI93; -.
DR BioGRID; 66073; 12.
DR IntAct; Q9VI93; 8.
DR STRING; 7227.FBpp0289745; -.
DR PaxDb; Q9VI93; -.
DR DNASU; 40879; -.
DR EnsemblMetazoa; FBtr0299637; FBpp0288912; FBgn0267337. [Q9VI93-2]
DR EnsemblMetazoa; FBtr0300518; FBpp0289745; FBgn0267337. [Q9VI93-1]
DR GeneID; 40879; -.
DR KEGG; dme:Dmel_CG42277; -.
DR CTD; 109542; -.
DR FlyBase; FBgn0267337; rn.
DR VEuPathDB; VectorBase:FBgn0267337; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_309561_0_0_1; -.
DR InParanoid; Q9VI93; -.
DR OMA; YAEPERM; -.
DR PhylomeDB; Q9VI93; -.
DR BioGRID-ORCS; 40879; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40879; -.
DR PRO; PR:Q9VI93; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0267337; Expressed in labial segment and 20 other tissues.
DR ExpressionAtlas; Q9VI93; baseline and differential.
DR Genevisible; Q9VI93; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0001708; P:cell fate specification; IMP:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..946
FT /note="Zinc finger protein rotund"
FT /id="PRO_0000372664"
FT ZN_FING 488..510
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 517..539
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 545..567
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 573..597
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 603..625
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 10..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..495
FT /note="MIMHGTWYKGPQLAHHPHSNPHNSSHGHSDYHQFRSYPSFVVTPYHDGHVQG
FT PATPTPCTAPPTPCNGPVPVSVPVSIPVCHTGGQGSPVIVESSFAIAAAAAAAAAAVAV
FT GGSSATPLLPSPPIKIEQVFGEPSSLGAVVEDYALGLDCPVEHTFRKPHNNNGYSWSTG
FT NNNEVVSHSSNGHTNNHPTTPPTPPNEASATQATSVSAINLNQAQPASQTRSNFGSSIK
FT SPPSEPDAVTAATCKSQENNSGQNPTPNSLSDHNPAHNLNSNSTAAAVAAAAAAAAAAN
FT MPIGGVQGQNPTQGLVHWMSAVMAEHMTGQTHHDPGAVGMHYMWNGNVDHAKDISDYNL
FT WPPTPRSHQHASEHHPMSLKQEYEAKMNDHHHNNLQKGHFLDDNRLEHHAVTGQGGLGL
FT GASNGVGGGGGGASVVGNSSLGASSHHAVAAAHHHNQAVAAASAAALLVVPQPINASKM
FT GGPGGVSSVAGGHATGGGSGRKYQCKMCPQ -> MEGRLIEYRPIGGGLDYHHNSPLIG
FT EIPPAGGDYSHAVHRSIDHLRNSLNERVALGPLSVFSNTADLRNSVLSYSQQPHQQPQP
FT PQQQQQQQQQQHHQQQQHQYQLVPEPKPSITNLESSVASSAVSGSVASGQKHVNDAVVS
FT SSSGSSSTAGPAPTGSTRGRKSRIYPNPNQHIIVTSNSVDNGGIRMQNATLNERNSQNS
FT SAGAAGVGNVTTAAGSGNGISSSTSSPHHMTQLDVKDTK (in isoform roe)"
FT /evidence="ECO:0000303|PubMed:11874922"
FT /id="VSP_037179"
FT VAR_SEQ 274..677
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_037180"
FT CONFLICT 278
FT /note="Missing (in Ref. 1; AAL59599)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="G -> R (in Ref. 1; AAL59599)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="G -> R (in Ref. 1; AAL59599)"
FT /evidence="ECO:0000305"
FT CONFLICT 938
FT /note="S -> I (in Ref. 4; AAY51555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 946 AA; 100948 MW; 05EA01C8F64F61A3 CRC64;
MIMHGTWYKG PQLAHHPHSN PHNSSHGHSD YHQFRSYPSF VVTPYHDGHV QGPATPTPCT
APPTPCNGPV PVSVPVSIPV CHTGGQGSPV IVESSFAIAA AAAAAAAAVA VGGSSATPLL
PSPPIKIEQV FGEPSSLGAV VEDYALGLDC PVEHTFRKPH NNNGYSWSTG NNNEVVSHSS
NGHTNNHPTT PPTPPNEASA TQATSVSAIN LNQAQPASQT RSNFGSSIKS PPSEPDAVTA
ATCKSQENNS GQNPTPNSLS DHNPAHNLNS NSTAAAVAAA AAAAAAANMP IGGVQGQNPT
QGLVHWMSAV MAEHMTGQTH HDPGAVGMHY MWNGNVDHAK DISDYNLWPP TPRSHQHASE
HHPMSLKQEY EAKMNDHHHN NLQKGHFLDD NRLEHHAVTG QGGLGLGASN GVGGGGGGAS
VVGNSSLGAS SHHAVAAAHH HNQAVAAASA AALLVVPQPI NASKMGGPGG VSSVAGGHAT
GGGSGRKYQC KMCPQIFSSK ADLQLHTQIH MREAKPYKCT QCSKAFANSS YLSQHTRIHL
GIKPYRCEIC QRKFTQLSHL QQHIRTHTGD KPYKCRHPGC QKAFSQLSNL QSHSRCHQTD
KPFKCNSCYK CFSDEPSLLE HIPKHKESKH LKTHICQYCG KSYTQETYLT KHMQKHAERT
DKRPPIVPGS AAAIAAAAAA AAGGSANPAN GPPPPPNPAQ HQRNNLGLPP VSIAPSDNGY
WPKVSPDSAA AANAMEVMHQ QQQQQQQQQQ QQQQQQQQQQ QQAHHHHPQH GVPPQQHVPP
QQQQQQQQQQ QHHHPQQQPP PQHSMEAHYA QPTAPNGSQS NGHGAELQPH HRMPDPVRED
IASTPSAVGP YDAASITKTT SNSAFTPINS MPPHLNSLSH HPMAQRPYLY DAISFPNKNV
NQNNANAFPN QLISLHQIRN YAHQPAGLMA GEHLLGVSVG PGKDKG
