SCAL_DROME
ID SCAL_DROME Reviewed; 440 AA.
AC P30052; Q9VXN7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Protein scalloped;
GN Name=sd; ORFNames=CG8544;
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].
RX PubMed=1547938; DOI=10.1101/gad.6.3.367;
RA Campbell S.D., Inamdar M., Rodrigues V., Raghavan V., Palazzolo M.,
RA Chovnick A.;
RT "The scalloped gene encodes a novel, evolutionarily conserved transcription
RT factor required for sensory organ differentiation in Drosophila.";
RL Genes Dev. 6:367-379(1992).
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.
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 FUNCTION, AND INTERACTION WITH VG.
RX PubMed=9869635; DOI=10.1101/gad.12.24.3815;
RA Simmonds A.J., Liu X., Soanes K.H., Krause H.M., Irvine K.D., Bell J.B.;
RT "Molecular interactions between Vestigial and Scalloped promote wing
RT formation in Drosophila.";
RL Genes Dev. 12:3815-3820(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH VG.
RX PubMed=9869643; DOI=10.1101/gad.12.24.3900;
RA Halder G., Polaczyk P., Kraus M.E., Hudson A., Kim J., Laughon A.,
RA Carroll S.B.;
RT "The Vestigial and Scalloped proteins act together to directly regulate
RT wing-specific gene expression in Drosophila.";
RL Genes Dev. 12:3900-3909(1998).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11112330; DOI=10.1006/dbio.2000.9939;
RA Liu X., Grammont M., Irvine K.D.;
RT "Roles for scalloped and vestigial in regulating cell affinity and
RT interactions between the wing blade and the wing hinge.";
RL Dev. Biol. 228:287-303(2000).
RN [7]
RP DNA-BINDING OF VG-SD COMPLEX.
RX PubMed=11546746; DOI=10.1242/dev.128.17.3295;
RA Halder G., Carroll S.B.;
RT "Binding of the vestigial co-factor switches the DNA-target selectivity of
RT the scalloped selector protein.";
RL Development 128:3295-3305(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH VG.
RX PubMed=12782275; DOI=10.1016/s0925-4773(03)00037-6;
RA Srivastava A., Bell J.B.;
RT "Further developmental roles of the vestigial/scalloped transcription
RT complex during wing development in Drosophila melanogaster.";
RL Mech. Dev. 120:587-596(2003).
RN [9]
RP FUNCTION, AND INTERACTION WITH YKI.
RX PubMed=18313299; DOI=10.1016/j.cub.2008.02.034;
RA Goulev Y., Fauny J.D., Gonzalez-Marti B., Flagiello D., Silber J.,
RA Zider A.;
RT "SCALLOPED interacts with YORKIE, the nuclear effector of the hippo tumor-
RT suppressor pathway in Drosophila.";
RL Curr. Biol. 18:435-441(2008).
RN [10]
RP FUNCTION.
RX PubMed=18258485; DOI=10.1016/j.devcel.2008.01.006;
RA Zhang L., Ren F., Zhang Q., Chen Y., Wang B., Jiang J.;
RT "The TEAD/TEF family of transcription factor Scalloped mediates Hippo
RT signaling in organ size control.";
RL Dev. Cell 14:377-387(2008).
CC -!- FUNCTION: Transcription factor which plays a key role in the Hippo/SWH
CC (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a
CC pivotal role in organ size control and tumor suppression by restricting
CC proliferation and promoting apoptosis. The core of this pathway is
CC composed of a kinase cascade wherein Hippo (Hpo), in complex with its
CC regulatory protein Salvador (Sav), phosphorylates and activates Warts
CC (Wts) in complex with its regulatory protein Mats, which in turn
CC phosphorylates and inactivates the Yorkie (Yki) oncoprotein. The
CC Hippo/SWH signaling pathway inhibits the activity of the
CC transcriptional complex formed by Scalloped (sd) and Yki and the target
CC genes of this pathway include cyclin-E (cycE), diap1 and bantam. Sd
CC promotes nuclear localization of Yki. Involved in the regulation of
CC cell-specific gene expression during development, particularly in the
CC differentiation of the nervous system. When in combination with
CC vestigial (vg) it acts as a transcriptional activation complex that
CC regulates gene expression in the wing. Binding to vg switches the DNA
CC target selectivity of sd. Required autonomously for cell proliferation
CC and viability within the wing blade. Required for proper sensory organ
CC precursor (SOP) differentiation at the wing margin; required for
CC correct expression of sens. {ECO:0000269|PubMed:11112330,
CC ECO:0000269|PubMed:12782275, ECO:0000269|PubMed:18258485,
CC ECO:0000269|PubMed:18313299, ECO:0000269|PubMed:9869635,
CC ECO:0000269|PubMed:9869643}.
CC -!- SUBUNIT: The C-terminus of sd interacts with the C-terminal serine-rich
CC protein domain of vg, to form a complex which acts as a selector for
CC wing development. Interacts (via C-terminus) with yki (via N-terminus)
CC and this interaction enhances its transcriptional activity.
CC {ECO:0000269|PubMed:12782275, ECO:0000269|PubMed:18313299,
CC ECO:0000269|PubMed:9869635, ECO:0000269|PubMed:9869643}.
CC -!- INTERACTION:
CC P30052; Q26366: vg; NbExp=7; IntAct=EBI-151228, EBI-162687;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Subset of neuroblasts in the central nervous system
CC and in the peripheral sense organs of the embryo. Expressed in the
CC developing wing primordia initially along the D/V wing boundary, and by
CC the late third larval instar, maximal expression is seen in cells at
CC the D/V wing disk boundary. Less expression in cells located farther
CC from this boundary. Also expressed in wing progenitor cells.
CC {ECO:0000269|PubMed:11112330}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M83787; AAA28881.1; -; mRNA.
DR EMBL; AE014298; AAF48521.1; -; Genomic_DNA.
DR PIR; A42136; A42136.
DR RefSeq; NP_001096990.1; NM_001103520.3.
DR RefSeq; NP_001096991.1; NM_001103521.3.
DR RefSeq; NP_001096992.1; NM_001103522.3.
DR RefSeq; NP_001245697.1; NM_001258768.1.
DR RefSeq; NP_001259582.1; NM_001272653.2.
DR RefSeq; NP_001259583.1; NM_001272654.2.
DR RefSeq; NP_511169.1; NM_078614.5.
DR PDB; 6Y20; X-ray; 1.85 A; A/B=222-440.
DR PDBsum; 6Y20; -.
DR AlphaFoldDB; P30052; -.
DR SMR; P30052; -.
DR BioGRID; 58884; 52.
DR DIP; DIP-21510N; -.
DR IntAct; P30052; 3.
DR SwissPalm; P30052; -.
DR PaxDb; P30052; -.
DR DNASU; 32536; -.
DR EnsemblMetazoa; FBtr0074099; FBpp0073914; FBgn0003345.
DR EnsemblMetazoa; FBtr0112825; FBpp0111737; FBgn0003345.
DR EnsemblMetazoa; FBtr0112826; FBpp0111738; FBgn0003345.
DR EnsemblMetazoa; FBtr0112827; FBpp0111739; FBgn0003345.
DR EnsemblMetazoa; FBtr0308129; FBpp0300451; FBgn0003345.
DR EnsemblMetazoa; FBtr0310312; FBpp0301995; FBgn0003345.
DR EnsemblMetazoa; FBtr0310313; FBpp0301996; FBgn0003345.
DR GeneID; 32536; -.
DR KEGG; dme:Dmel_CG8544; -.
DR CTD; 32536; -.
DR FlyBase; FBgn0003345; sd.
DR VEuPathDB; VectorBase:FBgn0003345; -.
DR eggNOG; KOG3841; Eukaryota.
DR GeneTree; ENSGT00950000182956; -.
DR InParanoid; P30052; -.
DR PhylomeDB; P30052; -.
DR Reactome; R-DME-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-DME-390193; Transcriptional activation by YKI.
DR Reactome; R-DME-8951671; RUNX3 regulates YAP1-mediated transcription.
DR SignaLink; P30052; -.
DR BioGRID-ORCS; 32536; 0 hits in 3 CRISPR screens.
DR ChiTaRS; sd; fly.
DR GenomeRNAi; 32536; -.
DR PRO; PR:P30052; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003345; Expressed in eye disc (Drosophila) and 58 other tissues.
DR ExpressionAtlas; P30052; baseline and differential.
DR Genevisible; P30052; DM.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:FlyBase.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
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:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:FlyBase.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:FlyBase.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:FlyBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
DR GO; GO:0035329; P:hippo signaling; IBA:GO_Central.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IDA:UniProtKB.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IDA:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:2000826; P:regulation of heart morphogenesis; IGI:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
DR GO; GO:0072089; P:stem cell proliferation; IDA:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR Gene3D; 6.10.20.40; -; 1.
DR InterPro; IPR000818; TEA/ATTS_dom.
DR InterPro; IPR038096; TEA/ATTS_sf.
DR InterPro; IPR016361; TEF_metazoa.
DR InterPro; IPR041086; YBD.
DR Pfam; PF01285; TEA; 1.
DR Pfam; PF17725; YBD; 1.
DR PIRSF; PIRSF002603; TEF; 1.
DR PRINTS; PR00065; TEADOMAIN.
DR SMART; SM00426; TEA; 1.
DR PROSITE; PS00554; TEA_1; 1.
DR PROSITE; PS51088; TEA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cell cycle; Developmental protein;
KW Differentiation; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..440
FT /note="Protein scalloped"
FT /id="PRO_0000205942"
FT DNA_BIND 86..162
FT /note="TEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00505"
FT REGION 32..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 228..243
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 246..256
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6Y20"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6Y20"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:6Y20"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:6Y20"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 319..330
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 334..342
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 362..371
FT /evidence="ECO:0007829|PDB:6Y20"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:6Y20"
FT HELIX 389..397
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 399..407
FT /evidence="ECO:0007829|PDB:6Y20"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 413..423
FT /evidence="ECO:0007829|PDB:6Y20"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:6Y20"
SQ SEQUENCE 440 AA; 49658 MW; B885D7F713473A79 CRC64;
MKNITSSSTC STGLLQLQNN LSCSELEVAE KTEQQAVGPG TIPSPWTPVN AGPPGALGSA
DTNGSMVDSK NLDVGDMSDD EKDLSSADAE GVWSPDIEQS FQEALSIYPP CGRRKIILSD
EGKMYGRNEL IARYIKLRTG KTRTRKQVSS HIQVLARRKL REIQAKIKVQ FWQPGLQPST
SQDFYDYSIK PFPQPPYPAG KTSTAVSGDE TGIPPSQLPW EGRAIATHKF RLLEFTAFME
IQRDEIYHRH LFVQLGGKPS FSDPLLETVD IRQIFDKFPE KSGGLKDLYE KGPQNAFYLV
KCWADLNTDL TTGSETGDFY GVTSQYESNE NVVLVCSTIV CSFGKQVVEK VESEYSRLEN
NRYVYRIQRS PMCEYMINFI QKLKNLPERY MMNSVLENFT ILQVMRARET QETLLCIAYV
FEVAAQNSGT THHIYRLIKE
