DECA_DROME
ID DECA_DROME Reviewed; 588 AA.
AC P07713; A4V009; P91651; Q6AWM1; Q8I0M7; Q8ITK4; Q9VQC6;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Protein decapentaplegic;
DE Short=Protein DPP-C;
DE Flags: Precursor;
GN Name=dpp; ORFNames=CG9885;
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=3467201; DOI=10.1038/325081a0;
RA Padgett R.W., St Johnston R.D., Gelbart W.M.;
RT "A transcript from a Drosophila pattern gene predicts a protein homologous
RT to the transforming growth factor-beta family.";
RL Nature 325:81-84(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-59 AND MET-121.
RC STRAIN=DP CN BW;
RX PubMed=9071586; DOI=10.1093/genetics/145.2.311;
RA Richter B., Long M., Lewontin R.C., Nitasaka E.;
RT "Nucleotide variation and conservation at the dpp locus, a gene controlling
RT early development in Drosophila.";
RL Genetics 145:311-323(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 291-509, AND VARIANT ALA-439.
RX PubMed=12618399; DOI=10.1093/genetics/163.2.599;
RA Mousset S., Brazier L., Cariou M.L., Chartois F., Depaulis F., Veuille M.;
RT "Evidence of a high rate of selective sweeps in African Drosophila
RT melanogaster.";
RL Genetics 163:599-609(2003).
RN [7]
RP PROTEIN SEQUENCE OF 457-476, FUNCTION, SUBCELLULAR LOCATION, AND
RP PROTEOLYTIC CLEAVAGE AT ARG-456.
RX PubMed=1692958; DOI=10.1128/mcb.10.6.2669-2677.1990;
RA Panganiban G.E.F., Rashka K.E., Neitzel M.D., Hoffmann F.M.;
RT "Biochemical characterization of the Drosophila dpp protein, a member of
RT the transforming growth factor beta family of growth factors.";
RL Mol. Cell. Biol. 10:2669-2677(1990).
RN [8]
RP FUNCTION.
RX PubMed=3123323; DOI=10.1101/gad.1.8.868;
RA Irish V.F., Gelbart W.M.;
RT "The decapentaplegic gene is required for dorsal-ventral patterning of the
RT Drosophila embryo.";
RL Genes Dev. 1:868-879(1987).
RN [9]
RP FUNCTION.
RX PubMed=8252627; DOI=10.1016/0092-8674(93)90535-x;
RA Heberlein U., Wolff T., Rubin G.M.;
RT "The TGF beta homolog dpp and the segment polarity gene hedgehog are
RT required for propagation of a morphogenetic wave in the Drosophila
RT retina.";
RL Cell 75:913-926(1993).
RN [10]
RP FUNCTION.
RX PubMed=7720583; DOI=10.1242/dev.121.3.785;
RA Sturtevant M.A., Bier E.;
RT "Analysis of the genetic hierarchy guiding wing vein development in
RT Drosophila.";
RL Development 121:785-801(1995).
RN [11]
RP FUNCTION.
RX PubMed=7700357; DOI=10.1038/374464a0;
RA Frasch M.;
RT "Induction of visceral and cardiac mesoderm by ectodermal Dpp in the early
RT Drosophila embryo.";
RL Nature 374:464-467(1995).
RN [12]
RP FUNCTION.
RX PubMed=9226445; DOI=10.1242/dev.124.14.2741;
RA Vincent S., Ruberte E., Grieder N.C., Chen C.-K., Haerry T., Schuh R.,
RA Affolter M.;
RT "DPP controls tracheal cell migration along the dorsoventral body axis of
RT the Drosophila embryo.";
RL Development 124:2741-2750(1997).
RN [13]
RP FUNCTION.
RX PubMed=9695953; DOI=10.1016/s0092-8674(00)81424-5;
RA Xie T., Spradling A.C.;
RT "decapentaplegic is essential for the maintenance and division of germline
RT stem cells in the Drosophila ovary.";
RL Cell 94:251-260(1998).
RN [14]
RP FUNCTION.
RX PubMed=9636086; DOI=10.1242/dev.125.14.2723;
RA Khalsa O., Yoon J.-W., Torres-Schumann S., Wharton K.A.;
RT "TGF-beta/BMP superfamily members, Gbb-60A and Dpp, cooperate to provide
RT pattern information and establish cell identity in the Drosophila wing.";
RL Development 125:2723-2734(1998).
RN [15]
RP FUNCTION.
RX PubMed=10495279; DOI=10.1016/s0925-4773(99)00157-4;
RA Steneberg P., Hemphala J., Samakovlis C.;
RT "Dpp and Notch specify the fusion cell fate in the dorsal branches of the
RT Drosophila trachea.";
RL Mech. Dev. 87:153-163(1999).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11136981; DOI=10.1016/s0092-8674(00)00199-9;
RA Teleman A.A., Cohen S.M.;
RT "Dpp gradient formation in the Drosophila wing imaginal disc.";
RL Cell 103:971-980(2000).
RN [17]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11136982; DOI=10.1016/s0092-8674(00)00200-2;
RA Entchev E.V., Schwabedissen A., Gonzalez-Gaitan M.;
RT "Gradient formation of the TGF-beta homolog Dpp.";
RL Cell 103:981-991(2000).
RN [18]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10903186; DOI=10.1242/dev.127.16.3631;
RA Araujo H., Bier E.;
RT "sog and dpp exert opposing maternal functions to modify toll signaling and
RT pattern the dorsoventral axis of the Drosophila embryo.";
RL Development 127:3631-3644(2000).
RN [19]
RP REVIEW.
RX PubMed=11432817; DOI=10.1093/emboj/20.13.3298;
RA Affolter M., Marty T., Vigano M.A., Jazwinska A.;
RT "Nuclear interpretation of Dpp signaling in Drosophila.";
RL EMBO J. 20:3298-3305(2001).
RN [20]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11231061; DOI=10.1016/s0925-4773(00)00555-4;
RA Takashima S., Murakami R.;
RT "Regulation of pattern formation in the Drosophila hindgut by wg, hh, dpp,
RT and en.";
RL Mech. Dev. 101:79-90(2001).
RN [21]
RP FUNCTION, AND INTERACTION WITH SOG AND TSG.
RX PubMed=11260716; DOI=10.1038/35068578;
RA Ross J.J., Shimmi O., Vilmos P., Petryk A., Kim H., Gaudenz K.,
RA Hermanson S., Ekker S.C., O'Connor M.B., Marsh J.L.;
RT "Twisted gastrulation is a conserved extracellular BMP antagonist.";
RL Nature 410:479-483(2001).
RN [22]
RP FUNCTION.
RX PubMed=12135920; DOI=10.1242/dev.129.16.3815;
RA Cavodeassi F., Rodriguez I., Modolell J.;
RT "Dpp signalling is a key effector of the wing-body wall subdivision of the
RT Drosophila mesothorax.";
RL Development 129:3815-3823(2002).
RN [23]
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=15797386; DOI=10.1016/j.cell.2005.02.009;
RA Shimmi O., Umulis D., Othmer H., O'Connor M.B.;
RT "Facilitated transport of a Dpp/Scw heterodimer by Sog/Tsg leads to robust
RT patterning of the Drosophila blastoderm embryo.";
RL Cell 120:873-886(2005).
RN [24]
RP REVIEW.
RX PubMed=15867930; DOI=10.1038/ncb0505-456;
RA Schuldt A.;
RT "Dpp gets in shape.";
RL Nat. Cell Biol. 7:456-456(2005).
CC -!- FUNCTION: Required during oogenesis for eggshell patterning and
CC dorsal/ventral patterning of the embryo. Acts as a morphogen during
CC embryogenesis to pattern the dorsal/ventral axis, specifying dorsal
CC ectoderm and amnioserosa cell fate within the dorsal half of the
CC embryo; this activity is antagonized by binding to sog and tsg. Induces
CC the formation of visceral mesoderm and the heart in early embryos.
CC Required later in embryogenesis for dorsal closure and patterning of
CC the hindgut. Also functions postembryonically as a long-range morphogen
CC during imaginal disk development; is responsible for the progression of
CC the morphogenetic furrow during eye development. Patterns the wing
CC imaginal disk along its anterior/posterior axis and has a role in
CC positioning pro-veins. Also required to subdivide the wing disk along
CC the proximal/distal axis into body wall (notum) and wing. Ensures the
CC correct architecture of wing epithelial cells. Has multiple roles in
CC the developing tracheal system, controlling directed tracheal cell
CC migration during embryogenesis and later specifying the fate of fusion
CC cells in the tracheal branches. Required for viability of larvae.
CC Essential for the maintenance and division of germline stem cells in
CC the ovary. Signals via the type I receptor tkv, the type II receptor
CC punt, and in some tissues via the type I receptor sax, in a signaling
CC cascade that leads to activation and repression of target genes.
CC {ECO:0000269|PubMed:10495279, ECO:0000269|PubMed:10903186,
CC ECO:0000269|PubMed:11136981, ECO:0000269|PubMed:11231061,
CC ECO:0000269|PubMed:11260716, ECO:0000269|PubMed:12135920,
CC ECO:0000269|PubMed:15797386, ECO:0000269|PubMed:1692958,
CC ECO:0000269|PubMed:3123323, ECO:0000269|PubMed:7700357,
CC ECO:0000269|PubMed:7720583, ECO:0000269|PubMed:8252627,
CC ECO:0000269|PubMed:9226445, ECO:0000269|PubMed:9636086,
CC ECO:0000269|PubMed:9695953}.
CC -!- SUBUNIT: Heterodimers of scw/dpp are the active subunit, dpp/dpp
CC homodimers elicit a basal response and scw/scw homodimers alone are
CC ineffective in specifying a dorsal pattern. Component of a complex
CC composed of dpp, sog and tsg. {ECO:0000269|PubMed:15797386}.
CC -!- INTERACTION:
CC P07713; P08120: Col4a1; NbExp=3; IntAct=EBI-499422, EBI-109669;
CC P07713; O18407: vkg; NbExp=5; IntAct=EBI-499422, EBI-15721782;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11136981,
CC ECO:0000269|PubMed:11136982, ECO:0000269|PubMed:1692958}. Note=Is
CC internalized by receptor-mediated endocytosis.
CC -!- TISSUE SPECIFICITY: Expressed in the dorsal region of the embryo, and
CC becomes enriched in a dorsal midline stripe just prior to gastrulation.
CC Expressed in midgut mesoderm and in two overlapping regions of the
CC embryonic large intestine. Expressed in a long-range concentration
CC gradient in the wing imaginal disk. {ECO:0000269|PubMed:11136981,
CC ECO:0000269|PubMed:11136982, ECO:0000269|PubMed:11231061,
CC ECO:0000269|PubMed:15797386}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. First
CC detected during stages 8 to 10 of oogenesis.
CC {ECO:0000269|PubMed:10903186}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; M30116; AAA28482.1; -; mRNA.
DR EMBL; U63857; AAC47552.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51250.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10431.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10432.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10434.1; -; Genomic_DNA.
DR EMBL; BT015227; AAT94456.1; -; mRNA.
DR EMBL; AF459545; AAN61361.1; -; Genomic_DNA.
DR EMBL; AF459546; AAN61362.1; -; Genomic_DNA.
DR EMBL; AF459547; AAN61363.1; -; Genomic_DNA.
DR EMBL; AF459548; AAN61364.1; -; Genomic_DNA.
DR EMBL; AF459549; AAN61365.1; -; Genomic_DNA.
DR EMBL; AF459550; AAN61366.1; -; Genomic_DNA.
DR EMBL; AF459551; AAN61367.1; -; Genomic_DNA.
DR EMBL; AF459552; AAN61368.1; -; Genomic_DNA.
DR EMBL; AF459553; AAN61369.1; -; Genomic_DNA.
DR EMBL; AF459554; AAN61370.1; -; Genomic_DNA.
DR EMBL; AF459555; AAN61371.1; -; Genomic_DNA.
DR EMBL; AF459556; AAN61372.1; -; Genomic_DNA.
DR EMBL; AF459557; AAN61373.1; -; Genomic_DNA.
DR EMBL; AF459558; AAN61374.1; -; Genomic_DNA.
DR EMBL; AF459559; AAN61375.1; -; Genomic_DNA.
DR EMBL; AF459560; AAN61376.1; -; Genomic_DNA.
DR EMBL; AF459561; AAN61377.1; -; Genomic_DNA.
DR EMBL; AF459562; AAN61378.1; -; Genomic_DNA.
DR EMBL; AF459563; AAN61379.1; -; Genomic_DNA.
DR EMBL; AF459564; AAN61380.1; -; Genomic_DNA.
DR PIR; A26158; A26158.
DR RefSeq; NP_477311.1; NM_057963.5.
DR RefSeq; NP_722810.1; NM_164485.2.
DR RefSeq; NP_722811.1; NM_164486.2.
DR RefSeq; NP_722813.1; NM_164488.2.
DR AlphaFoldDB; P07713; -.
DR SMR; P07713; -.
DR BioGRID; 59659; 101.
DR DIP; DIP-19N; -.
DR IntAct; P07713; 3.
DR STRING; 7227.FBpp0077451; -.
DR GlyGen; P07713; 4 sites.
DR PaxDb; P07713; -.
DR EnsemblMetazoa; FBtr0077771; FBpp0077451; FBgn0000490.
DR EnsemblMetazoa; FBtr0077772; FBpp0077452; FBgn0000490.
DR EnsemblMetazoa; FBtr0077773; FBpp0077453; FBgn0000490.
DR EnsemblMetazoa; FBtr0077775; FBpp0077455; FBgn0000490.
DR GeneID; 33432; -.
DR KEGG; dme:Dmel_CG9885; -.
DR UCSC; CG9885-RB; d. melanogaster.
DR CTD; 33432; -.
DR FlyBase; FBgn0000490; dpp.
DR VEuPathDB; VectorBase:FBgn0000490; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000174461; -.
DR HOGENOM; CLU_020515_4_2_1; -.
DR InParanoid; P07713; -.
DR OMA; HEEHMEQ; -.
DR OrthoDB; 1063560at2759; -.
DR PhylomeDB; P07713; -.
DR Reactome; R-DME-201451; Signaling by BMP.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR SignaLink; P07713; -.
DR BioGRID-ORCS; 33432; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33432; -.
DR PRO; PR:P07713; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000490; Expressed in crop (Drosophila) and 62 other tissues.
DR Genevisible; P07713; DM.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0098898; C:dense core granule lumen; IDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0070700; F:BMP receptor binding; IPI:FlyBase.
DR GO; GO:0005518; F:collagen binding; IDA:FlyBase.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IDA:FlyBase.
DR GO; GO:0016015; F:morphogen activity; IMP:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR GO; GO:0007378; P:amnioserosa formation; IMP:FlyBase.
DR GO; GO:0061327; P:anterior Malpighian tubule development; IMP:FlyBase.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:FlyBase.
DR GO; GO:0010002; P:cardioblast differentiation; IMP:FlyBase.
DR GO; GO:0061352; P:cell chemotaxis involved in Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0007304; P:chorion-containing eggshell formation; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IGI:FlyBase.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:UniProtKB.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0001715; P:ectodermal cell fate specification; IMP:FlyBase.
DR GO; GO:0048619; P:embryonic hindgut morphogenesis; IMP:UniProtKB.
DR GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:UniProtKB.
DR GO; GO:0035214; P:eye-antennal disc development; IMP:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0035156; P:fusion cell fate specification; IMP:UniProtKB.
DR GO; GO:0035224; P:genital disc anterior/posterior pattern formation; IEP:FlyBase.
DR GO; GO:0035215; P:genital disc development; IMP:FlyBase.
DR GO; GO:0035263; P:genital disc sexually dimorphic development; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR GO; GO:0042078; P:germ-line stem cell division; IMP:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0060323; P:head morphogenesis; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0007516; P:hemocyte development; IMP:FlyBase.
DR GO; GO:0007442; P:hindgut morphogenesis; IMP:FlyBase.
DR GO; GO:0007444; P:imaginal disc development; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0035217; P:labial disc development; IMP:FlyBase.
DR GO; GO:0035168; P:larval lymph gland hemocyte differentiation; IMP:FlyBase.
DR GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0007313; P:maternal specification of dorsal/ventral axis, oocyte, soma encoded; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IEP:FlyBase.
DR GO; GO:0045705; P:negative regulation of salivary gland boundary specification; TAS:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0061320; P:pericardial nephrocyte differentiation; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045572; P:positive regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0048636; P:positive regulation of muscle organ development; IMP:FlyBase.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:FlyBase.
DR GO; GO:0007458; P:progression of morphogenetic furrow involved in compound eye morphogenesis; IMP:UniProtKB.
DR GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; TAS:UniProtKB.
DR GO; GO:0045570; P:regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IGI:FlyBase.
DR GO; GO:0035158; P:regulation of tube diameter, open tracheal system; IMP:FlyBase.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR GO; GO:0030721; P:spectrosome organization; IMP:FlyBase.
DR GO; GO:0035309; P:wing and notum subfield formation; IMP:UniProtKB.
DR GO; GO:0035222; P:wing disc pattern formation; IMP:UniProtKB.
DR GO; GO:0007352; P:zygotic specification of dorsal/ventral axis; IMP:UniProtKB.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..456
FT /evidence="ECO:0000269|PubMed:1692958"
FT /id="PRO_0000033664"
FT CHAIN 457..588
FT /note="Protein decapentaplegic"
FT /id="PRO_0000033665"
FT REGION 74..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..154
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 456
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:1692958"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 487..553
FT /evidence="ECO:0000250"
FT DISULFID 516..585
FT /evidence="ECO:0000250"
FT DISULFID 520..587
FT /evidence="ECO:0000250"
FT DISULFID 552
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VARIANT 59
FT /note="V -> G (in strain: dp cn bw)"
FT /evidence="ECO:0000269|PubMed:9071586"
FT VARIANT 121
FT /note="K -> M (in strain: dp cn bw)"
FT /evidence="ECO:0000269|PubMed:9071586"
FT VARIANT 439
FT /note="P -> A"
FT /evidence="ECO:0000269|PubMed:12618399"
FT CONFLICT 473..474
FT /note="QP -> HA (in Ref. 1; AAA28482)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="T -> K (in Ref. 5; AAT94456)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="D -> G (in Ref. 5; AAT94456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 588 AA; 65868 MW; 2C8166C1BD2F666B CRC64;
MRAWLLLLAV LATFQTIVRV ASTEDISQRF IAAIAPVAAH IPLASASGSG SGRSGSRSVG
ASTSTALAKA FNPFSEPASF SDSDKSHRSK TNKKPSKSDA NRQFNEVHKP RTDQLENSKN
KSKQLVNKPN HNKMAVKEQR SHHKKSHHHR SHQPKQASAS TESHQSSSIE SIFVEEPTLV
LDREVASINV PANAKAIIAE QGPSTYSKEA LIKDKLKPDP STLVEIEKSL LSLFNMKRPP
KIDRSKIIIP EPMKKLYAEI MGHELDSVNI PKPGLLTKSA NTVRSFTHKD SKIDDRFPHH
HRFRLHFDVK SIPADEKLKA AELQLTRDAL SQQVVASRSS ANRTRYQVLV YDITRVGVRG
QREPSYLLLD TKTVRLNSTD TVSLDVQPAV DRWLASPQRN YGLLVEVRTV RSLKPAPHHH
VRLRRSADEA HERWQHKQPL LFTYTDDGRH KARSIRDVSG GEGGGKGGRN KRQPRRPTRR
KNHDDTCRRH SLYVDFSDVG WDDWIVAPLG YDAYYCHGKC PFPLADHFNS TNHAVVQTLV
NNMNPGKVPK ACCVPTQLDS VAMLYLNDQS TVVLKNYQEM TVVGCGCR
