TSG_DROME
ID TSG_DROME Reviewed; 249 AA.
AC P54356; Q9VYR6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein twisted gastrulation;
DE Flags: Precursor;
GN Name=tsg; ORFNames=CG1502;
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 [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=7958834; DOI=10.1101/gad.8.13.1489;
RA Mason E.D., Konrad K.D., Webb C.D., Marsh J.L.;
RT "Dorsal midline fate in Drosophila embryos requires twisted gastrulation, a
RT gene encoding a secreted protein related to human connective tissue growth
RT factor.";
RL Genes Dev. 8:1489-1501(1994).
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 DPP AND SOG.
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).
CC -!- FUNCTION: Involved in dorsal-ventral patterning. Required for
CC specification of a narrow strip of dorsal midline cells that will give
CC rise to the amnioserosa, but not for specification of dorsal ectoderm
CC cells. Inhibits BMP signaling; enhances the binding of sog to dpp, thus
CC enhancing the antagonistic activity of sog.
CC {ECO:0000269|PubMed:11260716, ECO:0000269|PubMed:7958834}.
CC -!- SUBUNIT: Component of a complex composed of dpp, sog and tsg.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: First appears in stage 4 embryos, expressed in two
CC domains: a broad mid-dorsal saddle and an anterior cap, expression
CC between the domains is continuous across the dorsal midline. At stage
CC 5, expression is refined into 4 graded stripes in the mid-dorsal region
CC and a paired domain in the anterior region. During stages 7 and 8,
CC anterior expression fades and the mid dorsal stripes are located
CC between the anterior and posterior transverse furrow (ATF and PTF).
CC Expressing cells become incorporated into the deepening PTF.
CC {ECO:0000269|PubMed:7958834}.
CC -!- DEVELOPMENTAL STAGE: Gastrulating embryo. {ECO:0000269|PubMed:7958834}.
CC -!- SIMILARITY: Belongs to the twisted gastrulation protein family.
CC {ECO:0000305}.
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DR EMBL; U09808; AAC24234.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48123.1; -; Genomic_DNA.
DR PIR; A53836; A53836.
DR RefSeq; NP_511135.1; NM_078580.4.
DR AlphaFoldDB; P54356; -.
DR BioGRID; 58565; 14.
DR DIP; DIP-17785N; -.
DR STRING; 7227.FBpp0073426; -.
DR GlyGen; P54356; 1 site.
DR PaxDb; P54356; -.
DR DNASU; 32160; -.
DR EnsemblMetazoa; FBtr0073582; FBpp0073426; FBgn0003865.
DR GeneID; 32160; -.
DR KEGG; dme:Dmel_CG1502; -.
DR CTD; 32160; -.
DR FlyBase; FBgn0003865; tsg.
DR VEuPathDB; VectorBase:FBgn0003865; -.
DR eggNOG; ENOG502QRE9; Eukaryota.
DR GeneTree; ENSGT00390000007058; -.
DR HOGENOM; CLU_082511_0_0_1; -.
DR InParanoid; P54356; -.
DR OMA; CECVGEN; -.
DR OrthoDB; 1254178at2759; -.
DR PhylomeDB; P54356; -.
DR BioGRID-ORCS; 32160; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32160; -.
DR PRO; PR:P54356; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003865; Expressed in cleaving embryo and 2 other tissues.
DR ExpressionAtlas; P54356; differential.
DR Genevisible; P54356; DM.
DR GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0036122; F:BMP binding; IPI:FlyBase.
DR GO; GO:0008201; F:heparin binding; IDA:FlyBase.
DR GO; GO:0007378; P:amnioserosa formation; IMP:FlyBase.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:FlyBase.
DR GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; IDA:FlyBase.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central.
DR InterPro; IPR006761; Tsg.
DR PANTHER; PTHR12312; PTHR12312; 1.
DR Pfam; PF04668; Tsg; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..249
FT /note="Protein twisted gastrulation"
FT /id="PRO_0000022598"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 249 AA; 27220 MW; 313EE6A406E4B86D CRC64;
MQLLCYFVIL FVGIAPWSSL ANDDGCNEVV CGSVVSKCLI TQSCQCKLND CHCCKDCLNC
LGELYIECCG CLDMCPKHKD VLPSLTPRSE IGDIEGVPEL FDTLTAEDDE GWSTIRFSMR
AGFKQRVQGG ASGDAGNGNG NGNAGSAGVT LCTVIYVNSC IRANKCRQQC ESMGASSYRW
FHDGCCECVG ENCLNYGINE SRCRGCPEDQ DQLLTADTVP AEAEQDLERF FGNEEIEDEW
GYGEEDEFS
