TSL_DROME
ID TSL_DROME Reviewed; 353 AA.
AC P40689; Q9VD80;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Torso-like protein;
DE Flags: Precursor;
GN Name=tsl; ORFNames=CG6705;
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, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=8107870; DOI=10.1038/367741a0;
RA Martin J.-R., Raibaud A., Ollo R.;
RT "Terminal pattern elements in Drosophila embryo induced by the torso-like
RT protein.";
RL Nature 367:741-745(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Canton-S;
RX PubMed=8276237; DOI=10.1101/gad.7.12b.2548;
RA Savant-Bhonsale S., Montell D.J.;
RT "Torso-like encodes the localized determinant of Drosophila terminal
RT pattern formation.";
RL Genes Dev. 7:2548-2555(1993).
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;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12814553; DOI=10.1016/s0960-9822(03)00379-8;
RA Stevens L.M., Beuchle D., Jurcsak J., Tong X., Stein D.;
RT "The Drosophila embryonic patterning determinant torsolike is a component
RT of the eggshell.";
RL Curr. Biol. 13:1058-1063(2003).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-264, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
CC -!- FUNCTION: Probable ligand that binds to the torso receptor. Implicated
CC in a receptor tyrosine kinase signaling pathway that specifies terminal
CC cell fate. {ECO:0000269|PubMed:8107870, ECO:0000269|PubMed:8276237}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12814553,
CC ECO:0000269|PubMed:8107870}. Note=Is a component of the vitelline
CC membrane (VM, the inner layer of the eggshell).
CC -!- TISSUE SPECIFICITY: Restricted to specialized categories of follicle
CC cells localized at the poles of the egg chamber.
CC {ECO:0000269|PubMed:8107870, ECO:0000269|PubMed:8276237}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. At
CC early blastoderm stage, forms a symmetrical concentration gradient at
CC the poles on the surface of the devitellinized embryo.
CC {ECO:0000269|PubMed:8107870, ECO:0000269|PubMed:8276237}.
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DR EMBL; Z30342; CAA82998.1; -; Genomic_DNA.
DR EMBL; X75614; CAA53285.1; -; mRNA.
DR EMBL; AE014297; AAF55919.1; -; Genomic_DNA.
DR EMBL; AY071336; AAL48958.1; -; mRNA.
DR PIR; S42388; S42388.
DR RefSeq; NP_001262810.1; NM_001275881.1.
DR RefSeq; NP_524440.2; NM_079716.3.
DR RefSeq; NP_732660.1; NM_169969.2.
DR AlphaFoldDB; P40689; -.
DR BioGRID; 67529; 10.
DR STRING; 7227.FBpp0083562; -.
DR TCDB; 1.C.39.15.1; the membrane attack complex/perforin (macpf) family.
DR GlyGen; P40689; 6 sites.
DR iPTMnet; P40689; -.
DR PaxDb; P40689; -.
DR DNASU; 42564; -.
DR EnsemblMetazoa; FBtr0084164; FBpp0083562; FBgn0003867.
DR EnsemblMetazoa; FBtr0084165; FBpp0083563; FBgn0003867.
DR EnsemblMetazoa; FBtr0334312; FBpp0306427; FBgn0003867.
DR GeneID; 42564; -.
DR KEGG; dme:Dmel_CG6705; -.
DR CTD; 790953; -.
DR FlyBase; FBgn0003867; tsl.
DR VEuPathDB; VectorBase:FBgn0003867; -.
DR eggNOG; ENOG502QU9D; Eukaryota.
DR HOGENOM; CLU_052230_0_0_1; -.
DR InParanoid; P40689; -.
DR OMA; NYSMIKE; -.
DR OrthoDB; 1433145at2759; -.
DR PhylomeDB; P40689; -.
DR SignaLink; P40689; -.
DR BioGRID-ORCS; 42564; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42564; -.
DR PRO; PR:P40689; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003867; Expressed in head capsule and 38 other tissues.
DR ExpressionAtlas; P40689; baseline and differential.
DR Genevisible; P40689; DM.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0030546; F:signaling receptor activator activity; IDA:FlyBase.
DR GO; GO:0005122; F:torso binding; IDA:FlyBase.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IGI:FlyBase.
DR GO; GO:0008358; P:maternal determination of anterior/posterior axis, embryo; IMP:FlyBase.
DR GO; GO:0007278; P:pole cell fate determination; IGI:FlyBase.
DR GO; GO:0110074; P:positive regulation of apical constriction involved in ventral furrow formation; IMP:FlyBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:0035073; P:pupariation; IMP:FlyBase.
DR GO; GO:0007362; P:terminal region determination; IMP:FlyBase.
DR GO; GO:0008293; P:torso signaling pathway; IDA:FlyBase.
DR InterPro; IPR020864; MACPF.
DR SMART; SM00457; MACPF; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..353
FT /note="Torso-like protein"
FT /id="PRO_0000022599"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1..2
FT /note="MR -> MLSDA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="P -> L (in Ref. 2; CAA53285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 41210 MW; 2E76B8C5E78A358A CRC64;
MRSWPGLFWL LTLALLADGG RRESQLRIGK AINIFLRYGY LGISMRVIPL NDNSEPDRWV
FKEPTKNIYR NLSGLAESHE DTTPGIFHGD FHMEFCENRR QLFQAYFRDF SIERMDKPWE
AFTGGWFPDN AAKKLGINTS FIQGDYSYVL VRVVRFRETG RLNAEIPVHQ PLEPDVRSRM
DQLQIGNITS AVRFMEDVGT HYVNSYTTGN SLYQVFVYSR KNYSMIKERI KSKGLNGLSK
LDLYNYFAPW FAAHLGQIRS ASANATVERW ARRKLQYEYY VVKYVTLLKL HGNSTLLRSL
DSLLGNDAIL QLDLKSLKPI FREEPEKESW YHEVLDNNVK LWELNMPQSH PTR
