TALAA_DROME
ID TALAA_DROME Reviewed; 32 AA.
AC A3RLR1;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Peptide tarsal-less AA {ECO:0000312|FlyBase:FBgn0259733};
DE AltName: Full=Peptide polished rice 4 {ECO:0000312|EMBL:BAF56588.1};
GN Name=tal-AA {ECO:0000312|FlyBase:FBgn0259733};
GN Synonyms=pri {ECO:0000312|EMBL:BAF56588.1},
GN tal {ECO:0000312|FlyBase:FBgn0259733};
GN ORFNames=CG42387 {ECO:0000312|FlyBase:FBgn0259733};
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] {ECO:0000312|EMBL:BAF56588.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17486114; DOI=10.1038/ncb1595;
RA Kondo T., Hashimoto Y., Kato K., Inagaki S., Hayashi S., Kageyama Y.;
RT "Small peptide regulators of actin-based cell morphogenesis encoded by a
RT polycistronic mRNA.";
RL Nat. Cell Biol. 9:660-665(2007).
RN [2] {ECO:0000312|EMBL:ABO09844.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17439302; DOI=10.1371/journal.pbio.0050106;
RA Galindo M.I., Pueyo J.I., Fouix S., Bishop S.A., Couso J.P.;
RT "Peptides encoded by short ORFs control development and define a new
RT eukaryotic gene family.";
RL PLoS Biol. 5:E106-E106(2007).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AFA55188.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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] {ECO:0000305}
RP FUNCTION.
RX PubMed=20647469; DOI=10.1126/science.1188158;
RA Kondo T., Plaza S., Zanet J., Benrabah E., Valenti P., Hashimoto Y.,
RA Kobayashi S., Payre F., Kageyama Y.;
RT "Small peptides switch the transcriptional activity of Shavenbaby during
RT Drosophila embryogenesis.";
RL Science 329:336-339(2010).
RN [7] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18801356; DOI=10.1016/j.ydbio.2008.08.025;
RA Pueyo J.I., Couso J.P.;
RT "The 11-aminoacid long Tarsal-less peptides trigger a cell signal in
RT Drosophila leg development.";
RL Dev. Biol. 324:192-201(2008).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=21527259; DOI=10.1016/j.ydbio.2011.03.033;
RA Pueyo J.I., Couso J.P.;
RT "Tarsal-less peptides control Notch signalling through the Shavenbaby
RT transcription factor.";
RL Dev. Biol. 355:183-193(2011).
RN [9] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=21682860; DOI=10.1186/1423-0127-18-42;
RA Pi H., Huang Y.C., Chen I.C., Lin C.D., Yeh H.F., Pai L.M.;
RT "Identification of 11-amino acid peptides that disrupt Notch-mediated
RT processes in Drosophila.";
RL J. Biomed. Sci. 18:42-42(2011).
RN [10] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION BY ECDYSONE.
RX PubMed=25344753; DOI=10.1038/ncb3052;
RA Chanut-Delalande H., Hashimoto Y., Pelissier-Monier A., Spokony R., Dib A.,
RA Kondo T., Bohere J., Niimi K., Latapie Y., Inagaki S., Dubois L.,
RA Valenti P., Polesello C., Kobayashi S., Moussian B., White K.P., Plaza S.,
RA Kageyama Y., Payre F.;
RT "Pri peptides are mediators of ecdysone for the temporal control of
RT development.";
RL Nat. Cell Biol. 16:1035-1044(2014).
RN [11] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26383956; DOI=10.1126/science.aac5677;
RA Zanet J., Benrabah E., Li T., Pelissier-Monier A., Chanut-Delalande H.,
RA Ronsin B., Bellen H.J., Payre F., Plaza S.;
RT "Pri sORF peptides induce selective proteasome-mediated protein
RT processing.";
RL Science 349:1356-1358(2015).
CC -!- FUNCTION: One of four peptides (tal-1A, tal-2A, tal-3A and tal-AA)
CC produced from a polycistronic gene that function redundantly in several
CC developmental processes (PubMed:17439302, PubMed:17486114,
CC PubMed:25344753, PubMed:21527259). Required in early stages of leg
CC development for the intercalation of the tarsal segments during the
CC mid-third instar stage and later for tarsal joint formation
CC (PubMed:17439302, PubMed:18801356, PubMed:21527259). Promotes the post-
CC translational modification of ovo isoform B (svb) into its active form
CC which in turn initiates trichome development and promotes tarsal joint
CC development (PubMed:21527259, PubMed:20647469, PubMed:26383956). This
CC is likely due to recruitment of the E3 ubiquitin-protein ligase Ubr3 to
CC svb for ubiquitination of its N-terminus, converting svb into a
CC transcriptional activator (PubMed:26383956). Also enhances interaction
CC of Ubr3 with Diap1 (PubMed:26383956). Required for correct wing and leg
CC formation through its regulation of several genes including those in
CC the Notch signaling pathway (PubMed:18801356, PubMed:21527259,
CC PubMed:21682860). Essential for denticle formation and may have a role
CC in the developmental timing of trichome differentiation
CC (PubMed:17486114, PubMed:25344753). Essential for the development of
CC taenidial folds in the trachea (PubMed:17486114).
CC {ECO:0000269|PubMed:17439302, ECO:0000269|PubMed:17486114,
CC ECO:0000269|PubMed:18801356, ECO:0000269|PubMed:20647469,
CC ECO:0000269|PubMed:21527259, ECO:0000269|PubMed:21682860,
CC ECO:0000269|PubMed:25344753, ECO:0000269|PubMed:26383956}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26383956}. Nucleus
CC {ECO:0000269|PubMed:26383956}.
CC -!- DEVELOPMENTAL STAGE: At early stages of embryogenesis, the
CC polycistronic RNA is expressed in seven segmentally separated
CC blastoderm stripes and in a cluster of cells in the anterior part of
CC the embryo (PubMed:17439302). By stage 13 to the end of embryo
CC development, it is expressed in the dorsal trunks, posterior spiracles,
CC pharynx, hindgut and the area which forms the denticle belts
CC (PubMed:17439302). In the leg disk, it is expressed in a ring pattern
CC presumed to be developing tarsal region around 80 to 96 h after egg
CC laying (AEL) and then in the tarsal furrow at the mid-third instar
CC larval stage (PubMed:17439302, PubMed:18801356). Not detected in the
CC tarsal primordium after 100h AEL but is still expressed in a dorsal
CC chordotonal organ of the leg disk (PubMed:17439302). In pupae,
CC expressed broadly throughout the leg disk 0-3 h after puparium
CC formation (APF) but is not detected in this region 6h APF
CC (PubMed:25344753). High expression 4-8 h APF in the presumptive joints
CC between tarsal segments (PubMed:21682860). In the noctum expressed from
CC 40 to 44 h APF (PubMed:25344753). In wing disks of third stage larvae,
CC expressed in two anterior stripes and later in the precursors for
CC chemosensory organs (PubMed:21682860). From late third stage instar
CC larvae to early pupal stages, it is also expressed in the wing provein
CC cells that develop into longitudinal veins L2-L5 (PubMed:21682860). In
CC eye disks, expressed in preclusters for presumptive R8 photoreceptors
CC and in a stripe of cells in the posterior region of the disk
CC (PubMed:21682860). {ECO:0000269|PubMed:17439302,
CC ECO:0000269|PubMed:18801356, ECO:0000269|PubMed:21682860,
CC ECO:0000269|PubMed:25344753}.
CC -!- INDUCTION: Polycistronic RNA up-regulated by ecdysone.
CC {ECO:0000269|PubMed:25344753}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous knockout of tal-1A, tal-2A, tal-3A
CC and tal-AA is embryonic lethal (PubMed:17439302, PubMed:17486114). In
CC embryos chitin secretion and formation of the cuticular exoskeleton
CC appears to be normal (PubMed:17439302, PubMed:17486114). However
CC embryos display a loss of denticle belts and dorsal hairs
CC (PubMed:17439302, PubMed:17486114). Segment-specific epidermal sensory
CC organs are present and segments form normally (PubMed:17439302). The
CC cephalopharyngeal skeleton is lost, and the head skeleton and posterior
CC spiracles are deformed (PubMed:17439302). In the developing leg, tarsal
CC constriction occurs but the tarsal fold does not form
CC (PubMed:17439302). The tracheal system is abnormal displaying a loss of
CC network integrity, an irregular tube diameter and the absence of
CC taenidial folds (PubMed:17439302, PubMed:17486114). Cell packing is not
CC affected, but there is no accumulation of F-actin at the sites of
CC denticle differentiation or formation of F-actin bundles during
CC taenidial development and tracheal tube dilation (stages 14 and 16)
CC (PubMed:17486114). Other F-actin based developmental processes such as
CC filopodia formation of tracheal tip cells, dorsal closure, mitosis or
CC tight packing of denticle cells are unaffected (PubMed:17486114).
CC Denticle and tracheal defects can be rescued by ectopic expression of
CC any one of the four tal peptides (tal-1A, tal-2A, tal-3A and tal-AA)
CC (PubMed:17486114). {ECO:0000269|PubMed:17439302,
CC ECO:0000269|PubMed:17486114}.
CC -!- MISCELLANEOUS: This protein is produced by a polycistronic gene which
CC also produces tal-1A, tal-2A and tal-3A from non-overlapping reading
CC frames (PubMed:17486114, PubMed:17439302). tal-1A and tal-2A produce
CC the same protein from different reading frames (PubMed:17486114,
CC PubMed:17439302). {ECO:0000269|PubMed:17439302,
CC ECO:0000269|PubMed:17486114}.
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DR EMBL; AB300657; BAF56588.1; -; mRNA.
DR EMBL; EF427619; ABO09844.1; -; mRNA.
DR EMBL; AE014297; ACL83507.1; -; Genomic_DNA.
DR EMBL; AY070879; AFA55188.1; -; mRNA.
DR RefSeq; NP_001138049.1; NM_001144577.2.
DR AlphaFoldDB; A3RLR1; -.
DR IntAct; A3RLR1; 1.
DR STRING; 7227.FBpp0289273; -.
DR PaxDb; A3RLR1; -.
DR EnsemblMetazoa; FBtr0299996; FBpp0289273; FBgn0259733.
DR GeneID; 7354377; -.
DR KEGG; dme:Dmel_CG42387; -.
DR CTD; 7354377; -.
DR FlyBase; FBgn0259733; tal-AA.
DR VEuPathDB; VectorBase:FBgn0259733; -.
DR HOGENOM; CLU_3392730_0_0_1; -.
DR InParanoid; A3RLR1; -.
DR OrthoDB; 1646028at2759; -.
DR BioGRID-ORCS; 7354377; 0 hits in 1 CRISPR screen.
DR ChiTaRS; tal-AA; fly.
DR GenomeRNAi; 7354377; -.
DR PRO; PR:A3RLR1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0259733; Expressed in saliva-secreting gland and 30 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007015; P:actin filament organization; IGI:FlyBase.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IGI:FlyBase.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..32
FT /note="Peptide tarsal-less AA"
FT /id="PRO_0000435524"
FT REPEAT 2..8
FT /note="1"
FT /evidence="ECO:0000305|PubMed:17439302,
FT ECO:0000305|PubMed:17486114"
FT REPEAT 26..32
FT /note="2"
FT /evidence="ECO:0000305|PubMed:17439302,
FT ECO:0000305|PubMed:17486114"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..32
FT /note="2 X 7 AA repeats of L-D-P-T-G-[TQ]-Y"
FT /evidence="ECO:0000305|PubMed:17439302,
FT ECO:0000305|PubMed:17486114"
FT COMPBIAS 9..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 32 AA; 3855 MW; 56E2E98A4BAE0ACE CRC64;
MLDPTGTYRR PRDTQDSRQK RRQDCLDPTG QY
