TLL_DROME
ID TLL_DROME Reviewed; 452 AA.
AC P18102; Q4V6W1; Q9VA33;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Protein tailless;
DE AltName: Full=Nuclear receptor subfamily 2 group E member 2;
GN Name=tll; Synonyms=NR2E2; ORFNames=CG1378;
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], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Oregon-R;
RX PubMed=2364433; DOI=10.1016/0092-8674(90)90249-e;
RA Pignoni F., Baldarelli R.M., Steingrimsson E., Diaz R.J., Patapoutian A.,
RA Merriam J.R., Lengyel J.A.;
RT "The Drosophila gene tailless is expressed at the embryonic termini and is
RT a member of the steroid receptor superfamily.";
RL Cell 62:151-163(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8430097; DOI=10.1073/pnas.90.3.858;
RA Liaw G.-J., Steingrimsson E., Pignoni F., Courey A.J., Lengyel J.A.;
RT "Characterization of downstream elements in a Raf-1 pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:858-862(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;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=10357938; DOI=10.1242/dev.126.13.2945;
RA Daniel A., Dumstrei K., Lengyel J.A., Hartenstein V.;
RT "The control of cell fate in the embryonic visual system by atonal,
RT tailless and EGFR signaling.";
RL Development 126:2945-2954(1999).
CC -!- FUNCTION: Orphan receptor that binds DNA as a monomer to hormone
CC response elements (HRE) containing an extended core motif half-site
CC sequence 5'-AAGTCA-3' in which the 5' flanking nucleotides participate
CC in determining receptor specificity. This receptor binds to the
CC consensus sequence [AG][AG]AAGTCAA. Plays a key role in the
CC establishment of non-metameric domains at the anterior and posterior
CC poles of the embryo. It may also play a role in the nervous system. The
CC maternal terminal pathway activates the tll gene in the termini; TLL
CC activity then represses segmentation and activates terminal-specific
CC genes in these domains. Involved in the regulation of early eye
CC development. In the embryonic visual system anlage drives cells to
CC optic lobe as opposed to Bolwig's organ fate.
CC {ECO:0000269|PubMed:10357938, ECO:0000269|PubMed:2364433}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC P18102; Q9N693: sbb; NbExp=2; IntAct=EBI-159966, EBI-3403504;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- TISSUE SPECIFICITY: Brain and peripheral nervous system.
CC {ECO:0000269|PubMed:2364433}.
CC -!- DEVELOPMENTAL STAGE: During stage 10 found in the anterior part of the
CC visual system that later gives rise to the anterior lip of the optic
CC lobe. At stage 12 also found in the posterior lip of the optic lobe. In
CC third larval instar expressed in the optic lobe of the larval brain and
CC in the eye antennal disk, both in antennal and eye portion.
CC {ECO:0000269|PubMed:2364433}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; M34639; AAA28936.1; -; mRNA.
DR EMBL; AF019362; AAB71371.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF57091.1; -; Genomic_DNA.
DR EMBL; BT022195; AAY51589.1; -; mRNA.
DR PIR; A35602; A35602.
DR RefSeq; NP_524596.1; NM_079857.4.
DR AlphaFoldDB; P18102; -.
DR SMR; P18102; -.
DR BioGRID; 68506; 32.
DR DIP; DIP-19302N; -.
DR IntAct; P18102; 7.
DR STRING; 7227.FBpp0085071; -.
DR PaxDb; P18102; -.
DR PRIDE; P18102; -.
DR EnsemblMetazoa; FBtr0085709; FBpp0085071; FBgn0003720.
DR GeneID; 43656; -.
DR KEGG; dme:Dmel_CG1378; -.
DR UCSC; CG1378-RA; d. melanogaster.
DR CTD; 43656; -.
DR FlyBase; FBgn0003720; tll.
DR VEuPathDB; VectorBase:FBgn0003720; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156693; -.
DR HOGENOM; CLU_007368_20_3_1; -.
DR InParanoid; P18102; -.
DR OMA; VVSLMHK; -.
DR OrthoDB; 870262at2759; -.
DR PhylomeDB; P18102; -.
DR Reactome; R-DME-383280; Nuclear Receptor transcription pathway.
DR SignaLink; P18102; -.
DR BioGRID-ORCS; 43656; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43656; -.
DR PRO; PR:P18102; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003720; Expressed in procephalic neurogenic region (Drosophila) and 39 other tissues.
DR Genevisible; P18102; DM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0001746; P:Bolwig's organ morphogenesis; TAS:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IMP:FlyBase.
DR GO; GO:0001708; P:cell fate specification; TAS:FlyBase.
DR GO; GO:0001748; P:insect visual primordium development; IMP:FlyBase.
DR GO; GO:0002121; P:inter-male aggressive behavior; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0014019; P:neuroblast development; IMP:FlyBase.
DR GO; GO:0055057; P:neuroblast division; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035271; P:ring gland development; IMP:FlyBase.
DR GO; GO:0023061; P:signal release; IGI:FlyBase.
DR GO; GO:0007362; P:terminal region determination; TAS:FlyBase.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Activator; Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Receptor; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..452
FT /note="Protein tailless"
FT /id="PRO_0000053597"
FT DOMAIN 189..450
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 31..108
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 34..54
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 70..96
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 342..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 50549 MW; A4ABEFFDE993A37C CRC64;
MQSSEGSPDM MDQKYNSVRL SPAASSRILY HVPCKVCRDH SSGKHYGIYA CDGCAGFFKR
SIRRSRQYVC KSQKQGLCVV DKTHRNQCRA CRLRKCFEVG MNKDAVQHER GPRNSTLRRH
MAMYKDAMMG AGEMPQIPAE ILMNTAALTG FPGVPMPMPG LPQRAGHHPA HMAAFQPPPS
AAAVLDLSVP RVPHHPVHQG HHGFFSPTAA YMNALATRAL PPTPPLMAAE HIKETAAEHL
FKNVNWIKSV RAFTELPMPD QLLLLEESWK EFFILAMAQY LMPMNFAQLL FVYESENANR
EIMGMVTREV HAFQEVLNQL CHLNIDSTEY ECLRAISLFR KSPPSASSTE DLANSSILTG
SGSPNSSASA ESRGLLESGK VAAMHNDARS ALHNYIQRTH PSQPMRFQTL LGVVQLMHKV
SSFTIEELFF RKTIGDITIV RLISDMYSQR KI