ID TRSF_DROME Reviewed; 197 AA.
AC P11596; Q540G8; Q86LR9; Q9VV78;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 02-SEP-2026, entry version 162.
DE RecName: Full=Female-specific protein transformer;
GN Name=tra; ORFNames=CG16724;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2441872; DOI=10.1016/0092-8674(87)90332-1;
RA Boggs R.T., Gregor P., Idriss S., Belote J.M., McKeown M.;
RT "Regulation of sexual differentiation in D. melanogaster via alternative
RT splicing of RNA from the transformer gene.";
RL Cell 50:739-747(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8013913; DOI=10.1093/genetics/136.4.1367;
RA Walthour C.S., Schaeffer S.W.;
RT "Molecular population genetics of sex determination genes: the transformer
RT gene of Drosophila melanogaster.";
RL Genetics 136:1367-1372(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=14021-0231.0, 14021-0231.4, 14021-0231.6, CPA129, CPA46, I-13,
RC Z(H)12, Z(H)16, and Z(H)34;
RX PubMed=12644565; DOI=10.1093/molbev/msg053;
RA Kulathinal R.J., Skwarek L., Morton R.A., Singh R.S.;
RT "Rapid evolution of the sex-determining gene, transformer: structural
RT diversity and rate heterogeneity among sibling species of Drosophila.";
RL Mol. Biol. Evol. 20:441-452(2003).
RN [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF RS DOMAIN.
RX PubMed=1655279; DOI=10.1016/0092-8674(91)90185-2;
RA Li H., Bingham P.M.;
RT "Arginine/serine-rich domains of the su(wa) and tra RNA processing
RT regulators target proteins to a subnuclear compartment implicated in
RT splicing.";
RL Cell 67:335-342(1991).
RN [7]
RP FUNCTION, AND INTERACTION WITH SR PROTEINS IN ENHANCER COMPLEX.
RX PubMed=8334698; DOI=10.1016/0092-8674(93)90298-5;
RA Tian M., Maniatis T.;
RT "A splicing enhancer complex controls alternative splicing of doublesex
RT pre-mRNA.";
RL Cell 74:105-114(1993).
RN [8]
RP FUNCTION.
RX PubMed=9418892; DOI=10.1128/mcb.18.1.450;
RA Heinrichs V., Ryner L.C., Baker B.S.;
RT "Regulation of sex-specific selection of fruitless 5' splice sites by
RT transformer and transformer-2.";
RL Mol. Cell. Biol. 18:450-458(1998).
RN [9]
RP FUNCTION.
RX PubMed=2503251; DOI=10.1016/0092-8674(89)90426-1;
RA Sosnowski B.A., Belote J.M., McKeown M.;
RT "Sex-specific alternative splicing of RNA from the transformer gene results
RT from sequence-dependent splice site blockage.";
RL Cell 58:449-459(1989).
RN [10]
RP FUNCTION.
RX PubMed=1690860; DOI=10.1038/344461a0;
RA Inoue K., Hoshijima K., Sakamoto H., Shimura Y.;
RT "Binding of the Drosophila sex-lethal gene product to the alternative
RT splice site of transformer primary transcript.";
RL Nature 344:461-463(1990).
RN [11]
RP FUNCTION.
RX PubMed=7680770; DOI=10.1038/362171a0;
RA Valcarcel J., Singh R., Zamore P.D., Green M.R.;
RT "The protein Sex-lethal antagonizes the splicing factor U2AF to regulate
RT alternative splicing of transformer pre-mRNA.";
RL Nature 362:171-175(1993).
CC -!- FUNCTION: Member of the regulatory pathway controlling female somatic
CC sexual differentiation, regulated by Sxl (PubMed:1690860,
CC PubMed:2441872, PubMed:2503251, PubMed:7680770). Activates dsx female-
CC specific splicing by promoting the formation of a splicing enhancer
CC complex which consists of tra, tra2 and sr proteins (PubMed:8334698).
CC Together with tra-2, plays a role in switching fru splicing from the
CC male-specific pattern to the female-specific pattern through activation
CC of the female-specific fru 5'-splice site (PubMed:9418892). No known
CC function in males (PubMed:1690860, PubMed:2441872, PubMed:2503251,
CC PubMed:7680770). {ECO:0000269|PubMed:1690860,
CC ECO:0000269|PubMed:2441872, ECO:0000269|PubMed:2503251,
CC ECO:0000269|PubMed:7680770, ECO:0000269|PubMed:8334698,
CC ECO:0000269|PubMed:9418892}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:1655279}.
CC Note=Speckled subnuclear compartment. {ECO:0000269|PubMed:1655279}.
CC -!- INDUCTION: Transformer protein is only present in females due to sex-
CC specific alternative mRNA splicing of tra pre-mRNA (PubMed:1690860,
CC PubMed:2503251, PubMed:7680770). Female-specific alternative splicing
CC of tra pre-mRNA is controlled by Sxl, which binds tightly to a
CC characteristic uridine-rich polypyrimidine tract at the non-sex
CC specific 3' splice site in one of the tra introns, preventing the
CC general splicing factor U2AF from binding to this site and forcing it
CC to bind to the female-specific 3' splice site (PubMed:1690860,
CC PubMed:2503251, PubMed:7680770). As consequence, only the female-
CC specific transcripts are translated, while non-sex-specific RNA
CC expressed in males is not translated (PubMed:1690860, PubMed:2503251,
CC PubMed:7680770). {ECO:0000269|PubMed:1690860,
CC ECO:0000269|PubMed:2503251, ECO:0000269|PubMed:7680770}.
CC -!- DOMAIN: RS domain directs localization of proteins to the speckled
CC subnuclear compartment and the purpose of this localization is to allow
CC colocalization and co-concentration of components of the splicing and
CC splicing regulatory machinery to permit relatively high rates and/or
CC efficiencies of reaction and interaction. {ECO:0000269|PubMed:1655279}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
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DR EMBL; M17478; AAB59226.1; -; Genomic_DNA.
DR EMBL; L19464; AAA75340.1; -; Genomic_DNA.
DR EMBL; L19465; AAA75341.1; -; Genomic_DNA.
DR EMBL; L19466; AAA75342.1; -; Genomic_DNA.
DR EMBL; L19467; AAA28958.1; -; Genomic_DNA.
DR EMBL; L19468; AAA28959.1; -; Genomic_DNA.
DR EMBL; L19469; AAA28960.1; -; Genomic_DNA.
DR EMBL; L19470; AAA28961.1; -; Genomic_DNA.
DR EMBL; L19618; AAA28962.1; -; Genomic_DNA.
DR EMBL; L19619; AAA28963.1; -; Genomic_DNA.
DR EMBL; L19620; AAA28964.1; -; Genomic_DNA.
DR EMBL; AY183383; AAO38891.1; -; Genomic_DNA.
DR EMBL; AY183385; AAO38893.1; -; Genomic_DNA.
DR EMBL; AY183386; AAO38894.1; -; Genomic_DNA.
DR EMBL; AY183387; AAO38895.1; -; Genomic_DNA.
DR EMBL; AY183388; AAO38896.1; -; Genomic_DNA.
DR EMBL; AY183389; AAO38897.1; -; Genomic_DNA.
DR EMBL; AY183390; AAO38898.1; -; Genomic_DNA.
DR EMBL; AY183382; AAO38890.1; -; Genomic_DNA.
DR EMBL; AY183384; AAO38892.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49441.1; -; Genomic_DNA.
DR PIR; A29648; A29648.
DR RefSeq; NP_524114.1; NM_079390.3.
DR AlphaFoldDB; P11596; -.
DR BioGRID; 65151; 14.
DR FunCoup; P11596; 3.
DR STRING; 7227.FBpp0075123; -.
DR PaxDb; 7227-FBpp0075123; -.
DR PeptideAtlas; P11596; -.
DR EnsemblMetazoa; FBtr0075364; FBpp0075123; FBgn0003741.
DR GeneID; 39849; -.
DR KEGG; dme:Dmel_CG16724; -.
DR UCSC; CG16724-RA; d. melanogaster.
DR AGR; FB:FBgn0003741; -.
DR CTD; 6955; -.
DR FlyBase; FBgn0003741; tra.
DR VEuPathDB; VectorBase:FBgn0003741; -.
DR HOGENOM; CLU_130078_0_0_1; -.
DR InParanoid; P11596; -.
DR OrthoDB; 7871011at2759; -.
DR BioGRID-ORCS; 39849; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39849; -.
DR PRO; PR:P11596; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003741; Expressed in midgut large flat cell (Drosophila) in digestive tract and 151 other cell types or tissues.
DR ExpressionAtlas; P11596; baseline and differential.
DR GO; GO:0016607; C:nuclear speck; EXP:UniProtKB.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:FlyBase.
DR GO; GO:1990399; P:epithelium regeneration; IMP:FlyBase.
DR GO; GO:0030237; P:female sex determination; IDA:UniProtKB.
DR GO; GO:0046660; P:female sex differentiation; IDA:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:FlyBase.
DR GO; GO:2000035; P:regulation of stem cell division; IMP:FlyBase.
DR InterPro; IPR010519; Tra.
DR Pfam; PF06495; Transformer; 1.
PE 1: Evidence at protein level;
KW Differentiation; Nucleus; Reference proteome; Sexual differentiation.
FT CHAIN 1..197
FT /note="Female-specific protein transformer"
FT /id="PRO_0000065645"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..127
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 94
FT /note="R -> M (in strain: 14021-0231.6)"
FT CONFLICT 99
FT /note="S -> N (in Ref. 4; AAF49441)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="R -> H (in Ref. 4; AAF49441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 197 AA; 24134 MW; 10C0B7A6F0C1AF81 CRC64;
MKMDADSSGT QHRDSRGSRS RSRREREYHG RSSERDSRKK EHKIPYFADE VREQDRLRRL
RQRAHQSTRR TRSRSRSQSS IRESRHRRHR QRSRSRNRSR SRSSERKRRQ RSRSRSSERR
RRQRSPHRYN PPPKIINYYV QVPPQDFYGM SGMQQSFGYQ RLPRPPPFPP APYRYRQRPP
FIGVPRFGYR NAGRPPY
//
