SXL_DROME
ID SXL_DROME Reviewed; 354 AA.
AC P19339; A4V434; A4V435; A4V436; A4V437; C9QP40; D0IQK2; D3PFI6; E1JJI8;
AC E1JJI9; E1JJJ0; E1JJJ2; E1JJJ3; P19340; Q0KHV2; Q26466; Q2MGN7; Q2MGN8;
AC Q2MGN9; Q2MGP1; Q7KVU6; Q7YZ92; Q8IRQ1; Q99141; Q9TYF5; Q9W3S6;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Protein sex-lethal;
GN Name=Sxl; Synonyms=Sx1; ORFNames=CG43770;
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] (ISOFORMS MS3 AND CM1), FUNCTION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=3144435; DOI=10.1016/0092-8674(88)90248-6;
RA Bell L.R., Maine E.M., Schedl P., Cline T.W.;
RT "Sex-lethal, a Drosophila sex determination switch gene, exhibits sex-
RT specific RNA splicing and sequence similarity to RNA binding proteins.";
RL Cell 55:1037-1046(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MS3; MS11 AND MS16), FUNCTION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=1710769; DOI=10.1128/mcb.11.7.3584-3602.1991;
RA Samuels M.E., Schedl P., Cline T.W.;
RT "The complex set of late transcripts from the Drosophila sex determination
RT gene sex-lethal encodes multiple related polypeptides.";
RL Mol. Cell. Biol. 11:3584-3602(1991).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORMS A; W; MS16 AND V).
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Booth B.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26 (ISOFORM 1), AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=1547493; DOI=10.1016/0092-8674(92)90036-c;
RA Keyes L.N., Cline T.W., Schedl P.;
RT "The primary sex determination signal of Drosophila acts at the level of
RT transcription.";
RL Cell 68:933-943(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41 (ISOFORM MS3).
RX PubMed=8978052; DOI=10.1093/genetics/144.4.1653;
RA Penalva L.O.F., Sakamoto H., Navarro-Sabate A., Sakashita E., Granadino B.,
RA Segarra C., Sanchez L.;
RT "Regulation of the gene Sex-lethal: a comparative analysis of Drosophila
RT melanogaster and Drosophila subobscura.";
RL Genetics 144:1653-1664(1996).
RN [8]
RP ALTERNATIVE SPLICING.
RX PubMed=1454517; DOI=10.1093/nar/20.21.5533;
RA Sakamoto H., Inoue K., Higuchi I., Ono Y., Shimura Y.;
RT "Control of Drosophila Sex-lethal pre-mRNA splicing by its own female-
RT specific product.";
RL Nucleic Acids Res. 20:5533-5540(1992).
RN [9]
RP IDENTIFICATION IN COMPLEX WITH FL(2)D AND VIR.
RX PubMed=12444081; DOI=10.1074/jbc.m210737200;
RA Ortega A., Niksic M., Bachi A., Wilm M., Sanchez L., Hastie N.,
RA Valcarcel J.;
RT "Biochemical function of female-lethal (2)D/Wilms' tumor suppressor-1-
RT associated proteins in alternative pre-mRNA splicing.";
RL J. Biol. Chem. 278:3040-3047(2003).
RN [10]
RP INTERACTION WITH NITO.
RX PubMed=26324914; DOI=10.1073/pnas.1515891112;
RA Yan D., Perrimon N.;
RT "spenito is required for sex determination in Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11606-11611(2015).
RN [11]
RP STRUCTURE BY NMR OF 199-294.
RX PubMed=7524663; DOI=10.1021/bi00250a031;
RA Lee A.L., Kanaar R., Rio D.C., Wemmer D.E.;
RT "Resonance assignments and solution structure of the second RNA-binding
RT domain of sex-lethal determined by multidimensional heteronuclear magnetic
RT resonance.";
RL Biochemistry 33:13775-13786(1994).
RN [12]
RP STRUCTURE BY NMR OF 122-209.
RX PubMed=9299339; DOI=10.1006/jmbi.1997.1213;
RA Inoue M., Muto Y., Sakamoto H., Kigawa T., Takio K., Shimura Y.,
RA Yokoyama S.;
RT "A characteristic arrangement of aromatic amino acid residues in the
RT solution structure of the amino-terminal RNA-binding domain of Drosophila
RT sex-lethal.";
RL J. Mol. Biol. 272:82-94(1997).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 122-289, AND RNA-BINDING.
RX PubMed=10217141; DOI=10.1038/19242;
RA Handa N., Nureki O., Kurimoto K., Kim I., Sakamoto H., Shimura Y., Muto Y.,
RA Yokoyama S.;
RT "Structural basis for recognition of the tra mRNA precursor by the Sex-
RT lethal protein.";
RL Nature 398:579-585(1999).
CC -!- FUNCTION: Sex determination switch protein which controls sexual
CC development by sex-specific splicing. Regulates dosage compensation in
CC females by suppressing hyperactivation of X-linked genes. Expression of
CC the embryo-specific isoform is under the control of primary sex-
CC determining signal, which depends on the ratio of X chromosomes
CC relative to autosomes (X:A ratio). Expression occurs in 2X:2A cells,
CC but not in X:2A cells. The X:A ratio seems to be signaled by the
CC relative concentration of the X-linked transcription factors SIS-A and
CC SIS-B. As a result, the embryo-specific product is expressed early only
CC in female embryos and specifies female-adult specific splicing; in the
CC male where it is not expressed, the default splicing gives rise to a
CC truncated non-functional protein. The female-specific isoform specifies
CC the splicing of its own transcript, thereby initiating a positive
CC autoregulatory feedback loop leading to female development pathway. The
CC female-specific isoform controls the sex-specific splicing of
CC transformer (TRA); acts as a translational repressor for male-specific
CC lethal-2 (MSL-2) and prevents male-less (MLE), MSL-1 and MSL-3 proteins
CC from associating with the female X chromosome.
CC {ECO:0000269|PubMed:1547493, ECO:0000269|PubMed:1710769,
CC ECO:0000269|PubMed:3144435}.
CC -!- SUBUNIT: Part of a complex containing fl(2)d, Sxl and vir
CC (PubMed:12444081). Interacts with nito (PubMed:26324914).
CC {ECO:0000269|PubMed:12444081, ECO:0000269|PubMed:26324914}.
CC -!- INTERACTION:
CC P19339-1; Q9VSK3: Unr; NbExp=8; IntAct=EBI-16120780, EBI-194879;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=14;
CC Comment=Additional isoforms seem to exist.;
CC Name=MS3; Synonyms=CF1, D, female-specific, L, T;
CC IsoId=P19339-1; Sequence=Displayed;
CC Name=1;
CC IsoId=P19339-2; Sequence=VSP_005881;
CC Name=A; Synonyms=E, U;
CC IsoId=P19339-10; Sequence=VSP_019287, VSP_005883;
CC Name=C; Synonyms=N;
CC IsoId=P19339-8; Sequence=VSP_005881, VSP_005883;
CC Name=CM1; Synonyms=B, F, M;
CC IsoId=P19339-3; Sequence=VSP_005882, VSP_005884;
CC Name=G; Synonyms=J;
CC IsoId=P19339-7; Sequence=VSP_005883;
CC Name=W;
CC IsoId=P19339-9; Sequence=VSP_005883, VSP_005886;
CC Name=K; Synonyms=Q;
CC IsoId=P19339-11; Sequence=VSP_019289, VSP_019290;
CC Name=MS11; Synonyms=H;
CC IsoId=P19339-4; Sequence=VSP_005883, VSP_005885;
CC Name=MS16; Synonyms=P;
CC IsoId=P19339-5; Sequence=VSP_005886;
CC Name=O;
CC IsoId=P19339-6; Sequence=VSP_005881, VSP_005883, VSP_005885;
CC Name=R;
CC IsoId=P19339-12; Sequence=VSP_005881, VSP_005883, VSP_005886;
CC Name=S;
CC IsoId=P19339-13; Sequence=VSP_019287;
CC Name=V;
CC IsoId=P19339-14; Sequence=VSP_040526;
CC -!- TISSUE SPECIFICITY: Expressed in somatic tissues, but not in the pole
CC cells, which are the precursors of the germline.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is embryo-specific. Isoform CM1 is male-
CC specific. Isoforms MS3, MS11 and MS16 are female specific. Isoform 1 is
CC expressed for a brief period during the syncytial blastoderm stage.
CC Isoform MS11 is expressed in 4-7 hours embryo.
CC {ECO:0000269|PubMed:1710769, ECO:0000269|PubMed:3144435}.
CC -!- DOMAIN: The Gly-Asn rich domain is required for the cooperative
CC interaction with RNA and for regulating the splicing activity.
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DR EMBL; M23635; AAA28885.1; -; mRNA.
DR EMBL; M23636; AAA28884.1; -; mRNA.
DR EMBL; M59447; AAA28922.1; -; mRNA.
DR EMBL; M59448; AAA28921.1; -; mRNA.
DR EMBL; AE014298; AAF46240.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF46241.4; -; Genomic_DNA.
DR EMBL; AE014298; AAG22410.1; -; Genomic_DNA.
DR EMBL; AE014298; AAG22411.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09197.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09198.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09200.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09201.2; -; Genomic_DNA.
DR EMBL; AE014298; AAO41638.2; -; Genomic_DNA.
DR EMBL; AE014298; AAZ52509.1; -; Genomic_DNA.
DR EMBL; AE014298; AAZ52510.1; -; Genomic_DNA.
DR EMBL; AE014298; AAZ52511.1; -; Genomic_DNA.
DR EMBL; AE014298; AAZ52512.1; -; Genomic_DNA.
DR EMBL; AE014298; AAZ52513.1; -; Genomic_DNA.
DR EMBL; AE014298; AAZ52514.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95222.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95223.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95224.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95225.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95226.1; -; Genomic_DNA.
DR EMBL; BT003583; AAO39587.1; -; mRNA.
DR EMBL; BT099922; ACX32993.1; -; mRNA.
DR EMBL; BT100240; ACY56908.1; -; mRNA.
DR EMBL; BT120392; ADD20766.1; -; mRNA.
DR EMBL; S88324; AAB21845.1; -; Genomic_DNA.
DR EMBL; D84425; BAA20294.1; -; Genomic_DNA.
DR PIR; A31639; A31639.
DR PIR; A39725; B31639.
DR RefSeq; NP_001027062.1; NM_001031891.3. [P19339-6]
DR RefSeq; NP_001027063.1; NM_001031892.2. [P19339-8]
DR RefSeq; NP_001027064.1; NM_001031893.2. [P19339-3]
DR RefSeq; NP_001027065.1; NM_001031894.1. [P19339-1]
DR RefSeq; NP_001027066.1; NM_001031895.1. [P19339-11]
DR RefSeq; NP_001162686.1; NM_001169215.2. [P19339-5]
DR RefSeq; NP_001162687.1; NM_001169216.2. [P19339-11]
DR RefSeq; NP_001162688.1; NM_001169217.2. [P19339-12]
DR RefSeq; NP_001162689.1; NM_001169218.3. [P19339-13]
DR RefSeq; NP_001162690.1; NM_001169219.1. [P19339-1]
DR RefSeq; NP_001259305.1; NM_001272376.1. [P19339-11]
DR RefSeq; NP_001259306.1; NM_001272377.1. [P19339-3]
DR RefSeq; NP_524791.3; NM_080052.4. [P19339-8]
DR RefSeq; NP_727160.2; NM_167110.3. [P19339-7]
DR RefSeq; NP_727161.3; NM_167111.3. [P19339-9]
DR RefSeq; NP_727162.2; NM_167112.2. [P19339-1]
DR RefSeq; NP_727163.2; NM_167113.3. [P19339-10]
DR RefSeq; NP_727164.2; NM_167114.2. [P19339-4]
DR RefSeq; NP_727165.2; NM_167115.3. [P19339-10]
DR RefSeq; NP_727166.2; NM_167116.2. [P19339-7]
DR RefSeq; NP_727167.2; NM_167117.2. [P19339-3]
DR RefSeq; NP_727168.1; NM_167118.2. [P19339-3]
DR PDB; 1B7F; X-ray; 2.60 A; A/B=122-289.
DR PDB; 1SXL; NMR; -; A=199-294.
DR PDB; 2SXL; NMR; -; A=122-209.
DR PDB; 3SXL; X-ray; 2.70 A; A/B/C=111-294.
DR PDB; 4QQB; X-ray; 2.80 A; A/B=122-294.
DR PDBsum; 1B7F; -.
DR PDBsum; 1SXL; -.
DR PDBsum; 2SXL; -.
DR PDBsum; 3SXL; -.
DR PDBsum; 4QQB; -.
DR AlphaFoldDB; P19339; -.
DR BMRB; P19339; -.
DR SASBDB; P19339; -.
DR SMR; P19339; -.
DR BioGRID; 533777; 116.
DR DIP; DIP-44607N; -.
DR IntAct; P19339; 9.
DR MINT; P19339; -.
DR STRING; 7227.FBpp0303693; -.
DR PaxDb; P19339; -.
DR DNASU; 3772180; -.
DR EnsemblMetazoa; FBtr0331247; FBpp0303689; FBgn0264270. [P19339-9]
DR EnsemblMetazoa; FBtr0331249; FBpp0303691; FBgn0264270. [P19339-3]
DR EnsemblMetazoa; FBtr0331250; FBpp0303692; FBgn0264270. [P19339-7]
DR EnsemblMetazoa; FBtr0331251; FBpp0303693; FBgn0264270. [P19339-4]
DR EnsemblMetazoa; FBtr0331253; FBpp0303695; FBgn0264270. [P19339-7]
DR EnsemblMetazoa; FBtr0331254; FBpp0303696; FBgn0264270. [P19339-11]
DR EnsemblMetazoa; FBtr0331255; FBpp0303697; FBgn0264270. [P19339-1]
DR EnsemblMetazoa; FBtr0331256; FBpp0303698; FBgn0264270. [P19339-3]
DR EnsemblMetazoa; FBtr0331257; FBpp0303699; FBgn0264270. [P19339-8]
DR EnsemblMetazoa; FBtr0331258; FBpp0303700; FBgn0264270. [P19339-6]
DR EnsemblMetazoa; FBtr0331259; FBpp0303701; FBgn0264270. [P19339-10]
DR EnsemblMetazoa; FBtr0331260; FBpp0303702; FBgn0264270. [P19339-3]
DR EnsemblMetazoa; FBtr0331261; FBpp0303703; FBgn0264270. [P19339-8]
DR EnsemblMetazoa; FBtr0331262; FBpp0303704; FBgn0264270. [P19339-1]
DR EnsemblMetazoa; FBtr0331263; FBpp0303705; FBgn0264270. [P19339-10]
DR EnsemblMetazoa; FBtr0331264; FBpp0303706; FBgn0264270. [P19339-5]
DR EnsemblMetazoa; FBtr0331265; FBpp0303707; FBgn0264270. [P19339-11]
DR EnsemblMetazoa; FBtr0331266; FBpp0303708; FBgn0264270. [P19339-12]
DR EnsemblMetazoa; FBtr0331268; FBpp0303710; FBgn0264270. [P19339-1]
DR EnsemblMetazoa; FBtr0336727; FBpp0307708; FBgn0264270. [P19339-11]
DR EnsemblMetazoa; FBtr0336728; FBpp0307709; FBgn0264270. [P19339-3]
DR EnsemblMetazoa; FBtr0336729; FBpp0307710; FBgn0264270. [P19339-13]
DR GeneID; 3772180; -.
DR KEGG; dme:Dmel_CG43770; -.
DR UCSC; CG18350-RE; d. melanogaster.
DR UCSC; CG18350-RF; d. melanogaster.
DR UCSC; CG18350-RL; d. melanogaster.
DR UCSC; CG18350-RN; d. melanogaster.
DR CTD; 3772180; -.
DR FlyBase; FBgn0264270; Sxl.
DR VEuPathDB; VectorBase:FBgn0264270; -.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; P19339; -.
DR PhylomeDB; P19339; -.
DR SignaLink; P19339; -.
DR BioGRID-ORCS; 3772180; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Sxl; fly.
DR EvolutionaryTrace; P19339; -.
DR GenomeRNAi; 3772180; -.
DR PRO; PR:P19339; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0264270; Expressed in saliva-secreting gland and 25 other tissues.
DR ExpressionAtlas; P19339; baseline and differential.
DR Genevisible; P19339; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IPI:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:FlyBase.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IDA:FlyBase.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:FlyBase.
DR GO; GO:0008187; F:poly-pyrimidine tract binding; IDA:FlyBase.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0007549; P:dosage compensation; TAS:FlyBase.
DR GO; GO:1990399; P:epithelium regeneration; IMP:FlyBase.
DR GO; GO:0030237; P:female sex determination; IMP:FlyBase.
DR GO; GO:0048142; P:germarium-derived cystoblast division; IMP:FlyBase.
DR GO; GO:0007446; P:imaginal disc growth; IMP:FlyBase.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; TAS:FlyBase.
DR GO; GO:0017148; P:negative regulation of translation; IDA:FlyBase.
DR GO; GO:0045947; P:negative regulation of translational initiation; IMP:FlyBase.
DR GO; GO:0009994; P:oocyte differentiation; IDA:FlyBase.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IDA:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IDA:FlyBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; TAS:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:FlyBase.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; TAS:FlyBase.
DR GO; GO:2000035; P:regulation of stem cell division; IMP:FlyBase.
DR GO; GO:0007530; P:sex determination; TAS:FlyBase.
DR GO; GO:0007541; P:sex determination, primary response to X:A ratio; TAS:FlyBase.
DR GO; GO:0007548; P:sex differentiation; TAS:FlyBase.
DR GO; GO:0018993; P:somatic sex determination; TAS:FlyBase.
DR DisProt; DP01605; -.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR002343; Hud_Sxl_RNA.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR006546; Sxl.
DR Pfam; PF00076; RRM_1; 2.
DR PRINTS; PR00961; HUDSXLRNA.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR TIGRFAMs; TIGR01659; sex-lethal; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Differentiation; Reference proteome;
KW Repeat; RNA-binding; Sexual differentiation; Transcription;
KW Transcription regulation.
FT CHAIN 1..354
FT /note="Protein sex-lethal"
FT /id="PRO_0000081967"
FT DOMAIN 125..203
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 211..291
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform A and isoform S)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_019287"
FT VAR_SEQ 1..25
FT /note="MYGNNNPGSNNNNGGYPPYGYNNKS -> MDFNFDTVTPCSTMSSYYNFKMA
FT (in isoform 1, isoform C, isoform O and isoform R)"
FT /evidence="ECO:0000305"
FT /id="VSP_005881"
FT VAR_SEQ 1..25
FT /note="MYGNNNPGSNNNNGGYPPYGYNNKS -> MDFNFDTVTPCSTMSSYYNFKMA
FT RNGIDSSY (in isoform V)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_040526"
FT VAR_SEQ 26..48
FT /note="SGGRGFGMSHSLPSGMSRYAFSP -> RHIFFHSPERSSHHYHRKAKDTH
FT (in isoform CM1)"
FT /evidence="ECO:0000303|PubMed:3144435"
FT /id="VSP_005882"
FT VAR_SEQ 27..42
FT /note="GGRGFGMSHSLPSGMS -> PERSSHHYHRKAKDTH (in isoform K)"
FT /evidence="ECO:0000305"
FT /id="VSP_019289"
FT VAR_SEQ 42..49
FT /note="Missing (in isoform A, isoform C, isoform G, isoform
FT W, isoform MS11, isoform O and isoform R)"
FT /evidence="ECO:0000303|PubMed:1710769, ECO:0000303|Ref.5"
FT /id="VSP_005883"
FT VAR_SEQ 43..354
FT /note="Missing (in isoform K)"
FT /evidence="ECO:0000305"
FT /id="VSP_019290"
FT VAR_SEQ 49..354
FT /note="Missing (in isoform CM1)"
FT /evidence="ECO:0000303|PubMed:3144435"
FT /id="VSP_005884"
FT VAR_SEQ 332..354
FT /note="GRSIKSQQRFQNSHPYFDAKKFI -> DGAMEKLRSLFDAICDAIFGLDSEN
FT FADLLDGLYRRKYHYPYL (in isoform MS11 and isoform O)"
FT /evidence="ECO:0000303|PubMed:1710769"
FT /id="VSP_005885"
FT VAR_SEQ 333..354
FT /note="RSIKSQQRFQNSHPYFDAKKFI -> ENFADLLDGLYRRKYHYPYL (in
FT isoform W, isoform MS16 and isoform R)"
FT /evidence="ECO:0000303|PubMed:1710769, ECO:0000303|Ref.5"
FT /id="VSP_005886"
FT CONFLICT 93
FT /note="P -> S (in Ref. 2; AAA28921)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="S -> G (in Ref. 2; AAA28921 and 5; ACY56908/
FT ADD20766)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="N -> K (in Ref. 5; ACY56908)"
FT /evidence="ECO:0000305"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1B7F"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:1B7F"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1B7F"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1B7F"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:1B7F"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:1B7F"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:4QQB"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1B7F"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:1B7F"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1B7F"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:1B7F"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1B7F"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:1B7F"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1B7F"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:1B7F"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:1B7F"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1B7F"
FT CONFLICT P19339-2:15
FT /note="S -> C (in Ref. 6; AAB21845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 38549 MW; 4E443D3BC88B134E CRC64;
MYGNNNPGSN NNNGGYPPYG YNNKSSGGRG FGMSHSLPSG MSRYAFSPQD TEFSFPSSSS
RRGYNDFPGC GGSGGNGGSA NNLGGGNMCH LPPMASNNSL NNLCGLSLGS GGSDDLMNDP
RASNTNLIVN YLPQDMTDRE LYALFRAIGP INTCRIMRDY KTGYSFGYAF VDFTSEMDSQ
RAIKVLNGIT VRNKRLKVSY ARPGGESIKD TNLYVTNLPR TITDDQLDTI FGKYGSIVQK
NILRDKLTGR PRGVAFVRYN KREEAQEAIS ALNNVIPEGG SQPLSVRLAE EHGKAKAAHF
MSQMGVVPAN VPPPPPQPPA HMAAAFNMMH RGRSIKSQQR FQNSHPYFDA KKFI
