TRA2_DROME
ID TRA2_DROME Reviewed; 264 AA.
AC P19018; A4UZH1; Q0E977; Q9V734;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Transformer-2 sex-determining protein;
GN Name=tra2; Synonyms=tra-2; ORFNames=CG10128;
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] (ISOFORM TMAJ), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=3144434; DOI=10.1016/0092-8674(88)90247-4;
RA Amrein H., Gorman M., Noethiger R.;
RT "The sex-determining gene tra-2 of Drosophila encodes a putative RNA
RT binding protein.";
RL Cell 55:1025-1035(1988).
RN [2]
RP ERRATUM OF PUBMED:3144434.
RA Amrein H., Gorman M., Noethiger R.;
RL Cell 58:420-420(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS TMAJ AND
RP TMIN), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=2120049; DOI=10.1002/j.1460-2075.1990.tb07573.x;
RA Amrein H., Maniatis T., Noethiger R.;
RT "Alternatively spliced transcripts of the sex-determining gene tra-2 of
RT Drosophila encode functional proteins of different size.";
RL EMBO J. 9:3619-3629(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MSTMIN), NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA], ALTERNATIVE SPLICING (ISOFORMS TMAJ; TMIN; MSTMAJ AND MSTMIN),
RP FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Imaginal disk;
RX PubMed=2116360; DOI=10.1101/gad.4.5.789;
RA Mattox W., Palmer M.J., Baker B.S.;
RT "Alternative splicing of the sex determination gene transformer-2 is sex-
RT specific in the germ line but not in the soma.";
RL Genes Dev. 4:789-805(1990).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TMAJ).
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-264 (ISOFORM TMAJ), AND FUNCTION.
RX PubMed=2493992; DOI=10.1016/0092-8674(89)90634-x;
RA Goralski T.J., Edstroem J.-E., Baker B.S.;
RT "The sex determination locus transformer-2 of Drosophila encodes a
RT polypeptide with similarity to RNA binding proteins.";
RL Cell 56:1011-1018(1989).
RN [9]
RP IDENTIFICATION OF A TRA-2 BINDING SITE IN PRE-MRNA.
RX PubMed=1674449; DOI=10.1016/0092-8674(91)90090-l;
RA Hedley M.L., Maniatis T.;
RT "Sex-specific splicing and polyadenylation of dsx pre-mRNA requires a
RT sequence that binds specifically to tra-2 protein in vitro.";
RL Cell 65:579-586(1991).
RN [10]
RP 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 [11]
RP CHARACTERIZATION OF STRUCTURAL DOMAINS, AND MUTAGENESIS.
RX PubMed=8124712; DOI=10.1016/0092-8674(94)90512-6;
RA Amrein H., Hedley M.L., Maniatis T.;
RT "The role of specific protein-RNA and protein-protein interactions in
RT positive and negative control of pre-mRNA splicing by Transformer 2.";
RL Cell 76:735-746(1994).
RN [12]
RP IDENTIFICATION OF A PURINE-RICH ENHANCER IN THE ENHANCER COMPLEX.
RX PubMed=7867927; DOI=10.1101/gad.9.3.284;
RA Lynch K.W., Maniatis T.;
RT "Synergistic interactions between two distinct elements of a regulated
RT splicing enhancer.";
RL Genes Dev. 9:284-293(1995).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; THR-180; SER-212; SER-214
RP AND SER-254, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required for female sex determination in somatic cells and
CC for spermatogenesis in male germ cells. Positive regulator of female-
CC specific splicing and/or polyadenylation of doublesex (dsx) pre-mRNA.
CC Splicing requires an enhancer complex, dsxRE (dsx repeat element: which
CC contains six copies of a 13-nucleotide repeat and a purine-rich
CC enhancer (PRE)). DsxRE is formed through cooperative interactions
CC between tra, tra2 and the sr proteins, and these interactions require
CC both the repeat sequences and PRE. PRE is required for specific binding
CC of tra2 to the dsxRE. Protein-RNA and protein-protein interactions are
CC involved in tra-2 dependent activation and repression of alternative
CC splicing. Together with tra-2, plays a role in switching fru splicing
CC from the male-specific pattern to the female-specific pattern through
CC activation of the female-specific fru 5'-splice site.
CC {ECO:0000269|PubMed:2116360, ECO:0000269|PubMed:2120049,
CC ECO:0000269|PubMed:2493992, ECO:0000269|PubMed:3144434,
CC ECO:0000269|PubMed:9418892}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Tmaj; Synonyms=Major, Mattox-A, A, F, G;
CC IsoId=P19018-1; Sequence=Displayed;
CC Name=Tmin; Synonyms=Minor, Mattox-B, C, D;
CC IsoId=P19018-2; Sequence=VSP_005901;
CC Name=MsTmaj; Synonyms=Mattox-C, E;
CC IsoId=P19018-3; Sequence=VSP_005900;
CC Name=MsTmin; Synonyms=Mattox-D, B;
CC IsoId=P19018-4; Sequence=VSP_005902;
CC -!- TISSUE SPECIFICITY: Isoform Tmaj and isoform Tmin are expressed in
CC males and females. Isoform msTmaj and isoform msTmin are present only
CC in male germ cells. {ECO:0000269|PubMed:2116360,
CC ECO:0000269|PubMed:2120049, ECO:0000269|PubMed:3144434}.
CC -!- DOMAIN: The RS2 (Arg/Ser-rich domain 2) and RNP-CS (ribonucleoprotein
CC consensus sequence) domains are required for both male sterility and
CC female-specific dsx splicing but the RS1 domain is dispensable.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; M23633; AAA28953.1; -; mRNA.
DR EMBL; X57484; CAA40722.1; -; Genomic_DNA.
DR EMBL; M30939; AAA28954.1; -; Genomic_DNA.
DR EMBL; M30939; AAA28955.1; -; Genomic_DNA.
DR EMBL; M30939; AAA28956.1; -; Genomic_DNA.
DR EMBL; M30939; AAA28957.1; -; Genomic_DNA.
DR EMBL; M76381; AAA69686.1; -; mRNA.
DR EMBL; AE013599; AAF58232.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68557.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68559.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68560.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64910.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64911.1; -; Genomic_DNA.
DR EMBL; AY058768; AAL13997.1; -; mRNA.
DR EMBL; J03155; AAA62771.1; -; mRNA.
DR PIR; A32373; A32373.
DR PIR; D35846; D35846.
DR PIR; S12003; A31638.
DR RefSeq; NP_476763.1; NM_057415.3. [P19018-4]
DR RefSeq; NP_476764.1; NM_057416.3. [P19018-1]
DR RefSeq; NP_476765.1; NM_057417.3. [P19018-2]
DR RefSeq; NP_476766.1; NM_057418.2. [P19018-3]
DR RefSeq; NP_599107.1; NM_134280.1. [P19018-2]
DR RefSeq; NP_995834.1; NM_206112.2. [P19018-1]
DR RefSeq; NP_995835.1; NM_206113.2. [P19018-1]
DR AlphaFoldDB; P19018; -.
DR SMR; P19018; -.
DR BioGRID; 62366; 14.
DR DIP; DIP-17430N; -.
DR IntAct; P19018; 3.
DR STRING; 7227.FBpp0088562; -.
DR iPTMnet; P19018; -.
DR PaxDb; P19018; -.
DR EnsemblMetazoa; FBtr0089615; FBpp0088560; FBgn0003742. [P19018-2]
DR EnsemblMetazoa; FBtr0089616; FBpp0088561; FBgn0003742. [P19018-3]
DR EnsemblMetazoa; FBtr0089617; FBpp0088562; FBgn0003742. [P19018-1]
DR EnsemblMetazoa; FBtr0089618; FBpp0088563; FBgn0003742. [P19018-4]
DR EnsemblMetazoa; FBtr0089619; FBpp0088564; FBgn0003742. [P19018-2]
DR EnsemblMetazoa; FBtr0089620; FBpp0088947; FBgn0003742. [P19018-1]
DR EnsemblMetazoa; FBtr0089621; FBpp0088946; FBgn0003742. [P19018-1]
DR GeneID; 36619; -.
DR KEGG; dme:Dmel_CG10128; -.
DR CTD; 36619; -.
DR FlyBase; FBgn0003742; tra2.
DR VEuPathDB; VectorBase:FBgn0003742; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000168616; -.
DR InParanoid; P19018; -.
DR OMA; TNTTQHK; -.
DR PhylomeDB; P19018; -.
DR Reactome; R-DME-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DME-9013422; RHOBTB1 GTPase cycle.
DR BioGRID-ORCS; 36619; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36619; -.
DR PRO; PR:P19018; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003742; Expressed in imaginal disc and 15 other tissues.
DR Genevisible; P19018; DM.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:FlyBase.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030237; P:female sex determination; IMP:UniProtKB.
DR GO; GO:0019101; P:female somatic sex determination; TAS:FlyBase.
DR GO; GO:0019102; P:male somatic sex determination; TAS:FlyBase.
DR GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:FlyBase.
DR GO; GO:0000003; P:reproduction; IMP:UniProtKB.
DR GO; GO:0007530; P:sex determination; NAS:UniProtKB.
DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; NAS:FlyBase.
DR GO; GO:0000245; P:spliceosomal complex assembly; NAS:FlyBase.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation;
KW mRNA processing; mRNA splicing; Phosphoprotein; Reference proteome;
KW RNA-binding; Sexual differentiation; Spermatogenesis.
FT CHAIN 1..264
FT /note="Transformer-2 sex-determining protein"
FT /id="PRO_0000081986"
FT DOMAIN 97..175
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..196
FT /note="Linker"
FT REGION 179..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform MsTmaj)"
FT /evidence="ECO:0000305"
FT /id="VSP_005900"
FT VAR_SEQ 2..39
FT /note="Missing (in isoform Tmin)"
FT /evidence="ECO:0000305"
FT /id="VSP_005901"
FT VAR_SEQ 134..264
FT /note="TQRSRGFCFIYFEKLSDARAAKDSCSGIEVDGRRIRVDFSITQRAHTPTPGV
FT YLGRQPRGKAPRSFSPRRGRRVYHDRSASPYDNYRDRYDYRNDRYDRNLRRSPSRNRYT
FT RNRSYSRSRSPQLRRTSSRY -> INP (in isoform MsTmin)"
FT /evidence="ECO:0000303|PubMed:2116360"
FT /id="VSP_005902"
FT MUTAGEN 11..82
FT /note="Missing: In d2; greatly reduced female-specific DSX
FT splicing."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 49..82
FT /note="Missing: In d1; greatly reduced female-specific DSX
FT splicing. Retains male fertility."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 113..123
FT /note="Missing: In a36; loss of female-specific DSX
FT splicing. Loss of male fertility."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 138
FT /note="R->L: In pm1; loss of female-specific DSX splicing.
FT Loss of male fertility."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 140
FT /note="F->A: In pm2; no female-specific DSX splicing. Some
FT low male fertility."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 151
FT /note="A->V: In ts1; little female-specific DSX splicing.
FT Loss of male fertility and temperature-sensitive
FT phenotype."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 172..264
FT /note="Missing: In d5; loss of female-specific DSX
FT splicing. Loss of male fertility."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 173
FT /note="S->A: In pm3; greatly reduced female-specific DSX
FT splicing. Retains male fertility and temperature-sensitive
FT phenotype."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 173
FT /note="S->F: In a15, loss of female-specific DSX splicing
FT and male fertility."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 173
FT /note="S->T: In pm4; loss of female-specific DSX splicing.
FT Retains male fertility and temperature-sensitive
FT phenotype."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 181
FT /note="P->S: In ts2; temperature-sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 205..264
FT /note="Missing: In d4; loss of female-specific DSX
FT splicing. Greatly reduced male fertility."
FT /evidence="ECO:0000269|PubMed:8124712"
FT MUTAGEN 236..264
FT /note="Missing: In d3; greatly reduced female-specific DSX
FT splicing. Retains male fertility."
FT /evidence="ECO:0000269|PubMed:8124712"
SQ SEQUENCE 264 AA; 31031 MW; 3BECBD694B0817B3 CRC64;
MDREPLSSGR LHCSARYKHK RSASSSSAGT TSSGHKDRRS DYDYCGSRRH QRSSSRRRSR
SRSSSESPPP EPRHRSGRSS RDRERMHKSR EHPQASRCIG VFGLNTNTSQ HKVRELFNKY
GPIERIQMVI DAQTQRSRGF CFIYFEKLSD ARAAKDSCSG IEVDGRRIRV DFSITQRAHT
PTPGVYLGRQ PRGKAPRSFS PRRGRRVYHD RSASPYDNYR DRYDYRNDRY DRNLRRSPSR
NRYTRNRSYS RSRSPQLRRT SSRY
