ID   TRA2_DROVI              Reviewed;         272 AA.
AC   O02008; O02009; Q6LCB6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Transformer-2 sex-determining protein;
GN   Name=tra2; Synonyms=tra-2;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX   PubMed=9111363; DOI=10.1128/mcb.17.5.2908;
RA   Chandler D., McGuffin M.E., Piskur J., Yao J., Baker B.S., Mattox W.;
RT   "Evolutionary conservation of regulatory strategies for the sex
RT   determination factor transformer-2.";
RL   Mol. Cell. Biol. 17:2908-2919(1997).
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 (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=272;
CC         IsoId=O02008-1; Sequence=Displayed;
CC       Name=179;
CC         IsoId=O02008-3; Sequence=VSP_020797;
CC       Name=225;
CC         IsoId=O02008-2; Sequence=VSP_005903;
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       {ECO:0000250}.
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; U72682; AAB58112.1; -; Genomic_DNA.
DR   EMBL; U72682; AAB58113.1; -; Genomic_DNA.
DR   EMBL; U72682; AAB58114.1; -; Genomic_DNA.
DR   RefSeq; XP_002049699.2; XM_002049663.2. [O02008-1]
DR   RefSeq; XP_015029822.1; XM_015174336.1. [O02008-2]
DR   AlphaFoldDB; O02008; -.
DR   SMR; O02008; -.
DR   STRING; 7244.FBpp0236157; -.
DR   PRIDE; O02008; -.
DR   EnsemblMetazoa; FBtr0436703; FBpp0393580; FBgn0015686. [O02008-2]
DR   EnsemblMetazoa; FBtr0444854; FBpp0401163; FBgn0015686. [O02008-1]
DR   GeneID; 6626623; -.
DR   KEGG; dvi:6626623; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Alternative splicing; Developmental protein; Differentiation;
KW   Phosphoprotein; RNA-binding; Sexual differentiation; Spermatogenesis.
FT   CHAIN           1..272
FT                   /note="Transformer-2 sex-determining protein"
FT                   /id="PRO_0000081987"
FT   DOMAIN          105..183
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          21..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..204
FT                   /note="Linker"
FT   COMPBIAS        26..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..267
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..93
FT                   /note="Missing (in isoform 179)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_020797"
FT   VAR_SEQ         3..49
FT                   /note="Missing (in isoform 225)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005903"
SQ   SEQUENCE   272 AA;  31841 MW;  560DDA5DC35B26EE CRC64;
     MSTGLVNARE KEYLHLHRID KHKCSHSSAT SSPSSAASSE SSRTRQRRSD GEVYGSRHNN
     YKSSSQHRRR SRSGSDSPQV RHYSGRTSRD RQRMRQARDH PQASRCIGVF GLNTNTTQQK
     VRELFNKFGP IERIQMVIDA HTHRSRGFCF IYFENLGDAR VAKDACTGME VDGRRIRVDY
     SITQRAHTPT PGVYMGRPSR PLGRRSRERD YSTRDTSRSR RRHRDESSSV SPYDSNRRKY
     RSRHRYDRSR SRTRSYSRSR SPRKPVRVQS RY