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TRSF_DROME
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   03-AUG-2022, entry version 152.
DE   RecName: Full=Female-specific protein transformer;
GN   Name=tra; ORFNames=CG16724;
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 [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   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).
CC   -!- FUNCTION: Member of the regulatory pathway controlling female somatic
CC       sexual differentiation, regulated by Sxl. Activates dsx female-specific
CC       splicing by promoting the formation of a splicing enhancer complex
CC       which consists of tra, tra2 and sr proteins. Together with tra-2, plays
CC       a role in switching fru splicing from the male-specific pattern to the
CC       female-specific pattern through activation of the female-specific fru
CC       5'-splice site. No known function in males.
CC       {ECO:0000269|PubMed:2441872, ECO:0000269|PubMed:9418892}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:1655279}.
CC       Note=Speckled subnuclear compartment.
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.
CC   -!- MISCELLANEOUS: The sexual regulation of tra occurs through a mechanism
CC       of sex-specific alternative RNA splicing. The non-sex-specific RNA
CC       expressed in males is not translated.
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   STRING; 7227.FBpp0075123; -.
DR   PaxDb; P11596; -.
DR   EnsemblMetazoa; FBtr0075364; FBpp0075123; FBgn0003741.
DR   GeneID; 39849; -.
DR   KEGG; dme:Dmel_CG16724; -.
DR   UCSC; CG16724-RA; d. melanogaster.
DR   CTD; 6955; -.
DR   FlyBase; FBgn0003741; tra.
DR   VEuPathDB; VectorBase:FBgn0003741; -.
DR   HOGENOM; CLU_130078_0_0_1; -.
DR   InParanoid; P11596; -.
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 brain and 25 other tissues.
DR   ExpressionAtlas; P11596; baseline and differential.
DR   Genevisible; P11596; DM.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0036002; F:pre-mRNA binding; IDA:FlyBase.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:1990399; P:epithelium regeneration; IMP:FlyBase.
DR   GO; GO:0030237; P:female sex determination; IMP:FlyBase.
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..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..128
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..176
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
 
 
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