ID   TRA2B_RAT               Reviewed;         288 AA.
AC   P62997; O15449; Q15815; Q64283;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 146.
DE   RecName: Full=Transformer-2 protein homolog beta {ECO:0000305};
DE            Short=TRA-2 beta;
DE            Short=TRA2-beta;
DE   AltName: Full=RA301;
DE   AltName: Full=Splicing factor, arginine/serine-rich 10;
DE   AltName: Full=Transformer-2 protein homolog B;
GN   Name=Tra2b {ECO:0000312|RGD:619886}; Synonyms=Sfrs10;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=Sprague-Dawley; TISSUE=Astrocyte;
RX   PubMed=7499316; DOI=10.1074/jbc.270.47.28216;
RA   Matsuo N., Ogawa S., Imai Y., Takagi T., Tohyama M., Stern D., Wanaka A.;
RT   "Cloning of a novel RNA binding polypeptide (RA301) induced by
RT   hypoxia/reoxygenation.";
RL   J. Biol. Chem. 270:28216-28222(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH SAFB/SAFB1.
RX   PubMed=9671816; DOI=10.1093/nar/26.15.3542;
RA   Nayler O., Straetling W., Bourquin J.-P., Stagljar I., Lindemann L.,
RA   Jasper H., Hartmann A.M., Fackelmeyer F.O., Ullrich A., Stamm S.;
RT   "SAF-B couples transcription and pre-mRNA splicing to SAR/MAR elements.";
RL   Nucleic Acids Res. 26:3542-3549(1998).
RN   [4]
RP   INTERACTION WITH RBMX.
RX   PubMed=19282290; DOI=10.1074/jbc.m901026200;
RA   Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M.,
RA   Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R.,
RA   Stamm S.;
RT   "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection
RT   by binding to CC(A/C)-rich regions in pre-mRNA.";
RL   J. Biol. Chem. 284:14303-14315(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-4; SER-14; SER-29;
RP   THR-33; SER-95; SER-97; SER-99 AND THR-201, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Sequence-specific RNA-binding protein which participates in
CC       the control of pre-mRNA splicing. Can either activate or suppress exon
CC       inclusion. Acts additively with RBMX to promote exon 7 inclusion of the
CC       survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10.
CC       Alters pre-mRNA splicing patterns by antagonizing the effects of
CC       splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the
CC       SMN exon 7 RNA. Binds to pre-mRNA (By similarity).
CC       {ECO:0000250|UniProtKB:P62995}.
CC   -!- SUBUNIT: Found in a pre-mRNA exonic splicing enhancer (ESE) complex
CC       with TRA2B/SFRS10, SNRNP70, SNRPA1 and SRRM1. Binds to A3 enhancer
CC       proteins SFRS4, SFRS5, SFRS6 and SFRS9. Interacts with CPSF6, RBMY1A1,
CC       RNPS1 and phosphorylated SFRS13A (By similarity). Interacts with RBMX
CC       and SAFB/SAFB1 (PubMed:9671816, PubMed:19282290). Interacts with ILDR1
CC       (via C-terminus) and ILDR2 (By similarity).
CC       {ECO:0000250|UniProtKB:P62995, ECO:0000250|UniProtKB:P62996,
CC       ECO:0000269|PubMed:19282290, ECO:0000269|PubMed:9671816}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62995}.
CC   -!- INDUCTION: Induced by reoxygenation following hypoxia and by exposure
CC       to silica. Repressed by interferon gamma, LPS and TPA.
CC       {ECO:0000269|PubMed:7499316}.
CC   -!- PTM: Phosphorylated in the RS domains. {ECO:0000250|UniProtKB:P62995}.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR   EMBL; D49708; BAA08556.1; -; mRNA.
DR   EMBL; BC070948; AAH70948.1; -; mRNA.
DR   RefSeq; NP_476460.1; NM_057119.1.
DR   AlphaFoldDB; P62997; -.
DR   BMRB; P62997; -.
DR   SMR; P62997; -.
DR   IntAct; P62997; 3.
DR   STRING; 10116.ENSRNOP00000002429; -.
DR   iPTMnet; P62997; -.
DR   PhosphoSitePlus; P62997; -.
DR   SwissPalm; P62997; -.
DR   jPOST; P62997; -.
DR   PaxDb; 10116-ENSRNOP00000002429; -.
DR   Ensembl; ENSRNOT00055008111; ENSRNOP00055006122; ENSRNOG00055005066.
DR   Ensembl; ENSRNOT00060019354; ENSRNOP00060015173; ENSRNOG00060011434.
DR   Ensembl; ENSRNOT00065005485; ENSRNOP00065003999; ENSRNOG00065003758.
DR   GeneID; 117259; -.
DR   KEGG; rno:117259; -.
DR   UCSC; RGD:619886; rat.
DR   AGR; RGD:619886; -.
DR   CTD; 6434; -.
DR   RGD; 619886; Tra2b.
DR   VEuPathDB; HostDB:ENSRNOG00000001783; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_050438_3_0_1; -.
DR   InParanoid; P62997; -.
DR   OrthoDB; 624416at2759; -.
DR   PhylomeDB; P62997; -.
DR   TreeFam; TF106265; -.
DR   Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-RNO-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR   Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR   PRO; PR:P62997; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000001783; Expressed in thymus and 20 other cell types or tissues.
DR   GO; GO:0001673; C:male germ cell nucleus; ISO:RGD.
DR   GO; GO:0005637; C:nuclear inner membrane; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0036002; F:pre-mRNA binding; ISO:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0003723; F:RNA binding; ISO:RGD.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; ISO:RGD.
DR   GO; GO:0021796; P:cerebral cortex regionalization; ISO:RGD.
DR   GO; GO:1990403; P:embryonic brain development; ISO:RGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEP:RGD.
DR   CDD; cd12363; RRM_TRA2; 1.
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   PANTHER; PTHR48034:SF1; TRANSFORMER-2 PROTEIN HOMOLOG BETA; 1.
DR   PANTHER; PTHR48034; TRANSFORMER-2 SEX-DETERMINING PROTEIN-RELATED; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   Genevisible; P62997; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Isopeptide bond; Methylation; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   RNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   CHAIN           2..288
FT                   /note="Transformer-2 protein homolog beta"
FT                   /id="PRO_0000081985"
FT   DOMAIN          118..196
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..230
FT                   /note="Linker"
FT   REGION          196..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..105
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         33
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   MOD_RES         95
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         103
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   MOD_RES         201
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         203
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   MOD_RES         215
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   MOD_RES         237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   MOD_RES         241
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   MOD_RES         241
FT                   /note="Dimethylated arginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   MOD_RES         241
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
FT   CROSSLNK        197
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62995"
SQ   SEQUENCE   288 AA;  33666 MW;  60B310C8BA443E28 CRC64;
     MSDSGEQNYG ERESRSASRS GSAHGSGKSA RHTPARSRSK EDSRRSRSKS RSRSESRSRS
     RRSSRRHYTR SRSRSRSHRR SRSRSYSRDY RRRHSHSHSP MSTRRRHVGN RANPDPNCCL
     GVFGLSLYTT ERDLREVFSK YGPIADVSIV YDQQSRRSRG FAFVYFENVD DAKEAKERAN
     GMELDGRRIR VDFSITKRPH TPTPGIYMGR PTYGSSRRRD YYDRGYDRGY DDRDYYSRSY
     RGGGGGGGGW RAAQDRDQIY RRRSPSPYYS RGGYRSRSRS RSYSPRRY
//