ID   THO4B_XENLA             Reviewed;         256 AA.
AC   Q6GLW1;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=THO complex subunit 4-B;
DE            Short=Tho4-B;
DE   AltName: Full=Aly/REF export factor-B;
GN   Name=alyref-b; Synonyms=thoc4-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Export adapter involved in nuclear export of spliced and
CC       unspliced mRNA. Binds mRNA which is thought to be transferred to the
CC       NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway). Component of the
CC       TREX complex which is thought to couple mRNA transcription, processing
CC       and nuclear export, and specifically associates with spliced mRNA and
CC       not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a
CC       transcription-independent mechanism, binds to mRNA upstream of the
CC       exon-junction complex (EJC) and is recruited in a splicing- and cap-
CC       dependent manner to a region near the 5' end of the mRNA where it
CC       functions in mRNA export to the cytoplasm. Involved in the nuclear
CC       export of intronless mRNA. Involved in transcription elongation and
CC       genome stability (By similarity). {ECO:0000250|UniProtKB:Q86V81}.
CC   -!- FUNCTION: Acts as chaperone and promotes the dimerization of
CC       transcription factors containing basic leucine zipper (bZIP) domains
CC       and thereby promotes transcriptional activation.
CC       {ECO:0000250|UniProtKB:Q86V81}.
CC   -!- SUBUNIT: Component of the transcription/export (TREX) complex; TREX
CC       seems to have a dynamic structure involving ATP-dependent remodeling
CC       (By similarity). {ECO:0000250|UniProtKB:Q86V81}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86V81}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:Q86V81}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q86V81}. Note=Travels to the cytoplasm as part
CC       of the exon junction complex (EJC) bound to mRNA.
CC       {ECO:0000250|UniProtKB:Q86V81}.
CC   -!- SIMILARITY: Belongs to the ALYREF family. {ECO:0000305}.
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DR   EMBL; BC074336; AAH74336.1; -; mRNA.
DR   RefSeq; NP_001086215.1; NM_001092746.1.
DR   AlphaFoldDB; Q6GLW1; -.
DR   SMR; Q6GLW1; -.
DR   DNASU; 444644; -.
DR   GeneID; 444644; -.
DR   KEGG; xla:444644; -.
DR   CTD; 444644; -.
DR   OrthoDB; 1369069at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 444644; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0062153; F:C5-methylcytidine-containing RNA binding; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006405; P:RNA export from nucleus; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR025715; FoP_C.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF13865; FoP_duplication; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM01218; FoP_duplication; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Cytoplasm; mRNA processing; mRNA splicing; mRNA transport;
KW   Nucleus; Reference proteome; RNA-binding; Transport.
FT   CHAIN           1..256
FT                   /note="THO complex subunit 4-B"
FT                   /id="PRO_0000378581"
FT   DOMAIN          105..182
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          15..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   256 AA;  27233 MW;  260EFF3FBB2F9B3A CRC64;
     MGDKMDMSLD DIIKLNRSQR TADRGRGRGR GVRGGSARGG AVGRVGGGRG GAAGVGVPMR
     SRPVLSRGGR NRPTPYSRPK QLPDKWQHDL FDSGFGTGAG METGGKLLVS NLDFGVSDAD
     IQELFAEFGS LKKAAVHYDR SGRSLGTADV HFERKADALK AMKQYNGVPL DGRSMNIQLV
     TSQIEAQRRP IQSQSRGGGV ARPRGGAIGF AAGGNRRDRG ANRGRGRGAG RNPKQQLSAE
     ELDAQLDAYN ARMDTS