THOC4_TAEGU
ID THOC4_TAEGU Reviewed; 254 AA.
AC B5FXN8; B5FXP4; B5FXP5; B5FXP6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=THO complex subunit 4;
DE Short=Tho4;
DE AltName: Full=Aly/REF export factor;
GN Name=ALYREF; Synonyms=THOC4;
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=17018643; DOI=10.1073/pnas.0607098103;
RA Wada K., Howard J.T., McConnell P., Whitney O., Lints T., Rivas M.V.,
RA Horita H., Patterson M.A., White S.A., Scharff C., Haesler S., Zhao S.,
RA Sakaguchi H., Hagiwara M., Shiraki T., Hirozane-Kishikawa T., Skene P.,
RA Hayashizaki Y., Carninci P., Jarvis E.D.;
RT "A molecular neuroethological approach for identifying and characterizing a
RT cascade of behaviorally regulated genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15212-15217(2006).
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. TREX recruitment occurs via
CC an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1.
CC Required for TREX complex assembly and for linking DDX39B to the cap-
CC binding complex (CBC). In conjunction with THOC5 functions in NXF1-NXT1
CC mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA
CC binding activity of NXF1 and are required for NXF1 localization to the
CC nuclear rim. Involved in the nuclear export of intronless mRNA;
CC proposed to be recruited to intronless mRNA by ATP-bound DDX39B.
CC Involved in transcription elongation and genome stability (By
CC 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: Homomultimer. Is part of several complexes involved in mRNA
CC processing and export. Component of the transcription/export (TREX)
CC complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP
CC and the THO subcomplex; TREX seems to have a dynamic structure
CC involving ATP-dependent remodeling (By similarity).
CC {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; DQ213511; ACH43799.1; -; mRNA.
DR EMBL; DQ213512; ACH43800.1; -; mRNA.
DR EMBL; DQ213513; ACH43801.1; -; mRNA.
DR EMBL; DQ213514; ACH43802.1; -; mRNA.
DR EMBL; DQ213516; ACH43804.1; -; mRNA.
DR EMBL; DQ213517; ACH43805.1; -; mRNA.
DR EMBL; DQ213518; ACH43806.1; -; mRNA.
DR EMBL; DQ213519; ACH43807.1; -; mRNA.
DR EMBL; DQ213520; ACH43808.1; -; mRNA.
DR RefSeq; NP_001232343.1; NM_001245414.1.
DR AlphaFoldDB; B5FXN8; -.
DR BMRB; B5FXN8; -.
DR SMR; B5FXN8; -.
DR STRING; 59729.ENSTGUP00000003623; -.
DR PRIDE; B5FXN8; -.
DR Ensembl; ENSTGUT00000003662; ENSTGUP00000003623; ENSTGUG00000003513.
DR GeneID; 100190053; -.
DR KEGG; tgu:100190053; -.
DR CTD; 10189; -.
DR GeneTree; ENSGT00410000025615; -.
DR InParanoid; B5FXN8; -.
DR OrthoDB; 1369069at2759; -.
DR Proteomes; UP000007754; Chromosome 18.
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..254
FT /note="THO complex subunit 4"
FT /id="PRO_0000378579"
FT DOMAIN 103..180
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 12..13
FT /note="II -> FL (in Ref. 1; ACH43805)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="E -> Y (in Ref. 1; ACH43806)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="S -> F (in Ref. 1; ACH43805/ACH43807/ACH43808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 26763 MW; 306DBF2B75B69033 CRC64;
MADKMDMSLD DIIKLNRSQR GASRGGRGGR GRGGTARGGG PGRGGVGGGR AGGGPVRNRP
VMARGGGRNR PAPYSRPKQL PEKWQHDLFD SGFGAGAGVE TGGKLLVSNL DFGVSDADIQ
ELFAEFGTLK KAAVHYDRSG RSLGTADVHF ERKADALKAM KQYNGVPLDG RPMNIQLVTS
QIDTQRRPAQ SVNRGGMTRN RGVLGGFGGG GNRRGTRGGN RGRGRGAGRT SKQQLSAEEL
DAQLDAYNAR MDTS
