THOC4_BOVIN
ID THOC4_BOVIN Reviewed; 257 AA.
AC Q3T0I4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=THO complex subunit 4;
DE Short=Tho4;
DE AltName: Full=Ally of AML-1 and LEF-1;
DE AltName: Full=Aly/REF export factor;
DE AltName: Full=Transcriptional coactivator Aly/REF;
DE AltName: Full=bZIP-enhancing factor BEF;
GN Name=ALYREF; Synonyms=ALY, BEF, THOC4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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. TREX recruitment occurs via
CC an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1.
CC The TREX complex is essential for the export of Kaposi's sarcoma-
CC associated herpesvirus (KSHV) intronless mRNAs and infectious virus
CC production; ALYREF/THOC4 mediates the recruitment of the TREX complex
CC to the intronless viral mRNA. Required for TREX complex assembly and
CC for linking DDX39B to the cap-binding complex (CBC). In conjunction
CC with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70
CC mRNA; both proteins enhance the RNA binding activity of NXF1 and are
CC required for NXF1 localization to the nuclear rim. Involved in the
CC nuclear export of intronless mRNA; proposed to be recruited to
CC intronless mRNA by ATP-bound DDX39B. Involved in transcription
CC elongation and genome stability. Involved in mRNA export of C5-
CC methylcytosine (m5C)-containing mRNAs: specifically recognizes and
CC binds m5C mRNAs and mediates their nucleo-cytoplasmic shuttling.
CC {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; in the complex interacts (via C-
CC terminus) directly with DDX39B and interacts directly with THOC1 and
CC THOC2. Found in mRNA splicing-dependent exon junction complexes (EJC).
CC Identified in the spliceosome C complex. Found in a mRNP complex with
CC UPF3A and UPF3B. Interacts with RBM8A, NCBP1, THOC5, LEF1, RUNX1,
CC EIF4A3, RNPS1, SRRM1, IWS1 and EXOSC1. Interacts with RBM15B. Interacts
CC with NXF1; the interaction is direct. {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=Colocalizes with the core EJC,
CC ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles.
CC Travels to the cytoplasm as part of the exon junction complex (EJC)
CC bound to mRNA. Localizes to regions surrounding nuclear speckles known
CC as perispeckles in which TREX complex assembly seems to occur.
CC {ECO:0000250|UniProtKB:Q86V81}.
CC -!- PTM: Arg-50 and Arg-204 are dimethylated, probably to asymmetric
CC dimethylarginine. {ECO:0000250}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ALYREF family. {ECO:0000305}.
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DR EMBL; BC102384; AAI02385.1; -; mRNA.
DR RefSeq; NP_001030494.1; NM_001035417.2.
DR AlphaFoldDB; Q3T0I4; -.
DR BMRB; Q3T0I4; -.
DR SMR; Q3T0I4; -.
DR STRING; 9913.ENSBTAP00000011202; -.
DR PaxDb; Q3T0I4; -.
DR PeptideAtlas; Q3T0I4; -.
DR PRIDE; Q3T0I4; -.
DR Ensembl; ENSBTAT00000011202; ENSBTAP00000011202; ENSBTAG00000008498.
DR GeneID; 537706; -.
DR KEGG; bta:537706; -.
DR CTD; 10189; -.
DR VEuPathDB; HostDB:ENSBTAG00000008498; -.
DR VGNC; VGNC:25855; ALYREF.
DR eggNOG; KOG0533; Eukaryota.
DR GeneTree; ENSGT00410000025615; -.
DR HOGENOM; CLU_052367_0_1_1; -.
DR InParanoid; Q3T0I4; -.
DR OMA; GIARVWF; -.
DR OrthoDB; 1369069at2759; -.
DR TreeFam; TF313312; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000008498; Expressed in spermatocyte and 106 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:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0062153; F:C5-methylcytidine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; 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 Acetylation; Chaperone; Citrullination; Cytoplasm; Methylation;
KW mRNA processing; mRNA splicing; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Spliceosome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT CHAIN 2..257
FT /note="THO complex subunit 4"
FT /id="PRO_0000378578"
FT DOMAIN 106..183
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 16..37
FT /note="Sufficient for RNA-binding, interaction with NXF1-
FT NXT1 heterodimer"
FT /evidence="ECO:0000250"
FT REGION 186..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 38
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O08583"
FT MOD_RES 38
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 58
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 63
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 71
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O08583"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 141
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 197
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O08583"
FT MOD_RES 197
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O08583"
FT MOD_RES 204
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 204
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 204
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O08583"
FT MOD_RES 220
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 235
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
SQ SEQUENCE 257 AA; 26953 MW; BF74C7F08A5C9216 CRC64;
MADKMDMSLD DIIKLNRSQR GGRGGGRGRG RAGSQGGRGG GAQAAARVNR GGGPIRNRPA
IARGAAGGGG RNRPAPYSRP KQLPDKWQHD LFDSGFGGGA GVETGGKLLV SNLDFGVSDA
DIQELFAEFG TLKKAAVHYD RSGRSLGTAD VHFERKADAL KAMKQYNGVP LDGRPMNIQL
VTSQIDTQRR PAQSVNRGGM TRNRGSGGFG GGGGTRRGTR GGSRGRGRGT GRSSKQQLSA
EELDAQLDAY NARMDTS
