ID   THOC5_XENTR             Reviewed;         678 AA.
AC   Q28DG8;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=THO complex subunit 5 homolog;
GN   Name=thoc5; ORFNames=TEgg015p03.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as component of the THO subcomplex of the TREX complex
CC       which is thought to couple mRNA transcription, processing and nuclear
CC       export, and which specifically associates with spliced mRNA and not
CC       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 via the TAP/NFX1 pathway (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: May be involved in cell differentiation. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the THO subcomplex of the transcription/export
CC       (TREX) complex which seems to have a dynamic structure involving ATP-
CC       dependent remodeling. Interacts with thoc7 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC       {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shuttles between nucleus
CC       and cytoplasm. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the THOC5 family. {ECO:0000305}.
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DR   EMBL; CR855522; CAJ82162.1; -; mRNA.
DR   RefSeq; NP_001016827.1; NM_001016827.2.
DR   AlphaFoldDB; Q28DG8; -.
DR   SMR; Q28DG8; -.
DR   STRING; 8364.ENSXETP00000035835; -.
DR   PaxDb; Q28DG8; -.
DR   GeneID; 549581; -.
DR   KEGG; xtr:549581; -.
DR   CTD; 8563; -.
DR   Xenbase; XB-GENE-1015168; thoc5.
DR   eggNOG; KOG2216; Eukaryota.
DR   HOGENOM; CLU_023759_0_0_1; -.
DR   InParanoid; Q28DG8; -.
DR   OrthoDB; 1048314at2759; -.
DR   Reactome; R-XTR-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-XTR-72187; mRNA 3'-end processing.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0000445; C:THO complex part of transcription export complex; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR019163; THO_Thoc5.
DR   PANTHER; PTHR13375; PTHR13375; 1.
DR   Pfam; PF09766; FmiP_Thoc5; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Differentiation; mRNA processing; mRNA splicing; mRNA transport;
KW   Nucleus; Reference proteome; RNA-binding; Transport.
FT   CHAIN           1..678
FT                   /note="THO complex subunit 5 homolog"
FT                   /id="PRO_0000310561"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           7..10
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        312..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   678 AA;  78129 MW;  E12C7AEEEB4D5123 CRC64;
     MSSDSLKKRK PKVNRNEDGK RGRHDEQEGR YYSEEAEVDV RDPREDYQLY KDTCLDLQRL
     MSEIQDLKNK GGKDSAMEIE EKKVQSCVHF MTLKKLNRLA HIRLKKARDQ THEAKQKVDA
     YHLQLQNLLY EVMHLQKEIT KCLEFKSKHE EIELVSVEEF YSEAPATISK PEITSTDSHQ
     QTLSRLDWEL EQRKRLAEKY KECLASKEKI LKEIEIKKEY LNSLQPQLNS IMQASLPVQE
     YLSMPFDCMH KQYETARHLP PPLYVLFVQA SAYSQACDRK LVVTIEGNVE EARALFKPPE
     DSQDDESDSD AEEEQTTKRR RPTLGVQLDD KRKEMLKRHP LCVTLTLKCK EGSTLNLTFY
     FLMNLNILTV KVKIQPALEL STAISAGDLL NPDLILSCLY QGDDGKTTPN PANRYQFDKI
     GILSLNDYIS ELGHPYIWVQ TMGGLHFPTD QPQPAVIADN ALSASHMEKT INLLRARLLS
     RLSLHRQFAS LEHGSIPVSL ECQTLFPAKV ISRLTKWNVI TYEDYLALPY TKDVIECGLA
     KETDQYFYLL IERGTAKLNG VVVLNPGYCA VPPVFSLCLN WKGERSSSND DNIRVMESEV
     NVYFKELCGP PPGFQLLTNQ IQRLCMLLDV YLETERHDNS VEGPHEFPPE KICLRLLRGP
     SRTKPFKYNY PQGFFSHR