ID   THO5B_XENLA             Reviewed;         678 AA.
AC   Q7ZXA8;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=THO complex subunit 5 homolog B;
GN   Name=thoc5-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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INTERACTION WITH THOC7.
RX   PubMed=19059247; DOI=10.1016/j.febslet.2008.11.024;
RA   El Bounkari O., Guria A., Klebba-Faerber S., Claussen M., Pieler T.,
RA   Griffiths J.R., Whetton A.D., Koch A., Tamura T.;
RT   "Nuclear localization of the pre-mRNA associating protein THOC7 depends
RT   upon its direct interaction with Fms tyrosine kinase interacting protein
RT   (FMIP).";
RL   FEBS Lett. 583:13-18(2009).
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.
CC       {ECO:0000269|PubMed:19059247}.
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; BC045075; AAH45075.1; -; mRNA.
DR   RefSeq; NP_001080668.1; NM_001087199.1.
DR   AlphaFoldDB; Q7ZXA8; -.
DR   SMR; Q7ZXA8; -.
DR   DNASU; 380360; -.
DR   GeneID; 380360; -.
DR   KEGG; xla:380360; -.
DR   CTD; 380360; -.
DR   Xenbase; XB-GENE-1015173; thoc5.S.
DR   OMA; EAYCDIV; -.
DR   OrthoDB; 1048314at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 380360; Expressed in pancreas and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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   1: Evidence at protein 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 B"
FT                   /id="PRO_0000310560"
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;  77763 MW;  2414F8D2352A64BC CRC64;
     MSSDSLKKRK PKVNRSEDGK RGRHDEQEGR YYSEEAEVDV RDSREDYQLY KDTCVALQRL
     MSEIQDLKSK GSKDSAMEIE EKKIQSCVHF MTLKKLNRLA NIRLKKARDQ THEAKQKVDA
     YNLQLQNLLY EVMHLQKEIT KCLEFKSKHE EIELVSVEEF YSDAPAAISK PEITSTDPHQ
     QTLSRLDWEL EQRKRLAEKY KECLASKEKI LKEIEIKKEY LNTLQPQLNS IMQASLPVQE
     YLSMPFDCMH KQYETARHLP APLYVLFVQA SAYSQACDQK LVVAIEGNVE EARALFKPPE
     DSQDDESDSD AEEEQTTKRR RPTLGVQLDD KRKEMLKRHP LCVTLTLMCK EGSTLTLTFY
     FLMNLNILTV KVKIQPAFEL STAISAGDLL NPDLILGCLY QGDDGKTTPN PANKYQFDKI
     GILSLSDYIS ELGHPYVWAQ TMGGLHFPTD QPQPEFVADN ALSASHMEKT IKLLKTRLLS
     RLSLHRQFAS LEHGSIPVSL ECQSLFPAKV ISRLTKWNVI AYEDYLALPY TKDVVECGLA
     KETDQYFCLL IERGTAKLNG VVVLNPDYSS VPPVFSLCLN WKGERSSSND DNIGVMESEV
     NVYYKELCGP PPGFQLLTNQ IQRLCMLLDV YLETERHDNS VEGPHEFPPE KICLRLLRGP
     SRTKPFKYNY PQGFFSHR