ID   THO5A_XENLA             Reviewed;         678 AA.
AC   Q6DFL5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=THO complex subunit 5 homolog A;
GN   Name=thoc5-a;
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=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) 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; BC076720; AAH76720.1; -; mRNA.
DR   RefSeq; NP_001086498.1; NM_001093029.1.
DR   AlphaFoldDB; Q6DFL5; -.
DR   SMR; Q6DFL5; -.
DR   IntAct; Q6DFL5; 1.
DR   MINT; Q6DFL5; -.
DR   DNASU; 446333; -.
DR   GeneID; 446333; -.
DR   KEGG; xla:446333; -.
DR   CTD; 446333; -.
DR   Xenbase; XB-GENE-6251494; thoc5.L.
DR   OMA; WNGCHTS; -.
DR   OrthoDB; 1048314at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 446333; Expressed in gastrula 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 A"
FT                   /id="PRO_0000310559"
FT   REGION          1..35
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;  78145 MW;  AF04036419F4357A CRC64;
     MASDSLKKRK PKVNRNEDVK RGRHEDQEGR YYSEEAEVDV RDPKEDYQLY KDTCLDLQRL
     MSEIQELKSK GSRDSALEIE EKKVQSCVHF MTLKKLNRLA HIRLKKARDQ THEAKQKVDA
     YHLQLQNLLY EVMHLQKEIT KCLEFKSKHE EIELVSVEEF YSKAPVAISK PEITSTDPHQ
     QTLSRLDWEL EQRKRLAEKY KECLASKEKI LKEIEIKKEY LNSLQPQLNS IMQASLPVQE
     YLSMPFDCMH KQYETARHLP APLYVLFVQA SAYSQACDRK LVVTIEGNVE EARALFKPPE
     DSQDDESDSD AEEEQTTKRR RPTLGVQLDD KRKEMLKRHP LCVTITLKCK EGSTLTLTFY
     FLMNLNILTV KVKILPAFEL STAISAGDLL NPDLMLSCLY QGDDGKTTPN PANQYQFDKI
     GILSLSDYIS ELGHPYIWVQ AMGGLHFPTD QPQPAVVADN ALSANHMEKT IKLLRTRLLS
     RLSLHRQFAS LEHGSIPVSL ECQSFFPAKV ISRLTKWNVI TYEDYLALPY TKDVIECGLA
     KETDQYFNLL IERGTAKLNG VVVLNPGYCA VPPVFSLCLN WKGERLSSND DNIRVMESEV
     NVYYKELCGP PPGFQLLTNQ IQRLCMLLDV YLETERHDNS VEGPHEFPPE KICLRLLRGP
     SRTKPFKYNY PQGFFSHR