ID   THOC5_DANRE             Reviewed;         684 AA.
AC   Q6NY52; Q7ZV69;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=THO complex subunit 5 homolog;
GN   Name=thoc5; ORFNames=zgc:76912;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2004) 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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC       {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the THOC5 family. {ECO:0000305}.
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DR   EMBL; BC045980; AAH45980.1; -; mRNA.
DR   EMBL; BC066736; AAH66736.1; -; mRNA.
DR   RefSeq; NP_997857.1; NM_212692.1.
DR   AlphaFoldDB; Q6NY52; -.
DR   SMR; Q6NY52; -.
DR   STRING; 7955.ENSDARP00000105284; -.
DR   PaxDb; Q6NY52; -.
DR   GeneID; 325064; -.
DR   KEGG; dre:325064; -.
DR   CTD; 8563; -.
DR   ZFIN; ZDB-GENE-030131-3789; thoc5.
DR   eggNOG; KOG2216; Eukaryota.
DR   InParanoid; Q6NY52; -.
DR   OrthoDB; 1048314at2759; -.
DR   PhylomeDB; Q6NY52; -.
DR   Reactome; R-DRE-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-DRE-72187; mRNA 3'-end processing.
DR   Reactome; R-DRE-73856; RNA Polymerase II Transcription Termination.
DR   PRO; PR:Q6NY52; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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..684
FT                   /note="THO complex subunit 5 homolog"
FT                   /id="PRO_0000310558"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..337
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        318..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        196
FT                   /note="D -> E (in Ref. 1; AAH45980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        553
FT                   /note="K -> E (in Ref. 1; AAH45980)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   684 AA;  77833 MW;  83B3878D7643F9DA CRC64;
     MSSDAVKKRK PKVIRSEAGT PETKRGRAES EQDVRVYNEE VELEGRDPQQ DYTLYKETCA
     ALAKLMSEIQ ELKTSGAKDG SAEIELRRKQ SSIHFITLKK LNRLAHMRLK KGRDQTHEAK
     QRVDVLHLQL QNLLYEVMHL QKEIGKCLEF KSQHEEIELV SEDEFFQDAP AEISRPQVTR
     EDHHQLTLAR LDWELDQRKR LAEQYKTSLS SKEKIQKAIE QKREYLSSLQ PGLHNIMQAS
     LPVQEYLSMP FEHMQKQAEV ARHLPPPLYV LFVQAGAYGQ ACDKNLTVSI RGDVDEAKAL
     SRPPEDSQDD ESDSDAEEEQ QNTKRRRPTV GVQLDDKRKE MLRRHPLSLG IDLKCKDGSV
     LHLYFYYLMN LNILTVKTKV STSVDLSGAI SAGELLNSES LLNCLYASDH GNETPNPANR
     YQFDKVGITT FADYVSDLGH PYVWVQKLSG LQFSSDAAQS ELSGSALSAS HMEKSMKLLR
     GRLQSRLALH KQFSSLEHSI VPVSSECQHL FPAKVVSGLT RWTMMSHQEF TELSFVQHVL
     KAGLVSETDL FFKAVVERGT ARLLAAVVVN PRYPEVTPLF SLSLLWKGER SGRTDDNLRA
     MESEVNVFRA ELQGPRPGLQ LLTNQIQRLC MCLDVYLETE SQVSDGSEGP KEFPREKMCL
     RTARGPSRLK PFKYNHPQGF FSHR