ID   THOC7_BOVIN             Reviewed;         204 AA.
AC   Q3SZ60;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=THO complex subunit 7 homolog;
GN   Name=THOC7;
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=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for efficient export of polyadenylated RNA. Acts as
CC       component of the THO subcomplex of the TREX complex which is thought to
CC       couple mRNA transcription, processing and nuclear export, and which
CC       specifically associates with spliced mRNA and not with unspliced pre-
CC       mRNA. TREX is recruited to spliced mRNAs by a transcription-independent
CC       mechanism, binds to mRNA upstream of the exon-junction complex (EJC)
CC       and is recruited in a splicing- and cap-dependent manner to a region
CC       near the 5' end of the mRNA where it functions in mRNA export to the
CC       cytoplasm via the TAP/NFX1 pathway. {ECO:0000250|UniProtKB:Q6I9Y2}.
CC   -!- SUBUNIT: Component of the THO complex, which is composed of THOC1,
CC       THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least
CC       ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the
CC       transcription/export (TREX) complex which seems to have a dynamic
CC       structure involving ATP-dependent remodeling. Interacts with NIF3L1.
CC       Interacts with THOC5. {ECO:0000250|UniProtKB:Q6I9Y2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6I9Y2}. Nucleus
CC       {ECO:0000250|UniProtKB:Q6I9Y2}. Nucleus speckle
CC       {ECO:0000250|UniProtKB:Q6I9Y2}. Note=Interaction with THOC5 is required
CC       for nuclear localization. {ECO:0000250|UniProtKB:Q6I9Y2}.
CC   -!- SIMILARITY: Belongs to the THOC7 family. {ECO:0000305}.
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DR   EMBL; BC103118; AAI03119.1; -; mRNA.
DR   RefSeq; NP_001035604.1; NM_001040514.1.
DR   RefSeq; XP_005217641.1; XM_005217584.3.
DR   AlphaFoldDB; Q3SZ60; -.
DR   SMR; Q3SZ60; -.
DR   STRING; 9913.ENSBTAP00000012008; -.
DR   PaxDb; Q3SZ60; -.
DR   Ensembl; ENSBTAT00000070159; ENSBTAP00000068025; ENSBTAG00000032872.
DR   GeneID; 510250; -.
DR   KEGG; bta:510250; -.
DR   CTD; 80145; -.
DR   VEuPathDB; HostDB:ENSBTAG00000032872; -.
DR   VGNC; VGNC:106977; THOC7.
DR   eggNOG; KOG3215; Eukaryota.
DR   GeneTree; ENSGT00390000002873; -.
DR   HOGENOM; CLU_087727_0_0_1; -.
DR   InParanoid; Q3SZ60; -.
DR   OMA; WANSKND; -.
DR   OrthoDB; 1394258at2759; -.
DR   TreeFam; TF319308; -.
DR   Proteomes; UP000009136; Chromosome 22.
DR   Bgee; ENSBTAG00000032872; Expressed in omasum and 108 other tissues.
DR   ExpressionAtlas; Q3SZ60; baseline and differential.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000445; C:THO complex part of transcription export complex; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; 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:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0046784; P:viral mRNA export from host cell nucleus; IEA:Ensembl.
DR   InterPro; IPR008501; THOC7/Mft1.
DR   Pfam; PF05615; THOC7; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Cytoplasm; mRNA processing; mRNA splicing;
KW   mRNA transport; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q6I9Y2"
FT   CHAIN           2..204
FT                   /note="THO complex subunit 7 homolog"
FT                   /id="PRO_0000310753"
FT   REGION          50..137
FT                   /note="Interaction with THOC5"
FT                   /evidence="ECO:0000250|UniProtKB:Q6I9Y2"
FT   REGION          105..204
FT                   /note="Interaction with NIF3L1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6I9Y2"
FT   REGION          182..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          75..194
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6I9Y2"
FT   MOD_RES         5
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6I9Y2"
FT   MOD_RES         36
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6I9Y2"
SQ   SEQUENCE   204 AA;  23743 MW;  CB0D2608A23E5BFC CRC64;
     MGAVTDDEVI RKRLLIDGDG AGDDRRINLL VKSFIKWCNS GSQEEGYSQY QRMLSTLSQC
     EFSMGKTLLV YDMNLREMEN YEKIYKEIEC SIAGAHEKIA ECKKQILQAK RIRKNRQEYD
     ALAKVIQHHP DRHETLKELE ALGKELEHLS HIKESVEDKL ELRRKQFHVL LSTIHELQQT
     LENDEKLSEV EEAQEASMET DPKP