THOC3_BOVIN
ID THOC3_BOVIN Reviewed; 351 AA.
AC Q29RH4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=THO complex subunit 3;
DE Short=Tho3;
GN Name=THOC3;
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 (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for efficient export of polyadenylated RNA and
CC spliced mRNA. Acts as component of the THO subcomplex of the TREX
CC complex which is thought to couple mRNA transcription, processing and
CC nuclear export, and which specifically associates with spliced mRNA and
CC not 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 -!- 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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus speckle
CC {ECO:0000305}.
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DR EMBL; BC114172; AAI14173.1; -; mRNA.
DR RefSeq; NP_001039765.1; NM_001046300.2.
DR AlphaFoldDB; Q29RH4; -.
DR SMR; Q29RH4; -.
DR STRING; 9913.ENSBTAP00000046521; -.
DR PRIDE; Q29RH4; -.
DR Ensembl; ENSBTAT00000049661; ENSBTAP00000046521; ENSBTAG00000035174.
DR GeneID; 529231; -.
DR KEGG; bta:529231; -.
DR CTD; 84321; -.
DR VEuPathDB; HostDB:ENSBTAG00000035174; -.
DR VGNC; VGNC:58351; THOC3.
DR GeneTree; ENSGT00940000158129; -.
DR InParanoid; Q29RH4; -.
DR OMA; YWLAYST; -.
DR OrthoDB; 1014314at2759; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000035174; Expressed in oocyte and 104 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0000445; C:THO complex part of transcription export complex; ISS:UniProtKB.
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 Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR040132; Tex1/THOC3.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22839; PTHR22839; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96J01"
FT CHAIN 2..351
FT /note="THO complex subunit 3"
FT /id="PRO_0000254021"
FT REPEAT 53..94
FT /note="WD 1"
FT REPEAT 97..137
FT /note="WD 2"
FT REPEAT 139..178
FT /note="WD 3"
FT REPEAT 180..221
FT /note="WD 4"
FT REPEAT 222..261
FT /note="WD 5"
FT REPEAT 264..303
FT /note="WD 6"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96J01"
SQ SEQUENCE 351 AA; 38873 MW; 270368CDC3F392FA CRC64;
MAIPQASMGP SSLGQSGPGS MAPWCSVSSG PTRYVLGMQE LFRGHSKTRE FPAHSAKVHS
VAWSCDGRRL ASGSFDKTAS VFLLEKDRLV KENNYRGHGD SVDQLCWHPS NPDLFVTASG
DKTIRIWDVR TTKCIATVNT KGENINICWS PDGQTIAVGN KDDVVTFIDA KTHRSKAEEQ
FKFEVNEISW NNDNNMFFLT NGNGCINILS YPELKPVQSI NAHPSNCICI KFDPMGKYFA
TGSADALVSL WDVDELVCVR CFSRLDWPVR TLSFSHDGKM LASASEDHFI DIAEVETGDK
LWEVQCESPT FTVAWHPKRP LLAFACDDKD GKYDSSREAG TVKLFGLPND S