THOC3_HUMAN
ID THOC3_HUMAN Reviewed; 351 AA.
AC Q96J01; Q6NZ53;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=THO complex subunit 3;
DE Short=Tho3;
DE AltName: Full=TEX1 homolog;
DE AltName: Full=hTREX45;
GN Name=THOC3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND INTERACTION WITH THE TREX COMPLEX.
RX PubMed=11979277; DOI=10.1038/nature746;
RA Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M.,
RA Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R.,
RA Hurt E.;
RT "TREX is a conserved complex coupling transcription with messenger RNA
RT export.";
RL Nature 417:304-308(2002).
RN [4]
RP IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15833825; DOI=10.1158/0008-5472.can-04-3624;
RA Guo S., Hakimi M.A., Baillat D., Chen X., Farber M.J., Klein-Szanto A.J.,
RA Cooch N.S., Godwin A.K., Shiekhattar R.;
RT "Linking transcriptional elongation and messenger RNA export to metastatic
RT breast cancers.";
RL Cancer Res. 65:3011-3016(2005).
RN [5]
RP IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15998806; DOI=10.1101/gad.1302205;
RA Masuda S., Das R., Cheng H., Hurt E., Dorman N., Reed R.;
RT "Recruitment of the human TREX complex to mRNA during splicing.";
RL Genes Dev. 19:1512-1517(2005).
RN [6]
RP FUNCTION OF THE TREX COMPLEX.
RX PubMed=17190602; DOI=10.1016/j.cell.2006.10.044;
RA Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.;
RT "Human mRNA export machinery recruited to the 5' end of mRNA.";
RL Cell 127:1389-1400(2006).
RN [7]
RP FUNCTION OF THE TREX COMPLEX.
RX PubMed=18974867; DOI=10.1371/journal.ppat.1000194;
RA Boyne J.R., Colgan K.J., Whitehouse A.;
RT "Recruitment of the complete hTREX complex is required for Kaposi's
RT sarcoma-associated herpesvirus intronless mRNA nuclear export and virus
RT replication.";
RL PLoS Pathog. 4:E1000194-E1000194(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP IDENTIFICATION IN THE THO COMPLEX.
RX PubMed=23222130; DOI=10.1093/nar/gks1188;
RA Chi B., Wang Q., Wu G., Tan M., Wang L., Shi M., Chang X., Cheng H.;
RT "Aly and THO are required for assembly of the human TREX complex and
RT association of TREX components with the spliced mRNA.";
RL Nucleic Acids Res. 41:1294-1306(2013).
RN [11] {ECO:0000305}
RP VARIANT PHE-326.
RX PubMed=29120066; DOI=10.1111/cge.13171;
RA Mejecase C., Mohand-Said S., El Shamieh S., Antonio A., Condroyer C.,
RA Blanchard S., Letexier M., Saraiva J.P., Sahel J.A., Audo I., Zeitz C.;
RT "A novel nonsense variant in REEP6 is involved in a sporadic rod-cone
RT dystrophy case.";
RL Clin. Genet. 93:707-711(2018).
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. The
CC TREX complex is essential for the export of Kaposi's sarcoma-associated
CC herpesvirus (KSHV) intronless mRNAs and infectious virus production.
CC {ECO:0000269|PubMed:11979277, ECO:0000269|PubMed:15833825,
CC ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602,
CC ECO:0000269|PubMed:18974867}.
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.
CC {ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806,
CC ECO:0000269|PubMed:23222130}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus speckle
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96J01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96J01-2; Sequence=VSP_056173;
CC -!- CAUTION: There are two almost identical copies of this gene on
CC chromosome 5q35. One copy is frameshifted and unlikely to encode a
CC functional protein. {ECO:0000305}.
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DR EMBL; AC138965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006849; AAH06849.1; -; mRNA.
DR EMBL; BC066325; AAH66325.1; -; mRNA.
DR EMBL; BC068499; AAH68499.1; -; mRNA.
DR CCDS; CCDS4397.1; -. [Q96J01-1]
DR RefSeq; NP_115737.1; NM_032361.3. [Q96J01-1]
DR PDB; 7APK; EM; 3.30 A; C/K/c/k=1-351.
DR PDBsum; 7APK; -.
DR AlphaFoldDB; Q96J01; -.
DR SMR; Q96J01; -.
DR BioGRID; 124047; 63.
DR CORUM; Q96J01; -.
DR IntAct; Q96J01; 30.
DR MINT; Q96J01; -.
DR STRING; 9606.ENSP00000265097; -.
DR iPTMnet; Q96J01; -.
DR PhosphoSitePlus; Q96J01; -.
DR BioMuta; THOC3; -.
DR DMDM; 48474597; -.
DR EPD; Q96J01; -.
DR jPOST; Q96J01; -.
DR MassIVE; Q96J01; -.
DR MaxQB; Q96J01; -.
DR PaxDb; Q96J01; -.
DR PeptideAtlas; Q96J01; -.
DR PRIDE; Q96J01; -.
DR ProteomicsDB; 66791; -.
DR ProteomicsDB; 76881; -. [Q96J01-1]
DR Antibodypedia; 17111; 169 antibodies from 24 providers.
DR DNASU; 84321; -.
DR Ensembl; ENST00000265097.9; ENSP00000265097.5; ENSG00000051596.10. [Q96J01-1]
DR Ensembl; ENST00000513482.1; ENSP00000422243.1; ENSG00000051596.10. [Q96J01-2]
DR GeneID; 84321; -.
DR KEGG; hsa:84321; -.
DR MANE-Select; ENST00000265097.9; ENSP00000265097.5; NM_032361.4; NP_115737.1.
DR UCSC; uc003mdg.6; human. [Q96J01-1]
DR CTD; 84321; -.
DR GeneCards; THOC3; -.
DR HGNC; HGNC:19072; THOC3.
DR HPA; ENSG00000051596; Low tissue specificity.
DR MIM; 606929; gene.
DR neXtProt; NX_Q96J01; -.
DR OpenTargets; ENSG00000051596; -.
DR PharmGKB; PA134893535; -.
DR VEuPathDB; HostDB:ENSG00000051596; -.
DR eggNOG; KOG1407; Eukaryota.
DR GeneTree; ENSGT00940000158129; -.
DR HOGENOM; CLU_045202_0_0_1; -.
DR InParanoid; Q96J01; -.
DR OMA; YWLAYST; -.
DR OrthoDB; 1014314at2759; -.
DR PhylomeDB; Q96J01; -.
DR TreeFam; TF314069; -.
DR PathwayCommons; Q96J01; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q96J01; -.
DR SIGNOR; Q96J01; -.
DR BioGRID-ORCS; 84321; 755 hits in 1012 CRISPR screens.
DR ChiTaRS; THOC3; human.
DR GenomeRNAi; 84321; -.
DR Pharos; Q96J01; Tbio.
DR PRO; PR:Q96J01; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96J01; protein.
DR Bgee; ENSG00000051596; Expressed in lower esophagus mucosa and 101 other tissues.
DR ExpressionAtlas; Q96J01; baseline and differential.
DR Genevisible; Q96J01; HS.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000445; C:THO complex part of transcription export complex; IDA:UniProtKB.
DR GO; GO:0000346; C:transcription export complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..351
FT /note="THO complex subunit 3"
FT /id="PRO_0000051273"
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..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 299..351
FT /note="DKLWEVQCESPTFTVAWHPKRPLLAFACDDKDGKYDSSREAGTVKLFGLPND
FT S -> NFMRIYRLSPLAVRTSLVISSLHVTTSPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056173"
FT VARIANT 326
FT /note="C -> F"
FT /evidence="ECO:0000269|PubMed:29120066"
FT /id="VAR_081223"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 109..131
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:7APK"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:7APK"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:7APK"
SQ SEQUENCE 351 AA; 38772 MW; 9BA03D9D5571E424 CRC64;
MAVPAAAMGP SALGQSGPGS MAPWCSVSSG PSRYVLGMQE LFRGHSKTRE FLAHSAKVHS
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
