THOC3_MOUSE
ID THOC3_MOUSE Reviewed; 351 AA.
AC Q8VE80; Q9CWI8;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=THO complex subunit 3;
DE Short=Tho3;
GN Name=Thoc3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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).
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; AK010668; BAB27103.1; -; mRNA.
DR EMBL; BC019603; AAH19603.1; -; mRNA.
DR CCDS; CCDS26527.1; -.
DR RefSeq; NP_082873.2; NM_028597.3.
DR AlphaFoldDB; Q8VE80; -.
DR SMR; Q8VE80; -.
DR BioGRID; 216177; 3.
DR IntAct; Q8VE80; 1.
DR STRING; 10090.ENSMUSP00000026990; -.
DR iPTMnet; Q8VE80; -.
DR PhosphoSitePlus; Q8VE80; -.
DR EPD; Q8VE80; -.
DR MaxQB; Q8VE80; -.
DR PaxDb; Q8VE80; -.
DR PeptideAtlas; Q8VE80; -.
DR PRIDE; Q8VE80; -.
DR ProteomicsDB; 262918; -.
DR Antibodypedia; 17111; 169 antibodies from 24 providers.
DR DNASU; 73666; -.
DR Ensembl; ENSMUST00000026990; ENSMUSP00000026990; ENSMUSG00000025872.
DR GeneID; 73666; -.
DR KEGG; mmu:73666; -.
DR UCSC; uc007qod.2; mouse.
DR CTD; 84321; -.
DR MGI; MGI:1920916; Thoc3.
DR VEuPathDB; HostDB:ENSMUSG00000025872; -.
DR eggNOG; KOG1407; Eukaryota.
DR GeneTree; ENSGT00940000158129; -.
DR HOGENOM; CLU_045202_0_0_1; -.
DR InParanoid; Q8VE80; -.
DR OMA; YWLAYST; -.
DR OrthoDB; 1014314at2759; -.
DR PhylomeDB; Q8VE80; -.
DR TreeFam; TF314069; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 73666; 30 hits in 75 CRISPR screens.
DR ChiTaRS; Thoc3; mouse.
DR PRO; PR:Q8VE80; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8VE80; protein.
DR Bgee; ENSMUSG00000025872; Expressed in urogenital fold and 264 other tissues.
DR Genevisible; Q8VE80; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
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:0000346; C:transcription export complex; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006406; P:mRNA export from nucleus; ISO:MGI.
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; ISO:MGI.
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_0000051274"
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96J01"
FT CONFLICT 12
FT /note="A -> V (in Ref. 1; BAB27103)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="W -> S (in Ref. 1; BAB27103)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="F -> I (in Ref. 1; BAB27103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 38738 MW; B7250DABE8BA456E CRC64;
MAAPAAVLGP SALGQSGPGS MAPWCSVSSG PSRYVLGMQE 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
