THOC7_MOUSE
ID THOC7_MOUSE Reviewed; 204 AA.
AC Q7TMY4; Q3UIA6; Q80VT4; Q9CQ50;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=THO complex subunit 7 homolog;
DE AltName: Full=Ngg1-interacting factor 3-like protein 1-binding protein 1;
GN Name=Thoc7; Synonyms=Nif3l1bp1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Kidney, Liver, and Pancreas;
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] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II, and FVB/N; TISSUE=Brain, and 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).
RN [3]
RP PROTEIN SEQUENCE OF 27-32, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION (ISOFORMS 1 AND 2), INTERACTION WITH NIF3L1, AND TISSUE
RP SPECIFICITY.
RX PubMed=12951069; DOI=10.1016/j.bbrc.2003.07.008;
RA Tascou S., Kang T.W., Trappe R., Engel W., Burfeind P.;
RT "Identification and characterization of NIF3L1 BP1, a novel cytoplasmic
RT interaction partner of the NIF3L1 protein.";
RL Biochem. Biophys. Res. Commun. 309:440-448(2003).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=16465402;
RA Giuffrida V., Pezzino F.M., Romano F., Litrico L., Garofalo M.R.,
RA Nicotra G., Libra M., D'Amico F., Castrogiovanni P., Imbesi R., Averna M.,
RA Sanfilippo S., D'Agata R., Vicari E., Calogero A.E., Travali S.;
RT "Gene expression in mouse spermatogenesis during ontogenesis.";
RL Int. J. Mol. Med. 17:523-528(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). Interacts
CC with NIF3L1 (PubMed:12951069). Interacts with THOC5 (By similarity).
CC {ECO:0000250|UniProtKB:Q6I9Y2, ECO:0000269|PubMed:12951069}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TMY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TMY4-2; Sequence=VSP_029326;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12951069}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in testis between P3 and
CC P14. Expression in testis increases at P20 and reaches maximum levels
CC in adult. {ECO:0000269|PubMed:16465402}.
CC -!- SIMILARITY: Belongs to the THOC7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH42209.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK005176; BAB23863.1; -; mRNA.
DR EMBL; AK007440; BAB25040.1; -; mRNA.
DR EMBL; AK010958; BAB27291.1; -; mRNA.
DR EMBL; AK147003; BAE27600.1; -; mRNA.
DR EMBL; AK013319; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC042209; AAH42209.1; ALT_INIT; mRNA.
DR EMBL; BC054419; AAH54419.1; -; mRNA.
DR EMBL; BC116919; AAI16920.1; -; mRNA.
DR EMBL; BC116945; AAI16946.1; -; mRNA.
DR EMBL; BF179247; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS49403.1; -. [Q7TMY4-1]
DR RefSeq; NP_001272709.1; NM_001285780.1.
DR RefSeq; NP_079711.1; NM_025435.3. [Q7TMY4-1]
DR AlphaFoldDB; Q7TMY4; -.
DR SMR; Q7TMY4; -.
DR BioGRID; 211313; 1.
DR IntAct; Q7TMY4; 6.
DR MINT; Q7TMY4; -.
DR STRING; 10090.ENSMUSP00000065819; -.
DR iPTMnet; Q7TMY4; -.
DR PhosphoSitePlus; Q7TMY4; -.
DR EPD; Q7TMY4; -.
DR MaxQB; Q7TMY4; -.
DR PaxDb; Q7TMY4; -.
DR PeptideAtlas; Q7TMY4; -.
DR PRIDE; Q7TMY4; -.
DR ProteomicsDB; 262979; -. [Q7TMY4-1]
DR ProteomicsDB; 262980; -. [Q7TMY4-2]
DR Antibodypedia; 46357; 129 antibodies from 23 providers.
DR DNASU; 66231; -.
DR Ensembl; ENSMUST00000065865; ENSMUSP00000065819; ENSMUSG00000053453. [Q7TMY4-1]
DR GeneID; 66231; -.
DR KEGG; mmu:66231; -.
DR UCSC; uc007sge.2; mouse. [Q7TMY4-1]
DR CTD; 80145; -.
DR MGI; MGI:1913481; Thoc7.
DR VEuPathDB; HostDB:ENSMUSG00000053453; -.
DR eggNOG; KOG3215; Eukaryota.
DR GeneTree; ENSGT00390000002873; -.
DR HOGENOM; CLU_087727_0_0_1; -.
DR InParanoid; Q7TMY4; -.
DR OMA; WANSKND; -.
DR OrthoDB; 1394258at2759; -.
DR PhylomeDB; Q7TMY4; -.
DR TreeFam; TF319308; -.
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; 66231; 19 hits in 73 CRISPR screens.
DR ChiTaRS; Thoc7; mouse.
DR PRO; PR:Q7TMY4; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q7TMY4; protein.
DR Bgee; ENSMUSG00000053453; Expressed in ventricular zone and 263 other tissues.
DR ExpressionAtlas; Q7TMY4; baseline and differential.
DR Genevisible; Q7TMY4; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000347; C:THO complex; ISO:MGI.
DR GO; GO:0000445; C:THO complex part of transcription export complex; ISO:MGI.
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 InterPro; IPR008501; THOC7/Mft1.
DR Pfam; PF05615; THOC7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Direct protein sequencing; mRNA processing; mRNA splicing; mRNA transport;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; 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_0000310755"
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..161
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"
FT VAR_SEQ 138..204
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029326"
FT CONFLICT 125
FT /note="V -> M (in Ref. 2; AAH54419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 204 AA; 23715 MW; C6D72609653F1EF8 CRC64;
MGAVTDDEVI RKRLLIDGDG AGDDRRINLL VKSFIKWCNS GSQEEGYSQY QRMLSTLSQC
EFSMGKTLLV YDMNLREMEN YEKIYKEIEC SIAGAHEKIA ECKKQILQAK RIRKNRQEYD
ALAKVIQHHP DRHETLKELE ALGKELEHLS HIKESVEDKL ELRRKQFHVL LSTIHELQQT
LENDDKLSEV DEAQESTMEA DPKP
