THOC7_DROME
ID THOC7_DROME Reviewed; 288 AA.
AC Q8IRJ8; Q1WWD6; Q9W0T8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=THO complex protein 7;
GN Name=thoc7; ORFNames=CG17143;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, AND IDENTIFICATION IN THE
RP THO COMPLEX.
RC TISSUE=Embryo;
RX PubMed=15133499; DOI=10.1038/nsmb759;
RA Rehwinkel J., Herold A., Gari K., Koecher T., Rode M., Ciccarelli F.L.,
RA Wilm M., Izaurralde E.;
RT "Genome-wide analysis of mRNAs regulated by the THO complex in
RT Drosophila.";
RL Nat. Struct. Mol. Biol. 11:558-566(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-287 (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-229; SER-256 AND
RP SER-260, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: The THO complex is required for cell proliferation and for
CC proper export of heat-shock mRNAs under heat stress.
CC {ECO:0000269|PubMed:15133499}.
CC -!- SUBUNIT: Part of the THO complex containing HPR1, THOC2, THOC5, THOC6
CC and THOC7. {ECO:0000269|PubMed:15133499}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6I9Y2}. Nucleus
CC {ECO:0000250|UniProtKB:Q6I9Y2}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q6I9Y2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q8IRJ8-2; Sequence=Displayed;
CC Name=B;
CC IsoId=Q8IRJ8-1; Sequence=VSP_037609;
CC -!- SIMILARITY: Belongs to the THOC7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ22544.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABE01200.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ620302; CAF04325.1; -; mRNA.
DR EMBL; AE014296; AAF47350.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN11424.1; -; Genomic_DNA.
DR EMBL; BT010075; AAQ22544.1; ALT_INIT; mRNA.
DR EMBL; BT024970; ABE01200.1; ALT_FRAME; mRNA.
DR RefSeq; NP_612011.1; NM_138167.1. [Q8IRJ8-1]
DR RefSeq; NP_728489.2; NM_167804.2. [Q8IRJ8-2]
DR AlphaFoldDB; Q8IRJ8; -.
DR SMR; Q8IRJ8; -.
DR BioGRID; 63596; 13.
DR IntAct; Q8IRJ8; 4.
DR STRING; 7227.FBpp0072425; -.
DR iPTMnet; Q8IRJ8; -.
DR PaxDb; Q8IRJ8; -.
DR PRIDE; Q8IRJ8; -.
DR DNASU; 38033; -.
DR EnsemblMetazoa; FBtr0072526; FBpp0072425; FBgn0035110. [Q8IRJ8-2]
DR EnsemblMetazoa; FBtr0072527; FBpp0072426; FBgn0035110. [Q8IRJ8-1]
DR GeneID; 38033; -.
DR KEGG; dme:Dmel_CG17143; -.
DR UCSC; CG17143-RA; d. melanogaster. [Q8IRJ8-2]
DR CTD; 80145; -.
DR FlyBase; FBgn0035110; thoc7.
DR VEuPathDB; VectorBase:FBgn0035110; -.
DR eggNOG; KOG3215; Eukaryota.
DR GeneTree; ENSGT00390000002873; -.
DR InParanoid; Q8IRJ8; -.
DR OMA; WANSKND; -.
DR PhylomeDB; Q8IRJ8; -.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q8IRJ8; -.
DR BioGRID-ORCS; 38033; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38033; -.
DR PRO; PR:Q8IRJ8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035110; Expressed in egg cell and 25 other tissues.
DR Genevisible; Q8IRJ8; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0000347; C:THO complex; IDA:UniProtKB.
DR GO; GO:0000445; C:THO complex part of transcription export complex; IBA:GO_Central.
DR GO; GO:0000346; C:transcription export complex; ISS:FlyBase.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IC:FlyBase.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR InterPro; IPR008501; THOC7/Mft1.
DR Pfam; PF05615; THOC7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..288
FT /note="THO complex protein 7"
FT /id="PRO_0000310759"
FT REGION 196..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..178
FT /evidence="ECO:0000255"
FT COMPBIAS 196..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 25
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15133499"
FT /id="VSP_037609"
SQ SEQUENCE 288 AA; 33052 MW; C4811571DB5C67B4 CRC64;
MSEQCQLRPH SDTLVRKLVE MNDEEIIKQR LLIDGDGTGE DRRIVVLLKQ FLKWASDSLD
SNPIMYDRLM AQFAQCKLTA LKNVQTLQMI AGERDNYTQL VEHHEESIVL AKAEIESSKK
ELITAKQIRK NKMEYDLLAS LIQDQPDRSE TQRHIETIRR EIDDLVQKKL KMERKFQKRR
NDFTLLMYTI HELEQQLDQD SSSSASSSSS DCDARSEPDL DDNGIMEVSD EDDDLNNSTP
TKFDGARGEP KYHSVSTEDS KAMSVEEDTV LELSIDKDEH DVDVAVAN
