ID   THO2_SCHPO              Reviewed;        1628 AA.
AC   Q09779; O13884;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 3.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=THO complex subunit 2;
GN   Name=tho2; ORFNames=SPAC1D4.14, SPAC22F3.14c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1406; THR-1408 AND SER-1577,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Component the THO subcomplex of the TREX complex, which
CC       operates in coupling transcription elongation to mRNA export. The THO
CC       complex is recruited to transcribed genes and moves along the gene with
CC       the elongating polymerase during transcription. THO is important for
CC       stabilizing nascent RNA in the RNA polymerase II elongation complex by
CC       preventing formation of DNA:RNA hybrids behind the elongating
CC       polymerase.
CC   -!- SUBUNIT: Component of the THO complex. THO associates with DNA and RNA
CC       in vitro (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the THOC2 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA93223.1; -; Genomic_DNA.
DR   PIR; T38055; T38055.
DR   RefSeq; XP_001713043.1; XM_001712991.2.
DR   AlphaFoldDB; Q09779; -.
DR   SMR; Q09779; -.
DR   BioGRID; 280530; 9.
DR   STRING; 4896.SPAC1D4.14.1; -.
DR   iPTMnet; Q09779; -.
DR   MaxQB; Q09779; -.
DR   PaxDb; Q09779; -.
DR   PRIDE; Q09779; -.
DR   EnsemblFungi; SPAC1D4.14.1; SPAC1D4.14.1:pep; SPAC1D4.14.
DR   PomBase; SPAC1D4.14; tho2.
DR   VEuPathDB; FungiDB:SPAC1D4.14; -.
DR   eggNOG; KOG1874; Eukaryota.
DR   HOGENOM; CLU_000511_1_1_1; -.
DR   InParanoid; Q09779; -.
DR   OMA; PEIAFWI; -.
DR   PhylomeDB; Q09779; -.
DR   Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-SPO-72187; mRNA 3'-end processing.
DR   PRO; PR:Q09779; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000445; C:THO complex part of transcription export complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; ISO:PomBase.
DR   GO; GO:0003729; F:mRNA binding; ISO:PomBase.
DR   GO; GO:0031124; P:mRNA 3'-end processing; ISO:PomBase.
DR   GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:PomBase.
DR   InterPro; IPR009818; Ataxin-2_C.
DR   InterPro; IPR040007; Tho2.
DR   InterPro; IPR021418; THO_THOC2_C.
DR   InterPro; IPR021726; THO_THOC2_N.
DR   InterPro; IPR032302; THOC2_N.
DR   PANTHER; PTHR21597; PTHR21597; 1.
DR   Pfam; PF07145; PAM2; 1.
DR   Pfam; PF11262; Tho2; 1.
DR   Pfam; PF11732; Thoc2; 1.
DR   Pfam; PF16134; THOC2_N; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1628
FT                   /note="THO complex subunit 2"
FT                   /id="PRO_0000116472"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1337..1628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1365..1428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1457..1472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1473..1496
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1497..1527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1528..1549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1550..1564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1578..1628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1406
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         1408
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         1577
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   1628 AA;  188833 MW;  85A30FB43D2CAED0 CRC64;
     MTSLPEKDQQ GEVSVSENQK KLSEEWEPYI DKLVASNRTR DERVESIQEL FQKCVIEEKL
     PVDIFFSIFS LAFERLEEKN TLASYVIDTL WLFDTEWIKN FHEGSHDKAE KRLVSIGKGL
     KEFLPEEWLL SRLDCKFLEN INVVPNGDFL NRKIVRTNTS LLYRQKKFNL LREESEGFSH
     LMINFFDALT CLRNKSLNED YLIVQVNKSI ISTIGAFDLD PNKVLDLILL LFSENLLDSW
     RFFLSILRNS PWGPNKERKF WNQLPDREKE TFLNNLSNAN GIFNFDERFT NTKSIMSQVL
     GHNLQYMYKE DDENLESYFM MVALLIKYNF ISIDNIWAHL SPSDEELGKE LGKYKDKLDE
     QTFKAKGNAL TMAAPLPDDE IEDGETMDGQ KAEAVPEIKK AKPSQKLGLL KSLLSIGDLS
     SSLLILGRYP FLLRAYPELS NLYHKLLHIS ISSIYANYSP LKLLPNDVRE RLKQPKFIPE
     DSRLREITLR PPKEKNLVFS LDPFADRFNK TESEVFYYFE NYDEDIPILR NLTEFYNIAI
     PWLRLSGLAL CHDPVIVTKL CRIGQKCVDN SSESRTLWLD IIRSLLLPLI TLIDVNTGLS
     YELFELLSKF DSSTRYALYG EWSSTSMKKF PELKLQNSIT EKETKGILRR LTKTNVKQFG
     RLLAKVCHSN PCTVFSIALN QIETYDNLVE VVVDSARFIT ALDFDALTFI ILSSFSNEFK
     KRLKSDGTSI AHWLQGLASF CGRVFRRYSS LDCTSIVEYV IKQFKVNQMF DLVILKELLS
     QMTGLQPWTN LSDNQIQGAA GGPVLRQLSL SLIYENPDVV RKSSMRLFNT LQKNGLATQL
     LVLLSQKYST CIYDVTDENS HLKLISSLQD ECSDVLYLLM EFLNMVCSPK SYYKLIPSFE
     QLIQDFHIQP QVAFYLSRYK NLDHSLTGSN TEDAMDIDYE NTSSPNTASN PVWSIDNSVI
     TELLPKQIWD YFSPNFYLTF WKLSLYDVFV PLERYEFERS RAFDQIRQTD AANTFYSRHR
     HDRQKIMQLS NSLQNELKEH INSLESVRKV LQGDCVKWFI PNGVFPNGTR LEHARFNCAR
     YLWTLCIAPR LKMSPHDALY CAKFVKLLHS LGTPNFSTMS FLEILFNSQL PSFIFSMTQR
     EADNFGRFLY EVLYDITSWY RDKILYEREC LANGALPGFR LYWSDEQNDP DLSAVLPYNK
     FVLLFSKWHK YLTSYFESCL LSTEYMHIYN SVIILEKILP CFPLIIESGS ALKRAAERLK
     DEEKREDLKV LALGYFAKLS KKQPEWVSFN SFSGTVRPSN SEKLQRPQQL SVAATSAVDS
     KTASISEEQA KIDKQKVALN PSAPEFVPDS TPSDAVASET DNKNLVENKA VEKRVEARSS
     ANERKQEERR RKTTPEGNRR ALRTRTPTNE DIQRSDSKLR EDQSRDRTPQ SRSFTNENND
     NLRSVSRHTR REPQQAQNLN ARREHESQKS DRWRQNGNVN RNPRVSNNNS TNVSRERSSE
     ANHRTSNDNK RDEVTEGKDK NKRQDISGES NSRQNNAISR AGRSNGSNRG NDSRDADGRR
     STHYASNKRP RSSDSQSPSN LREEDERENS RRRARQDDRR DRDSRQQRDR PRDRTSRSAR
     EEKRRKIQ