THOC2_ARATH
ID THOC2_ARATH Reviewed; 1823 AA.
AC F4IAT2; Q8GUG8; Q9FXJ7; Q9FXJ8;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=THO complex subunit 2;
DE Short=AtTHO2;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2793;
GN Name=THO2; Synonyms=EMB2793; OrderedLocusNames=At1g24706;
GN ORFNames=F5A9.21/F5A9.22;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-668.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-668.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1646 AND SER-1696, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=20634427; DOI=10.1073/pnas.0911341107;
RA Yelina N.E., Smith L.M., Jones A.M., Patel K., Kelly K.A., Baulcombe D.C.;
RT "Putative Arabidopsis THO/TREX mRNA export complex is involved in transgene
RT and endogenous siRNA biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13948-13953(2010).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=20668032; DOI=10.1261/rna.2265710;
RA Furumizu C., Tsukaya H., Komeda Y.;
RT "Characterization of EMU, the Arabidopsis homolog of the yeast THO complex
RT member HPR1.";
RL RNA 16:1809-1817(2010).
CC -!- FUNCTION: Acts as component of the THO subcomplex of the TREX complex
CC which is thought to couple mRNA transcription, processing and nuclear
CC export. {ECO:0000250}.
CC -!- SUBUNIT: Component of the THO complex, which is composed of THO1, THO2,
CC THO3, THO5, THO6 and THO7. {ECO:0000269|PubMed:20634427}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=F4IAT2-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:20668032}.
CC -!- SIMILARITY: Belongs to the THOC2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG03121.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
CC Sequence=AAG03122.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004133; AAG03121.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004133; AAG03122.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30558.1; -; Genomic_DNA.
DR EMBL; BT002519; AAO00879.1; -; mRNA.
DR EMBL; AK227201; BAE99240.1; -; mRNA.
DR PIR; H86379; H86379.
DR RefSeq; NP_001185086.1; NM_001198157.1. [F4IAT2-1]
DR AlphaFoldDB; F4IAT2; -.
DR SMR; F4IAT2; -.
DR BioGRID; 24318; 26.
DR STRING; 3702.AT1G24706.2; -.
DR iPTMnet; F4IAT2; -.
DR PaxDb; F4IAT2; -.
DR PRIDE; F4IAT2; -.
DR ProteomicsDB; 246423; -. [F4IAT2-1]
DR EnsemblPlants; AT1G24706.2; AT1G24706.2; AT1G24706. [F4IAT2-1]
DR GeneID; 839081; -.
DR Gramene; AT1G24706.2; AT1G24706.2; AT1G24706. [F4IAT2-1]
DR KEGG; ath:AT1G24706; -.
DR Araport; AT1G24706; -.
DR TAIR; locus:2826042; AT1G24706.
DR eggNOG; KOG1874; Eukaryota.
DR InParanoid; F4IAT2; -.
DR OrthoDB; 979205at2759; -.
DR PRO; PR:F4IAT2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IAT2; baseline and differential.
DR Genevisible; F4IAT2; AT.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:TAIR.
DR GO; GO:0035196; P:miRNA processing; IMP:TAIR.
DR GO; GO:1990428; P:miRNA transport; IDA:TAIR.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; PF11262; Tho2; 1.
DR Pfam; PF11732; Thoc2; 1.
DR Pfam; PF16134; THOC2_N; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Transport.
FT CHAIN 1..1823
FT /note="THO complex subunit 2"
FT /id="PRO_0000425583"
FT REGION 1244..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 935..1003
FT /evidence="ECO:0000255"
FT MOTIF 964..969
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1244..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1611
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1729..1748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1772..1786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 1696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 615
FT /note="P -> S (in Ref. 4; AAO00879/BAE99240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1823 AA; 207075 MW; 9C112EB30AF39DAA CRC64;
MSLPLLECKY VTEEFVREGK NGNYGTKLPS SVPMLRFLYE LSWILVRGEL PIQSCKAVLE
GVEFLDKPSR EELASCFADV VTQIAQDLTM SGDQRSRLIK LAKWLVESQT VPQRLFQERC
EEEFLWEADM VKIKAQDLKG KEVRLNTRLL YQQTKFNLLR EESEGYAKLA TLLCRGSASS
SHNASAATMG IIKSLIGHFD LDPNRVFDIV LDCFELEQDY DTFLNLIPIF PKSHASQILG
FKFQYYQRLE VNSPVPVGLY KLTALLVKEE FINLESIYAH LLPKDEEVFE DYNVSSAKRF
EEANKIGKIN LAATGKDLME DEKQGDVTVD LFAALDMESE AVTERLPELE NNQTLGLLNG
FLSVDDWYHA NILFERLAPL NPVAHDQICS GLFRLIEKSI THSYRIARQT RFQSSSSAST
VKLTPTANTT ANRTYLDLPK EVFQMLVTVG PYLYRNTQLL QKICRVLRAY YLSALDLVRD
GSNQEGSAYE VSRGHLKEVR LRVEEALGTC LLPSLQLVPA NPAVGHEIWE VMSLLPYEAR
YRLYGEWEKD DEQNPLLLAA RQVAKLDTRR ILKRLAKENL KQLGRMVAKL AHANPMTVLR
TIVNQIEAYR DMIAPVVDAF KYLTQLEYDI LEYVVIERLA QSGRDKLKDD GINLSDWLQS
LASFWGHLCK KYPSMELRGL FQYLVNQLKR GQGIELVLLQ ELVQQMANVQ YTENLTEDQL
DAMAGSETLR YHATSFGMMR NNKALIKSSN RLRDSLLPND EPKLAIPLLL LIAQHRSLVV
VNADAPYIKM VTEQFDRCHG ILLQYVDFLS SAVSPTTAYA RLVPSLDELV HTYHLEAEVA
FLVFRPVMRL FKCRRNGDVS WPLDSGESMD ADSEISESES SMILDVGTSE KAVTWSDVLD
TVRTMLPSKA WNSLSPDLYA TFWGLTLYDL HVPRNRYESE ISKQHTALKT LEEVADNSSS
AITKRKKEKE RIQESLDRLT GELKKHEEHV ASVRRRLSRE KDTWLSSCPD TLKINMEFLQ
RCIFPRCTFS MADSVYCAMF VNMLHSLGTP FFNTVNHIDV LICKTLQPMI CCCTEYEVGR
LGRFLFETLK IAYHWKSKES VYEHECGNMP GFAVYYRYPN SQRVTFGQFV KVHWKWSGRI
TRLLIQCLES NEYMEIRNAL IMLTKISGVF PVTRKTGINL EKRATKIKND EREDLKVLAT
GVGAALSARK PHWVTDEEFS MGFLELKAPP VHTPKHASSQ NGLLVGVSQG EPTGERATVN
QQPESGGLGK DQMLKTKPLD GRTESIPSKS DQGHLKSKGG NPLDSQPSIS KKSMEQKETD
ETPRISDENP VKPASKYSEA ELKASSKRGA SVNKSAKQDF GKDDGKSGKA IGRTSTADKD
LNYLESRQSG LTKALSSTAA NGSIATGSSK VKDDGAEALD AQKQSSRTVH SPRHEIVTSV
RSSDRLQKRA NAVEDSERIS KRRKGDAEHK EHDSEPRSSD RDRSVEARLD LNKTVTDDQS
THRDQDRSKD KGYERQDRDH RERVDRSDKP RGDDVEKARD KSLERHGRER SVEKGLDKGT
TRSYDRNKDE RNKDDRSKLR HSEASLEKSH PDDHFHSQGL PPPPPLPPNI IPHSMAAKED
LERRAGGARH SQRLSPRHEE REKRRSEENL SVSVDDAKRR RDDDIRDRKR DDRETITVKG
EERERERERE REREKSLPLK EDFEASKRRK LKREQQVPSA EPGEYSPMPH HSSLSTSMGP
SSYEGRERKS SSMIQHGGYL EEPSIRLLGK EASSKMARRD PDPIAKSKSK NSNFLDIALE
SMTVNGKTTR GEQSGSGEIG SRE
