THO4C_ARATH
ID THO4C_ARATH Reviewed; 295 AA.
AC Q94EH8; Q9C7U4; Q9LF77;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=THO complex subunit 4C;
DE AltName: Full=ALYREF homolog 3 {ECO:0000303|PubMed:15299117};
DE Short=AtALY3 {ECO:0000303|PubMed:15299117};
GN Name=ALY3 {ECO:0000303|PubMed:15299117};
GN Synonyms=DIP1 {ECO:0000303|PubMed:11432957}, THO4C;
GN OrderedLocusNames=At1g66260 {ECO:0000312|Araport:AT1G66260};
GN ORFNames=T6J19.1 {ECO:0000312|EMBL:AAG51767.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH PARP1.
RX PubMed=11432957; DOI=10.1093/jxb/52.359.1375;
RA Storozhenko S., Inze D., Van Montagu M., Kushnir S.;
RT "Arabidopsis coactivator ALY-like proteins, DIP1 and DIP2, interact
RT physically with the DNA-binding domain of the Zn-finger poly(ADP-ribose)
RT polymerase.";
RL J. Exp. Bot. 52:1375-1380(2001).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15299117; DOI=10.1104/pp.104.046086;
RA Uhrig J.F., Canto T., Marshall D., MacFarlane S.A.;
RT "Relocalization of nuclear ALY proteins to the cytoplasm by the tomato
RT bushy stunt virus P19 pathogenicity protein.";
RL Plant Physiol. 135:2411-2423(2004).
CC -!- FUNCTION: Export adapter involved in nuclear export of spliced and
CC unspliced mRNA. {ECO:0000269|PubMed:11432957}.
CC -!- SUBUNIT: Interacts with PARP1. {ECO:0000269|PubMed:11432957}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:11432957, ECO:0000269|PubMed:15299117}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15299117}.
CC -!- SIMILARITY: Belongs to the ALYREF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51767.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ278492; CAC01083.1; -; mRNA.
DR EMBL; AC066691; AAG51767.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34486.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34487.1; -; Genomic_DNA.
DR EMBL; AF410310; AAK95296.1; -; mRNA.
DR EMBL; AY149925; AAN31079.1; -; mRNA.
DR PIR; F96687; F96687.
DR RefSeq; NP_001185329.1; NM_001198400.1.
DR RefSeq; NP_564871.1; NM_105297.4.
DR AlphaFoldDB; Q94EH8; -.
DR SMR; Q94EH8; -.
DR BioGRID; 28164; 5.
DR IntAct; Q94EH8; 1.
DR STRING; 3702.AT1G66260.2; -.
DR iPTMnet; Q94EH8; -.
DR PaxDb; Q94EH8; -.
DR PRIDE; Q94EH8; -.
DR ProteomicsDB; 234419; -.
DR EnsemblPlants; AT1G66260.1; AT1G66260.1; AT1G66260.
DR EnsemblPlants; AT1G66260.2; AT1G66260.2; AT1G66260.
DR GeneID; 842943; -.
DR Gramene; AT1G66260.1; AT1G66260.1; AT1G66260.
DR Gramene; AT1G66260.2; AT1G66260.2; AT1G66260.
DR KEGG; ath:AT1G66260; -.
DR Araport; AT1G66260; -.
DR TAIR; locus:2205293; AT1G66260.
DR eggNOG; KOG0533; Eukaryota.
DR HOGENOM; CLU_052367_0_0_1; -.
DR InParanoid; Q94EH8; -.
DR OMA; GMPISAR; -.
DR OrthoDB; 1369069at2759; -.
DR PhylomeDB; Q94EH8; -.
DR PRO; PR:Q94EH8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94EH8; baseline and differential.
DR Genevisible; Q94EH8; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IMP:TAIR.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR025715; FoP_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF13865; FoP_duplication; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM01218; FoP_duplication; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; mRNA transport; Nucleus; Reference proteome; RNA-binding;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6NQ72"
FT CHAIN 2..295
FT /note="THO complex subunit 4C"
FT /id="PRO_0000425587"
FT DOMAIN 107..184
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NQ72"
FT CONFLICT 231..238
FT /note="RLPLQQNQ -> HLPLQHSH (in Ref. 1; CAC01083)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="R -> I (in Ref. 1; CAC01083)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="R -> I (in Ref. 1; CAC01083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 31318 MW; E823691E82F3365B CRC64;
MSDALNMTLD EIVKKSKSER SAAARSGGKG VSRKSGRGRG GPNGVVGGGR GGGPVRRGPL
AVNTRPSSSF SINKLARRKR SLPWQNQNDL YEETLRAVGV SGVEVGTTVY ITNLDQGVTN
EDIRELYAEI GELKRYAIHY DKNGRPSGSA EVVYMRRSDA IQAMRKYNNV LLDGRPMKLE
ILGGNTESAP VAARVNVTGL NGRMKRSVFI GQGVRGGRVG RGRGSGPSGR RLPLQQNQQG
GVTAGRGGFR GRGRGNGGGR GNKSGGRGGK KPVEKSAADL DKDLESYHAE AMNIS