THO4D_ARATH
ID THO4D_ARATH Reviewed; 288 AA.
AC Q6NQ72; Q9FHP9; Q9LF76;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=THO complex subunit 4D;
DE AltName: Full=ALYREF homolog 4 {ECO:0000303|PubMed:15299117};
DE Short=AtALY4 {ECO:0000303|PubMed:15299117};
GN Name=ALY4 {ECO:0000303|PubMed:15299117};
GN Synonyms=DIP2 {ECO:0000303|PubMed:11432957}, THO4D;
GN OrderedLocusNames=At5g37720; ORFNames=K12B20.19;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
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).
RN [7]
RP INTERACTION WITH EIF4A3.
RX PubMed=19435936; DOI=10.1105/tpc.108.060434;
RA Koroleva O.A., Calder G., Pendle A.F., Kim S.H., Lewandowska D.,
RA Simpson C.G., Jones I.M., Brown J.W.S., Shaw P.J.;
RT "Dynamic behavior of Arabidopsis eIF4A-III, putative core protein of exon
RT junction complex: fast relocation to nucleolus and splicing speckles under
RT hypoxia.";
RL Plant Cell 21:1592-1606(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP FUNCTION.
RX PubMed=24723400; DOI=10.1093/jxb/eru136;
RA Teng W., Zhang H., Wang W., Li D., Wang M., Liu J., Zhang H., Zheng X.,
RA Zhang Z.;
RT "ALY proteins participate in multifaceted Nep1Mo-triggered responses in
RT Nicotiana benthamiana and Arabidopsis thaliana.";
RL J. Exp. Bot. 65:2483-2494(2014).
CC -!- FUNCTION: Export adapter involved in nuclear export of spliced and
CC unspliced mRNA (PubMed:11432957). Plays a role in disease resistance.
CC Mediates multiple defense responses triggered by NEP1, including
CC stomatal closure, hypersensitive cell death (HCD) and defense-related
CC gene expression (PubMed:24723400). {ECO:0000269|PubMed:11432957,
CC ECO:0000269|PubMed:24723400}.
CC -!- SUBUNIT: Interacts with PARP1 (PubMed:11432957). Interacts with EIF4A3
CC (PubMed:19435936). {ECO:0000269|PubMed:11432957,
CC ECO:0000269|PubMed:19435936}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:11432957, ECO:0000269|PubMed:15299117}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15299117}.
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=Q6NQ72-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the ALYREF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08317.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ278493; CAC01084.1; -; mRNA.
DR EMBL; AB018107; BAB08317.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94222.1; -; Genomic_DNA.
DR EMBL; BT010588; AAQ89610.1; -; mRNA.
DR EMBL; AK227931; BAE99901.1; -; mRNA.
DR RefSeq; NP_198588.2; NM_123131.4. [Q6NQ72-1]
DR AlphaFoldDB; Q6NQ72; -.
DR SMR; Q6NQ72; -.
DR BioGRID; 19001; 8.
DR IntAct; Q6NQ72; 1.
DR STRING; 3702.AT5G37720.1; -.
DR iPTMnet; Q6NQ72; -.
DR PaxDb; Q6NQ72; -.
DR PRIDE; Q6NQ72; -.
DR ProteomicsDB; 246458; -. [Q6NQ72-1]
DR EnsemblPlants; AT5G37720.1; AT5G37720.1; AT5G37720. [Q6NQ72-1]
DR GeneID; 833750; -.
DR Gramene; AT5G37720.1; AT5G37720.1; AT5G37720. [Q6NQ72-1]
DR KEGG; ath:AT5G37720; -.
DR Araport; AT5G37720; -.
DR TAIR; locus:2151779; AT5G37720.
DR eggNOG; KOG0533; Eukaryota.
DR InParanoid; Q6NQ72; -.
DR OMA; MSHPNGF; -.
DR PhylomeDB; Q6NQ72; -.
DR PRO; PR:Q6NQ72; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6NQ72; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
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; Alternative splicing; mRNA transport; Nucleus; Plant defense;
KW Reference proteome; RNA-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..288
FT /note="THO complex subunit 4D"
FT /id="PRO_0000425588"
FT DOMAIN 93..170
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 206
FT /note="R -> I (in Ref. 1; CAC01084)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="G -> E (in Ref. 1; CAC01084)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="R -> L (in Ref. 1; CAC01084)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="G -> D (in Ref. 1; CAC01084)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="K -> N (in Ref. 1; CAC01084)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="D -> A (in Ref. 1; CAC01084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 30435 MW; 6542DE6F7E0E4FC2 CRC64;
MSGALNMTLD EIVKRGKTAR SGGRGISRGR GRGRGGGGRG AGPARRGPLA VNARPSSFTI
NKPVRRVRSL PWQSGLFEDG LRAAGASGVE VGTRLHVTNL DQGVTNEDIR ELFSEIGEVE
RYAIHYDKNG RPSGTAEVVY PRRSDAFQAL KKYNNVLLDG RPMRLEILGG NNSSEAPLSG
RVNVNVTGLN GRLKRTVVIQ QGGGGRGRVR GGRGGRGPAP TVSRRLPIHN QQGGGMRGGR
GGFRARGRGN GGRGRGGGRG NGKKPVEKSA ADLDKDLESY HADAMNTS
