THO4A_ARATH
ID THO4A_ARATH Reviewed; 244 AA.
AC Q8L773; Q8LCA6; Q9FJE1;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=THO complex subunit 4A;
DE AltName: Full=ALYREF homolog 1;
DE Short=AtALY1;
GN Name=ALY1; Synonyms=THO4A; OrderedLocusNames=At5g59950; ORFNames=MMN10.26;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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].
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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).
RN [6]
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).
CC -!- FUNCTION: Export adapter involved in nuclear export of spliced and
CC unspliced mRNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15299117}. Nucleus, nucleolus
CC {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=Q8L773-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the ALYREF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08363.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB015475; BAB08363.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97254.1; -; Genomic_DNA.
DR EMBL; AY136433; AAM97099.1; -; mRNA.
DR EMBL; BT000217; AAN15536.1; -; mRNA.
DR EMBL; AY086704; AAM63758.1; -; mRNA.
DR RefSeq; NP_851229.1; NM_180898.3. [Q8L773-1]
DR AlphaFoldDB; Q8L773; -.
DR SMR; Q8L773; -.
DR BioGRID; 21361; 3.
DR STRING; 3702.AT5G59950.5; -.
DR iPTMnet; Q8L773; -.
DR MetOSite; Q8L773; -.
DR PaxDb; Q8L773; -.
DR PRIDE; Q8L773; -.
DR EnsemblPlants; AT5G59950.1; AT5G59950.1; AT5G59950. [Q8L773-1]
DR GeneID; 836117; -.
DR Gramene; AT5G59950.1; AT5G59950.1; AT5G59950. [Q8L773-1]
DR KEGG; ath:AT5G59950; -.
DR Araport; AT5G59950; -.
DR eggNOG; KOG0533; Eukaryota.
DR PhylomeDB; Q8L773; -.
DR PRO; PR:Q8L773; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L773; baseline and differential.
DR Genevisible; Q8L773; AT.
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; IBA:GO_Central.
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;
KW Reference proteome; RNA-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..244
FT /note="THO complex subunit 4A"
FT /id="PRO_0000425585"
FT DOMAIN 88..165
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..244
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 197
FT /note="Missing (in Ref. 4; AAM63758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 25755 MW; 0A035EA0E1FFA5CF CRC64;
MSTGLDMSLD DMIAKNRKSR GGAGPARGTG SGSGPGPTRR NNPNRKSTRS APYQSAKAPE
STWGHDMFSD RSEDHRSGRS SAGIETGTKL YISNLDYGVM NEDIKELFAE VGELKRYTVH
FDRSGRSKGT AEVVYSRRGD ALAAVKKYND VQLDGKPMKI EIVGTNLQTA AAPSGRPANG
NSNGAPWRGG QGRGGQQRGG GRGGGGRGGG GRGRRPGKGP AEKISAEDLD ADLDKYHSGD
METN
