LRP1A_ARATH
ID LRP1A_ARATH Reviewed; 826 AA.
AC Q940X9; Q56WZ6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=La-related protein 1A;
DE Short=AtLARP1a;
GN Name=LARP1A; OrderedLocusNames=At5g21160; ORFNames=T10F18.190;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
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 475-826.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-381, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-381, 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 [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19299548; DOI=10.1261/rna.1478709;
RA Bousquet-Antonelli C., Deragon J.M.;
RT "A comprehensive analysis of the La-motif protein superfamily.";
RL RNA 15:750-764(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [10]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH XRN4, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24332370; DOI=10.1016/j.celrep.2013.11.019;
RA Merret R., Descombin J., Juan Y.T., Favory J.J., Carpentier M.C.,
RA Chaparro C., Charng Y.Y., Deragon J.M., Bousquet-Antonelli C.;
RT "XRN4 and LARP1 are required for a heat-triggered mRNA decay pathway
RT involved in plant acclimation and survival during thermal stress.";
RL Cell Rep. 5:1279-1293(2013).
CC -!- FUNCTION: Required for acclimation and survival during thermal stress.
CC Heat-specific cofactor of XRN4 required for its targeting to polysomes
CC and subsequent rapid degradation of seedling transcriptome during the
CC early steps of the heat stress response. {ECO:0000269|PubMed:24332370}.
CC -!- SUBUNIT: Interacts with XRN4 and facilitates its attachment to
CC polysomes upon heat stress. {ECO:0000269|PubMed:24332370}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:24332370}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:24332370}. Note=Translocates
CC from cytosol to P-bodies upon heat stress.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q940X9-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Reduced heat-induced fold reduction of mRNAs and
CC impaired attachment of XNR4 to polysomes.
CC {ECO:0000269|PubMed:24332370}.
CC -!- SIMILARITY: Belongs to the LARP family. {ECO:0000305}.
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DR EMBL; AC140977; AAO73903.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92941.1; -; Genomic_DNA.
DR EMBL; AY052365; AAK96556.1; -; mRNA.
DR EMBL; AY139801; AAM98107.1; -; mRNA.
DR EMBL; AK221883; BAD94211.1; -; mRNA.
DR RefSeq; NP_568409.1; NM_122123.3. [Q940X9-1]
DR AlphaFoldDB; Q940X9; -.
DR SMR; Q940X9; -.
DR BioGRID; 17517; 3.
DR IntAct; Q940X9; 3.
DR STRING; 3702.AT5G21160.3; -.
DR iPTMnet; Q940X9; -.
DR PaxDb; Q940X9; -.
DR PRIDE; Q940X9; -.
DR EnsemblPlants; AT5G21160.1; AT5G21160.1; AT5G21160. [Q940X9-1]
DR GeneID; 832242; -.
DR Gramene; AT5G21160.1; AT5G21160.1; AT5G21160. [Q940X9-1]
DR KEGG; ath:AT5G21160; -.
DR Araport; AT5G21160; -.
DR eggNOG; KOG2590; Eukaryota.
DR HOGENOM; CLU_336291_0_0_1; -.
DR PhylomeDB; Q940X9; -.
DR PRO; PR:Q940X9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q940X9; baseline and differential.
DR Genevisible; Q940X9; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0005844; C:polysome; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR006607; DM15.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
DR Pfam; PF05383; La; 1.
DR SMART; SM00684; DM15; 3.
DR SMART; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..826
FT /note="La-related protein 1A"
FT /id="PRO_0000428666"
FT DOMAIN 272..361
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..78
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..592
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
SQ SEQUENCE 826 AA; 91377 MW; 8D41922E5B609D9A CRC64;
MMAETEGSVA DDRELITREG GIGTKSPWKT TTSPVETIDA PVMGAHSWPA LADAAQQPRP
KNPPAPAPAP PSKNIPTSIP IPTPAVTGQA KSKGGGKANP GHKNPSGRHS KPGPRSNQNG
PPPPPYLVHA VPYHPPPFPP MVPLPHAAGP DFPYAPYPPY PVPVPPVTES GNEKQVQASP
LPPVLPAPQG DPGKPWPHQR GFDPRNMPQG AGPRNFGRPP FMGPAPGFLV GPGPGFPGPV
YYLPGPPPGA IRGPYPPRFA PYPVNQGPPI LSPEKLDLRD RVLKQVEYYF SDENLENDHY
LISLMDEEGW VPTKIIAGFK RVKAMTMDVD FIVYALGFSN SVEVQGDQIR KRDKWSDWIP
ASKKSTSAET IGDGDKDSPK SITSGDNFGN PSKGSSKPTV SDFSSEGAQS SRTNNYKSGN
LKSSADEKRN VEDLSNDFSN TFLLDEELDL EHRSPRKSGL SMSKSIEYED DDMAVDDQDI
QKLVIVTQNS GKSDGAGIGG TEAKNIPKEL ASTINDGLYY FEQELKKKRS GRRKNNSHLD
TKDGKIKSGE GLNTKLGENS AANDGGEEHG IITSRRKQNK GTHKHHTAHA RRFFSSNIRN
NGNISESPPS SSIGFFFGST PPDSHGPRLS KLSSSPQCTL SGSSPPVGSL PKSFPPFQHP
SHQLLEENGF KQEKYLKYRK RCLNERKKLG SGCSEEMNHL YRFWSYFLRD TFVLSMYDDF
QKFALEDAAG NYDYGLECLF RFYSYGLEKH FDEDLYKDFE KLSLDFYHKG NLYGLEKYWA
FHHYRGKEEP ITKHPELEKL LKEEFRSIDD FRAKETITNQ KENKSH
