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La-related protein 1A (AtLARP1a)

 LRP1A_ARATH             Reviewed;         826 AA.
Q940X9; Q56WZ6;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-APR-2018, entry version 113.
RecName: Full=La-related protein 1A;
Short=AtLARP1a;
Name=LARP1A; OrderedLocusNames=At5g21160; ORFNames=T10F18.190;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 475-826.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-381, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-381, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=19299548; DOI=10.1261/rna.1478709;
Bousquet-Antonelli C., Deragon J.M.;
"A comprehensive analysis of the La-motif protein superfamily.";
RNA 15:750-764(2009).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[10]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH XRN4, AND SUBCELLULAR
LOCATION.
PubMed=24332370; DOI=10.1016/j.celrep.2013.11.019;
Merret R., Descombin J., Juan Y.T., Favory J.J., Carpentier M.C.,
Chaparro C., Charng Y.Y., Deragon J.M., Bousquet-Antonelli C.;
"XRN4 and LARP1 are required for a heat-triggered mRNA decay pathway
involved in plant acclimation and survival during thermal stress.";
Cell Rep. 5:1279-1293(2013).
-!- FUNCTION: Required for acclimation and survival during thermal
stress. Heat-specific cofactor of XRN4 required for its targeting
to polysomes and subsequent rapid degradation of seedling
transcriptome during the early steps of the heat stress response.
{ECO:0000269|PubMed:24332370}.
-!- SUBUNIT: Interacts with XRN4 and facilitates its attachment to
polysomes upon heat stress. {ECO:0000269|PubMed:24332370}.
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body
{ECO:0000269|PubMed:24332370}. Cytoplasm, cytosol
{ECO:0000269|PubMed:24332370}. Note=Translocates from cytosol to
P-bodies upon heat stress.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q940X9-1; Sequence=Displayed;
-!- DISRUPTION PHENOTYPE: Reduced heat-induced fold reduction of mRNAs
and impaired attachment of XNR4 to polysomes.
{ECO:0000269|PubMed:24332370}.
-!- SIMILARITY: Belongs to the LARP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC140977; AAO73903.1; -; Genomic_DNA.
EMBL; CP002688; AED92941.1; -; Genomic_DNA.
EMBL; AY052365; AAK96556.1; -; mRNA.
EMBL; AY139801; AAM98107.1; -; mRNA.
EMBL; AK221883; BAD94211.1; -; mRNA.
RefSeq; NP_568409.1; NM_122123.3. [Q940X9-1]
UniGene; At.21994; -.
ProteinModelPortal; Q940X9; -.
SMR; Q940X9; -.
BioGrid; 17517; 3.
IntAct; Q940X9; 3.
STRING; 3702.AT5G21160.3; -.
iPTMnet; Q940X9; -.
PaxDb; Q940X9; -.
EnsemblPlants; AT5G21160.1; AT5G21160.1; AT5G21160. [Q940X9-1]
GeneID; 832242; -.
Gramene; AT5G21160.1; AT5G21160.1; AT5G21160. [Q940X9-1]
KEGG; ath:AT5G21160; -.
Araport; AT5G21160; -.
eggNOG; KOG2590; Eukaryota.
eggNOG; COG5193; LUCA.
HOGENOM; HOG000082993; -.
KO; K18757; -.
PhylomeDB; Q940X9; -.
PRO; PR:Q940X9; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q940X9; baseline and differential.
Genevisible; Q940X9; AT.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:0005844; C:polysome; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR006607; DM15.
InterPro; IPR006630; La_HTH.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF05383; La; 1.
SMART; SM00684; DM15; 3.
SMART; SM00715; LA; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS50961; HTH_LA; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Phosphoprotein; Reference proteome; RNA-binding.
CHAIN 1 826 La-related protein 1A.
/FTId=PRO_0000428666.
DOMAIN 272 361 HTH La-type RNA-binding.
{ECO:0000255|PROSITE-ProRule:PRU00332}.
COMPBIAS 58 273 Pro-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19376835}.
MOD_RES 381 381 Phosphoserine.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19376835}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000244|PubMed:19245862}.
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


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