LRP1C_ARATH
ID LRP1C_ARATH Reviewed; 523 AA.
AC Q94K80; O65626;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=La-related protein 1C;
DE Short=AtLARP1c;
GN Name=LARP1C; OrderedLocusNames=At4g35890; ORFNames=T19K4.20;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP 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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=22965746; DOI=10.1007/s10059-012-0111-5;
RA Zhang B., Jia J., Yang M., Yan C., Han Y.;
RT "Overexpression of a LAM domain containing RNA-binding protein LARP1c
RT induces precocious leaf senescence in Arabidopsis.";
RL Mol. Cells 34:367-374(2012).
CC -!- FUNCTION: Promotes leaf senescence mediated by abscisic acid (ABA),
CC salicylic acid (SA) and jasmonic acid (MeJA), probably though the
CC induction of expression of senescence-associated genes (SAGs) and
CC defense-related genes. {ECO:0000269|PubMed:22965746}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22965746}.
CC Note=Present in cytoplasmic foci.
CC -!- TISSUE SPECIFICITY: Age-dependent accumulation in rosette leaves.
CC {ECO:0000269|PubMed:22965746}.
CC -!- DISRUPTION PHENOTYPE: Impaired abscisic acid- (ABA)-, salicylic
CC acid- (SA)- and jasmonic acid- (MeJA)-induced leaf senescence in
CC detached leaves. {ECO:0000269|PubMed:22965746}.
CC -!- SIMILARITY: Belongs to the LARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18483.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA21475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81498.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022373; CAA18483.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL031986; CAA21475.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161588; CAB81498.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86585.1; -; Genomic_DNA.
DR EMBL; AF370207; AAK44022.1; -; mRNA.
DR EMBL; AY133869; AAM91803.1; -; mRNA.
DR PIR; T04699; T04699.
DR RefSeq; NP_567991.1; NM_119755.3.
DR AlphaFoldDB; Q94K80; -.
DR SMR; Q94K80; -.
DR STRING; 3702.AT4G35890.1; -.
DR iPTMnet; Q94K80; -.
DR PaxDb; Q94K80; -.
DR PRIDE; Q94K80; -.
DR ProteomicsDB; 238613; -.
DR EnsemblPlants; AT4G35890.1; AT4G35890.1; AT4G35890.
DR GeneID; 829743; -.
DR Gramene; AT4G35890.1; AT4G35890.1; AT4G35890.
DR KEGG; ath:AT4G35890; -.
DR Araport; AT4G35890; -.
DR TAIR; locus:2125334; AT4G35890.
DR eggNOG; KOG2590; Eukaryota.
DR HOGENOM; CLU_026607_1_0_1; -.
DR InParanoid; Q94K80; -.
DR OMA; QFQSVGL; -.
DR OrthoDB; 1153108at2759; -.
DR PhylomeDB; Q94K80; -.
DR PRO; PR:Q94K80; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94K80; baseline and differential.
DR Genevisible; Q94K80; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
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; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Acetylation; Cytoplasm;
KW Jasmonic acid signaling pathway; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..523
FT /note="La-related protein 1C"
FT /id="PRO_0000428668"
FT DOMAIN 363..452
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 523 AA; 55838 MW; 4684BF6C59653E48 CRC64;
MASATSNNPA SSSMSPRRIS GNHGSPTASV AQSPRRPSRQ VSSPWTQIVR GESEPIAAAA
AVAGPSSPQS RAPIEPIASV SVAAPTAAVL TVEAAAGDEK SEASGGQDNA GKKPVWKRPS
NGASEVGPVM GASSWPALSE TTKAPSNKSS SDSLKSLGDV PSSSSASSSV PVTQGIANAS
VPAPKQAGRA NPNPTPNHSR QRSFKQRNGA SGSANGTVSQ PSAQGSFTEL PSHNPSPRGQ
NQKNGFASQN HGGTENPSQR DSYRNQNGNH HQSHGGRRNQ EHGNQNWTFQ RSFNGREGNA
QSQRGTPAFV RHPSPTVQPI PQFMAAQPFP SHIPFPTELA QSSYYPRMPY MTPIPHGPQF
FYHYQDPPLH MKLHKQIQYY FSDENLITDI YLRGFMNNEG FVPLRVVAGF KKVAELTDNI
QQIVEALQNS PHVEVQGDFI RKRDNWQNWV LRRNPTGSGP QSVDRADAVA KRLGNLSVDQ
SSADPIGGSS SQLQPTEALS DDQQQSSSTA PVSNHNAPDG ANR
