LRP1B_ARATH
ID LRP1B_ARATH Reviewed; 452 AA.
AC Q8RWR2; Q9FKX2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=La-related protein 1B;
DE Short=AtLARP1b;
GN Name=LARP1B; OrderedLocusNames=At5g66100; ORFNames=K2A18.18;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(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 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 [5]
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 [6]
RP FUNCTION.
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. {ECO:0000269|PubMed:22965746}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM10313.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN31109.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AED98159.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB10415.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB011474; BAB10415.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98159.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY091765; AAM10313.1; ALT_INIT; mRNA.
DR EMBL; AY149955; AAN31109.1; ALT_INIT; mRNA.
DR RefSeq; NP_201411.2; NM_126008.5.
DR AlphaFoldDB; Q8RWR2; -.
DR SMR; Q8RWR2; -.
DR STRING; 3702.AT5G66100.1; -.
DR iPTMnet; Q8RWR2; -.
DR PaxDb; Q8RWR2; -.
DR PeptideAtlas; Q8RWR2; -.
DR PRIDE; Q8RWR2; -.
DR ProteomicsDB; 238428; -.
DR EnsemblPlants; AT5G66100.1; AT5G66100.1; AT5G66100.
DR GeneID; 836742; -.
DR Gramene; AT5G66100.1; AT5G66100.1; AT5G66100.
DR KEGG; ath:AT5G66100; -.
DR Araport; AT5G66100; -.
DR TAIR; locus:2156912; AT5G66100.
DR eggNOG; KOG2590; Eukaryota.
DR HOGENOM; CLU_026607_1_0_1; -.
DR InParanoid; Q8RWR2; -.
DR OMA; HDMASPV; -.
DR OrthoDB; 1153108at2759; -.
DR PRO; PR:Q8RWR2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RWR2; baseline and differential.
DR Genevisible; Q8RWR2; AT.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0010150; P:leaf senescence; IMP:TAIR.
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 Acetylation; Cytoplasm; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..452
FT /note="La-related protein 1B"
FT /id="PRO_0000428667"
FT DOMAIN 328..417
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT REGION 1..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..445
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"
SQ SEQUENCE 452 AA; 48936 MW; EBA164D9DE6184EE CRC64;
MATTASSAAN SASRFSIDSS ISRSRHGDSS PWLLPSDSHD HPTLSLSQDD PFSAPSVSPP
TGNNSSDYDN ADKKPPPVWN MPSSNSSSDV GPVMGAAESW PALSLSARSS SIKSPSLDAS
KPFPDGSSSS IPPPQATSNT STNANAGSSV SATSSENSAV NNSQRKPFRR NNNTSSSSTS
SNVSNAAPLN TRDQNHSQRG GGSFGSGNFR NSQRNRNSSS YPRGEGLHHG NRRNYEHGNQ
SGFSHRNYSG RDMHLQPQRG VGMIRPQMLM GPPSFPASSA QYMAAPQLGS YGGPIIYPDY
AQHVFMPHPS PDPMGLVGPF PLQPMYFRNF DAILYNKILT QVEYYFSADN LSRDEHLRDQ
MNDEGWVPVR VIAAFRRLAE LTNNIQTILE ALRSSEVVEI QGETLRRRGD WDKYLLPREP
SRSGPAAGAS NNASLVSQIE SMTLSERSRE GV
