LSM5_ARATH
ID LSM5_ARATH Reviewed; 88 AA.
AC Q9FKB0; Q0WMZ9;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Sm-like protein LSM5 {ECO:0000305};
DE Short=AtLSM5 {ECO:0000303|PubMed:23620288};
DE AltName: Full=Protein SUPERSENSITIVE TO ABA AND DROUGHT 1 {ECO:0000303|PubMed:11740939};
DE Short=AtSAD1 {ECO:0000303|PubMed:11740939};
DE AltName: Full=U6 snRNA-associated Sm-like protein LSM5 {ECO:0000305};
GN Name=LSM5 {ECO:0000303|PubMed:23221597};
GN Synonyms=SAD1 {ECO:0000303|PubMed:11740939};
GN OrderedLocusNames=At5g48870 {ECO:0000312|Araport:AT5G48870};
GN ORFNames=K24G6.21 {ECO:0000312|EMBL:AAK61592.1};
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 [MRNA], FUNCTION, AND MUTAGENESIS OF GLU-12.
RC STRAIN=cv. Columbia;
RX PubMed=11740939; DOI=10.1016/s1534-5807(01)00087-9;
RA Xiong L., Gong Z., Rock C.D., Subramanian S., Guo Y., Xu W., Galbraith D.,
RA Zhu J.K.;
RT "Modulation of abscisic acid signal transduction and biosynthesis by an Sm-
RT like protein in Arabidopsis.";
RL Dev. Cell 1:771-781(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ali K., Tyagi A.;
RT "Isolation and characterization of genes induced under water stress.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=12427994; DOI=10.1104/pp.009480;
RA Hugouvieux V., Murata Y., Young J.J., Kwak J.M., Mackesy D.Z.,
RA Schroeder J.I.;
RT "Localization, ion channel regulation, and genetic interactions during
RT abscisic acid signaling of the nuclear mRNA cap-binding protein, ABH1.";
RL Plant Physiol. 130:1276-1287(2002).
RN [8]
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 [9]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH LSM6A; LSM6B AND
RP LSM7, TISSUE SPECIFICITY, GENE FAMILY, AND DISRUPTION PHENOTYPE.
RX PubMed=23221597; DOI=10.1105/tpc.112.103697;
RA Perea-Resa C., Hernandez-Verdeja T., Lopez-Cobollo R.,
RA del Mar Castellano M., Salinas J.;
RT "LSM proteins provide accurate splicing and decay of selected transcripts
RT to ensure normal Arabidopsis development.";
RL Plant Cell 24:4930-4947(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23620288; DOI=10.1093/nar/gkt296;
RA Golisz A., Sikorski P.J., Kruszka K., Kufel J.;
RT "Arabidopsis thaliana LSM proteins function in mRNA splicing and
RT degradation.";
RL Nucleic Acids Res. 41:6232-6249(2013).
RN [11]
RP FUNCTION.
RX PubMed=24393432; DOI=10.1186/gb-2014-15-1-r1;
RA Cui P., Zhang S., Ding F., Ali S., Xiong L.;
RT "Dynamic regulation of genome-wide pre-mRNA splicing and stress tolerance
RT by the Sm-like protein LSm5 in Arabidopsis.";
RL Genome Biol. 15:R1.1-R1.18(2014).
CC -!- FUNCTION: Component of LSM protein complexes, which are involved in RNA
CC processing. Component of the cytoplasmic LSM1-LSM7 complex which is
CC involved in mRNA degradation by promoting decapping and leading to
CC accurate 5'-3' mRNA decay. The cytoplasmic LSM1-LSM7 complex regulates
CC developmental gene expression by the decapping of specific development-
CC related transcripts. Component of the nuclear LSM2-LSM8 complex which
CC is involved splicing nuclear mRNAs. LSM2-LSM8 binds directly to the U6
CC small nuclear RNAs (snRNAs) and is essential for accurate splicing of
CC selected development-related mRNAs through the stabilization of the
CC spliceosomal U6 snRNA. Plays a critical role in the regulation of
CC development-related gene expression (PubMed:23221597, PubMed:23620288).
CC Involved in the control of plant sensitivity to abscisic acid (ABA) and
CC drought (PubMed:11740939). Functions with ABH1 as negative regulator of
CC ABA signaling in guard cells (PubMed:12427994). Required for regulation
CC of splicing efficiency of many stress-responsive genes under stress
CC conditions (PubMed:24393432). {ECO:0000269|PubMed:11740939,
CC ECO:0000269|PubMed:12427994, ECO:0000269|PubMed:23221597,
CC ECO:0000269|PubMed:23620288, ECO:0000269|PubMed:24393432}.
CC -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex that forms a
CC seven-membered ring structure with a donut shape. The LSM subunits are
CC arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4.
CC Component of the heptameric LSM2-LSM8 complex that forms a seven-
CC membered ring structure with a donut shape. The LSM subunits are
CC arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4
CC (PubMed:23221597, PubMed:23620288). LSM2 subunit interacts only with
CC its two neighboring subunits, LSM6A or LSM6B and LSM7
CC (PubMed:23221597). {ECO:0000269|PubMed:23221597,
CC ECO:0000269|PubMed:23620288}.
CC -!- INTERACTION:
CC Q9FKB0; A0A178WEI8: At1g54380; NbExp=3; IntAct=EBI-16419382, EBI-25520453;
CC Q9FKB0; Q9M1Z3: LSM6A; NbExp=3; IntAct=EBI-16419382, EBI-4431531;
CC Q9FKB0; Q9SEZ4: MYB105; NbExp=3; IntAct=EBI-16419382, EBI-15202260;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23221597,
CC ECO:0000269|PubMed:23620288}. Nucleus {ECO:0000269|PubMed:23221597,
CC ECO:0000269|PubMed:23620288}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:23221597, ECO:0000269|PubMed:23620288}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000305|PubMed:23221597}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; AY034896; AAK61592.1; -; mRNA.
DR EMBL; JQ612715; AFJ05005.1; -; Genomic_DNA.
DR EMBL; AB012242; BAB09440.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95735.1; -; Genomic_DNA.
DR EMBL; BT025700; ABF82603.1; -; mRNA.
DR EMBL; AK229657; BAF01501.1; -; mRNA.
DR RefSeq; NP_199698.1; NM_124264.4.
DR AlphaFoldDB; Q9FKB0; -.
DR SMR; Q9FKB0; -.
DR ComplexPortal; CPX-1308; LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6A-PAT1.
DR ComplexPortal; CPX-1309; LSM2-8 complex, variant LSM3A-LSM6A.
DR ComplexPortal; CPX-1345; LSM1-7-PAT1 complex, variant LSM1A-LSM3B-LSM6B-PAT1.
DR ComplexPortal; CPX-1346; LSM1-7-PAT1 complex, variant LSM1A-LSM3B-LSM6A-PAT1.
DR ComplexPortal; CPX-1347; LSM1-7-PAT1 complex, variant LSM1B-LSM3A-LSM6A-PAT1.
DR ComplexPortal; CPX-1348; LSM1-7-PAT1 complex, variant LSM1B-LSM3B-LSM6A-PAT1.
DR ComplexPortal; CPX-1349; LSM1-7-PAT1 complex, variant LSM1B-LSM3B-LSM6B-PAT1.
DR ComplexPortal; CPX-1350; LSM1-7-PAT1 complex, variant LSM1B-LSM3A-LSM6B-PAT1.
DR ComplexPortal; CPX-1351; LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6B-PAT1.
DR ComplexPortal; CPX-1352; LSM2-8 complex, variant LSM3A-LSM6B.
DR ComplexPortal; CPX-1353; LSM2-8 complex, variant LSM3B-LSM6A.
DR ComplexPortal; CPX-1354; LSM2-8 complex, variant LSM3B-LSM6B.
DR ComplexPortal; CPX-1391; LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6A-PAT1H1.
DR ComplexPortal; CPX-1392; LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6B-PAT1H1.
DR ComplexPortal; CPX-1393; LSM1-7-PAT1 complex, variant LSM1A-LSM3B-LSM6A-PAT1H1.
DR ComplexPortal; CPX-1394; LSM1-7-PAT1 complex, variant LSM1A-LSM3B-LSM6B-PAT1H1.
DR ComplexPortal; CPX-1395; LSM1-7-PAT1 complex, variant LSM1B-LSM3A-LSM6A-PAT1H1.
DR ComplexPortal; CPX-1396; LSM1-7-PAT1 complex, variant LSM1B-LSM3A-LSM6B-PAT1H1.
DR ComplexPortal; CPX-1397; LSM1-7-PAT1 complex, variant LSM1B-LSM3B-LSM6A-PAT1H1.
DR ComplexPortal; CPX-1398; LSM1-7-PAT1 complex, variant LSM1B-LSM3B-LSM6B-PAT1H1.
DR ComplexPortal; CPX-1399; LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6A-PAT1H2.
DR ComplexPortal; CPX-1400; LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6B-PAT1H2.
DR ComplexPortal; CPX-1401; LSM1-7-PAT1 complex, variant LSM1A-LSM3B-LSM6A-PAT1H2.
DR ComplexPortal; CPX-1402; LSM1-7-PAT1 complex, variant LSM1A-LSM3B-LSM6B-PAT1H2.
DR ComplexPortal; CPX-1403; LSM1-7-PAT1 complex, variant LSM1B-LSM3A-LSM6A-PAT1H2.
DR ComplexPortal; CPX-1404; LSM1-7-PAT1 complex, variant LSM1B-LSM3A-LSM6B-PAT1H2.
DR ComplexPortal; CPX-1405; LSM1-7-PAT1 complex, variant LSM1B-LSM3B-LSM6A-PAT1H2.
DR ComplexPortal; CPX-1406; LSM1-7-PAT1 complex, variant LSM1B-LSM3B-LSM6B-PAT1H2.
DR IntAct; Q9FKB0; 3.
DR STRING; 3702.AT5G48870.1; -.
DR iPTMnet; Q9FKB0; -.
DR PaxDb; Q9FKB0; -.
DR PRIDE; Q9FKB0; -.
DR ProteomicsDB; 238726; -.
DR EnsemblPlants; AT5G48870.1; AT5G48870.1; AT5G48870.
DR GeneID; 834945; -.
DR Gramene; AT5G48870.1; AT5G48870.1; AT5G48870.
DR KEGG; ath:AT5G48870; -.
DR Araport; AT5G48870; -.
DR TAIR; locus:2156589; AT5G48870.
DR eggNOG; KOG1775; Eukaryota.
DR HOGENOM; CLU_076902_6_1_1; -.
DR InParanoid; Q9FKB0; -.
DR OMA; YETTPQG; -.
DR OrthoDB; 1558822at2759; -.
DR PhylomeDB; Q9FKB0; -.
DR PRO; PR:Q9FKB0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKB0; baseline and differential.
DR Genevisible; Q9FKB0; AT.
DR GO; GO:1990726; C:Lsm1-7-Pat1 complex; IBA:GO_Central.
DR GO; GO:0120115; C:Lsm2-8 complex; IMP:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0000932; C:P-body; IC:ComplexPortal.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005688; C:U6 snRNP; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:TAIR.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:ComplexPortal.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR CDD; cd01732; LSm5; 1.
DR InterPro; IPR033871; LSm5.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR PANTHER; PTHR20971; PTHR20971; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..88
FT /note="Sm-like protein LSM5"
FT /id="PRO_0000431647"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 12
FT /note="E->K: In sad1; decreased germination rate, dwarf
FT plants with round-shaped leaves and increased sensitivity
FT to inhibition of seed germination and plant growth by
FT exogenous ABA."
FT /evidence="ECO:0000269|PubMed:11740939"
FT CONFLICT 86
FT /note="D -> N (in Ref. 6; BAF01501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 88 AA; 9658 MW; C85DCCDB73BFF661 CRC64;
MANNPSQLLP SELIDRCIGS KIWVIMKGDK ELVGILKGFD VYVNMVLEDV TEYEITAEGR
RVTKLDQILL NGNNIAILVP GGSPEDGE
