LSM2_ARATH
ID LSM2_ARATH Reviewed; 93 AA.
AC Q1H595; Q8L5U6; Q9ZVT4;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Sm-like protein LSM2 {ECO:0000305};
DE Short=AtLSM2 {ECO:0000303|PubMed:23620288};
DE AltName: Full=U6 snRNA-associated Sm-like protein LSM2 {ECO:0000305};
GN Name=LSM2 {ECO:0000303|PubMed:23221597};
GN OrderedLocusNames=At1g03330 {ECO:0000312|Araport:AT1G03330};
GN ORFNames=F15K9.7 {ECO:0000312|EMBL:AAC72111.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH LSM1A; LSM3A; LSM3B AND LSM8, SUBCELLULAR
RP LOCATION, 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, AND TISSUE
RP 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).
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. {ECO:0000269|PubMed:23221597,
CC ECO:0000269|PubMed:23620288}.
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 (PubMed:23221597, PubMed:23620288). LSM2 subunit interacts only with
CC its two neighboring subunits, LSM1A or LSM1B and LSM3A or LSM3B
CC (PubMed:23221597). Component of the heptameric LSM2-LSM8 complex that
CC forms a seven-membered ring structure with a donut shape. The LSM
CC subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7
CC and LSM4 (PubMed:23221597, PubMed:23620288). LSM2 subunit interacts
CC only with its two neighboring subunits, LSM8 and LSM3A or LSM3B
CC (PubMed:23221597). {ECO:0000269|PubMed:23221597,
CC ECO:0000269|PubMed:23620288}.
CC -!- INTERACTION:
CC Q1H595; Q17TI5: BRX; NbExp=3; IntAct=EBI-9347308, EBI-4426649;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23221597}. Nucleus
CC {ECO:0000269|PubMed:23221597}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72111.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC005278; AAC72111.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27560.1; -; Genomic_DNA.
DR EMBL; BT025569; ABF58987.1; -; mRNA.
DR EMBL; AY085777; AAM62994.1; -; mRNA.
DR PIR; H86164; H86164.
DR RefSeq; NP_563682.1; NM_100215.4.
DR AlphaFoldDB; Q1H595; -.
DR SMR; Q1H595; -.
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; Q1H595; 2.
DR STRING; 3702.AT1G03330.1; -.
DR PaxDb; Q1H595; -.
DR PRIDE; Q1H595; -.
DR ProteomicsDB; 238802; -.
DR EnsemblPlants; AT1G03330.1; AT1G03330.1; AT1G03330.
DR GeneID; 839526; -.
DR Gramene; AT1G03330.1; AT1G03330.1; AT1G03330.
DR KEGG; ath:AT1G03330; -.
DR Araport; AT1G03330; -.
DR TAIR; locus:2014480; AT1G03330.
DR eggNOG; KOG3448; Eukaryota.
DR HOGENOM; CLU_130474_3_0_1; -.
DR InParanoid; Q1H595; -.
DR OMA; EERYPHM; -.
DR OrthoDB; 1571169at2759; -.
DR PhylomeDB; Q1H595; -.
DR PRO; PR:Q1H595; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q1H595; baseline and differential.
DR Genevisible; Q1H595; AT.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
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; IEA:UniProtKB-KW.
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 CDD; cd01725; LSm2; 1.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR016654; U6_snRNA_Lsm2.
DR PANTHER; PTHR13829; PTHR13829; 1.
DR Pfam; PF01423; LSM; 1.
DR PIRSF; PIRSF016394; U6_snRNA_Lsm2; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..93
FT /note="Sm-like protein LSM2"
FT /id="PRO_0000431643"
FT CONFLICT 84
FT /note="D -> G (in Ref. 4; AAM62994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 93 AA; 10694 MW; 8DD4B49DB99D9920 CRC64;
MLFFSYFKDL VGQEVTVELK NDLAIRGTLH SVDQYLNIKL ENTRVVDQDK YPHMLSVRNC
FIRGSVVRYV QLPKDGVDVD LLHDAARREA RGG
