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LSM1B_ARATH
ID   LSM1B_ARATH             Reviewed;         128 AA.
AC   Q8LFL8; Q9LJI0;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Sm-like protein LSM1B {ECO:0000305};
DE            Short=AtLSM1b {ECO:0000303|PubMed:23620288};
GN   Name=LSM1B {ECO:0000303|PubMed:23221597};
GN   OrderedLocusNames=At3g14080 {ECO:0000312|Araport:AT3G14080};
GN   ORFNames=MAG2.4 {ECO:0000312|EMBL:BAB02972.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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;
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   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, SUBUNIT, INTERACTION WITH LSM2 AND LSM4, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND GENE FAMILY.
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, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 the cytoplasmic LSM1-LSM7 complex which is
CC       involved in mRNA degradation by promoting decapping and leading to
CC       accurate 5'-3' mRNA decay. LSM1A and LSM1B are essential for the
CC       formation of the cytoplasmic LSM1-LSM7 complex which regulates
CC       developmental gene expression by the decapping of specific development-
CC       related transcripts (PubMed:23221597, PubMed:23620288). Required for P-
CC       body formation during heat stress (PubMed:23221597).
CC       {ECO:0000269|PubMed:23221597, 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). LSM1B subunit interacts only with
CC       its two neighboring subunits, LSM2 and LSM4 (PubMed:23221597).
CC       {ECO:0000269|PubMed:23221597, ECO:0000269|PubMed:23620288}.
CC   -!- INTERACTION:
CC       Q8LFL8; Q38845: PP2AA1; NbExp=3; IntAct=EBI-4434198, EBI-1645478;
CC       Q8LFL8; A0A1I9LQF0: SAUR57; NbExp=3; IntAct=EBI-4434198, EBI-25517419;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23221597,
CC       ECO:0000269|PubMed:23620288}. Cytoplasm, P-body
CC       {ECO:0000269|PubMed:23221597}. Note=Translocates from cytosol to P-
CC       bodies upon heat stress. {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: No visible phenotype under normal growth
CC       conditions, but the double mutants lsm1a and lsm1b show severe
CC       developmental alterations, such as delayed seed germination, reduced
CC       root length, epinastic, chlorotic and small cotyledons, small and
CC       serrated leaves, abnormal venation in cotyledons and leaves, dwarf
CC       plants with early flowering, short siliques with reduced seed number
CC       and small morphologically alterated seeds.
CC       {ECO:0000269|PubMed:23221597, ECO:0000269|PubMed:23620288}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB02972.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP000600; BAB02972.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE75465.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75466.1; -; Genomic_DNA.
DR   EMBL; BT002795; AAO22620.1; -; mRNA.
DR   EMBL; BT004340; AAO42334.1; -; mRNA.
DR   EMBL; AY084768; AAM61336.1; -; mRNA.
DR   RefSeq; NP_001326377.1; NM_001338101.1.
DR   RefSeq; NP_566476.1; NM_112264.4.
DR   RefSeq; NP_850580.1; NM_180249.4.
DR   AlphaFoldDB; Q8LFL8; -.
DR   SMR; Q8LFL8; -.
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-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-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; Q8LFL8; 6.
DR   STRING; 3702.AT3G14080.2; -.
DR   PaxDb; Q8LFL8; -.
DR   ProteomicsDB; 238567; -.
DR   EnsemblPlants; AT3G14080.1; AT3G14080.1; AT3G14080.
DR   EnsemblPlants; AT3G14080.2; AT3G14080.2; AT3G14080.
DR   GeneID; 820624; -.
DR   Gramene; AT3G14080.1; AT3G14080.1; AT3G14080.
DR   Gramene; AT3G14080.2; AT3G14080.2; AT3G14080.
DR   KEGG; ath:AT3G14080; -.
DR   Araport; AT3G14080; -.
DR   TAIR; locus:2087522; AT3G14080.
DR   eggNOG; KOG1782; Eukaryota.
DR   HOGENOM; CLU_076902_0_2_1; -.
DR   InParanoid; Q8LFL8; -.
DR   OrthoDB; 1508864at2759; -.
DR   PhylomeDB; Q8LFL8; -.
DR   PRO; PR:Q8LFL8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8LFL8; baseline and differential.
DR   Genevisible; Q8LFL8; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:1990726; C:Lsm1-7-Pat1 complex; IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; IDA:TAIR.
DR   GO; GO:0003723; F:RNA binding; IDA:TAIR.
DR   GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR   GO; GO:0009631; P:cold acclimation; IMP:TAIR.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR   GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR   GO; GO:0006397; P:mRNA processing; IGI:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR   GO; GO:0016070; P:RNA metabolic process; IGI:TAIR.
DR   CDD; cd01728; LSm1; 1.
DR   InterPro; IPR034104; Lsm1.
DR   InterPro; IPR001163; LSM_dom_euk/arc.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR044642; PTHR15588.
DR   PANTHER; PTHR15588; PTHR15588; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; mRNA processing; Reference proteome; Ribonucleoprotein;
KW   RNA-binding.
FT   CHAIN           1..128
FT                   /note="Sm-like protein LSM1B"
FT                   /id="PRO_0000431642"
SQ   SEQUENCE   128 AA;  14693 MW;  F8592E72212CCE9D CRC64;
     MSWAGPEEIY LSTSLASYLD RKLLVLLRDG RKLMGTLRSF DQFANAVLEG ACERVIVGEQ
     YCDIPLGLYV IRGENVVLIG ELDTEREELP PHMIRVSEAE IKRAQKVERE ASELRGTMRK
     RMEFLDFD
 
 
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