LSM8_ARATH
ID LSM8_ARATH Reviewed; 98 AA.
AC Q8VYI0; Q9SHY4;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Sm-like protein LSM8 {ECO:0000305};
DE Short=AtLSM8 {ECO:0000303|PubMed:23620288};
DE AltName: Full=U6 snRNA-associated Sm-like protein LSM8 {ECO:0000305};
GN Name=LSM8 {ECO:0000303|PubMed:23221597};
GN OrderedLocusNames=At1g65700 {ECO:0000312|Araport:AT1G65700};
GN ORFNames=F1E22.8 {ECO:0000312|EMBL:AAF23841.1};
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], AND GENOME REANNOTATION.
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;
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, 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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH PFD1; PFD2; PFD3;
RP PFD4; PFD5 AND PFD6.
RC STRAIN=cv. Columbia;
RX PubMed=32396196; DOI=10.1093/nar/gkaa354;
RA Esteve-Bruna D., Carrasco-Lopez C., Blanco-Tourinan N., Iserte J.,
RA Calleja-Cabrera J., Perea-Resa C., Urbez C., Carrasco P., Yanovsky M.J.,
RA Blazquez M.A., Salinas J., Alabadi D.;
RT "Prefoldins contribute to maintaining the levels of the spliceosome LSM2-8
RT complex through Hsp90 in Arabidopsis.";
RL Nucleic Acids Res. 48:6280-6293(2020).
CC -!- FUNCTION: Component of the nuclear LSM2-LSM8 complex which is involved
CC splicing nuclear mRNAs. LSM2-LSM8 binds directly to the U6 small
CC nuclear RNAs (snRNAs). LSM8 is essential for the formation of the
CC nuclear LSM2-LSM8 complex involved in the accurate splicing of selected
CC development-related mRNAs through the stabilization of the spliceosomal
CC U6 snRNA (PubMed:32396196). Plays a critical role in the regulation of
CC development-related gene expression. {ECO:0000269|PubMed:23221597,
CC ECO:0000269|PubMed:23620288, ECO:0000269|PubMed:32396196}.
CC -!- SUBUNIT: Component of the heptameric LSM2-LSM8 complex that forms a
CC seven-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). LSM8 subunit interacts only with
CC its two neighboring subunits, LSM2 and LSM4 (PubMed:23221597).
CC Interacts with the prefoldin co-chaperone subunits PFD1, PFD2, PFD3,
CC PFD4, PFD5 and PFD6 (PubMed:32396196). {ECO:0000269|PubMed:23221597,
CC ECO:0000269|PubMed:23620288, ECO:0000269|PubMed:32396196}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23221597,
CC ECO:0000269|PubMed:23620288}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q8VYI0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:23221597, ECO:0000269|PubMed:23620288}.
CC -!- DISRUPTION PHENOTYPE: Developmental alterations, such as reduced root
CC length, alterations in the shape and number of cotyledons, small
CC rosette leaves with short petioles, early flowering, short siliques
CC with reduced seed number and frequently aborted seeds
CC (PubMed:23221597). Lower pre-mRNA splicing events and reduced levels of
CC U6 snRNA, but elevated levels of U4 snRNA (PubMed:32396196).
CC {ECO:0000269|PubMed:23221597, ECO:0000269|PubMed:32396196}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23841.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g65700 and At1g65710.; Evidence={ECO:0000305};
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DR EMBL; AC007234; AAF23841.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34413.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34414.1; -; Genomic_DNA.
DR EMBL; AY070767; AAL50104.1; -; mRNA.
DR EMBL; AY094059; AAM16215.1; -; mRNA.
DR EMBL; AY087015; AAM64576.1; -; mRNA.
DR PIR; G96681; G96681.
DR RefSeq; NP_001031238.1; NM_001036161.1. [Q8VYI0-1]
DR RefSeq; NP_176747.1; NM_105244.4. [Q8VYI0-1]
DR AlphaFoldDB; Q8VYI0; -.
DR SMR; Q8VYI0; -.
DR ComplexPortal; CPX-1309; LSM2-8 complex, variant LSM3A-LSM6A.
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 PRIDE; Q8VYI0; -.
DR ProteomicsDB; 238529; -. [Q8VYI0-1]
DR EnsemblPlants; AT1G65700.1; AT1G65700.1; AT1G65700. [Q8VYI0-1]
DR EnsemblPlants; AT1G65700.2; AT1G65700.2; AT1G65700. [Q8VYI0-1]
DR GeneID; 842881; -.
DR Gramene; AT1G65700.1; AT1G65700.1; AT1G65700. [Q8VYI0-1]
DR Gramene; AT1G65700.2; AT1G65700.2; AT1G65700. [Q8VYI0-1]
DR KEGG; ath:AT1G65700; -.
DR Araport; AT1G65700; -.
DR HOGENOM; CLU_076902_8_2_1; -.
DR OMA; CDGSMNL; -.
DR PhylomeDB; Q8VYI0; -.
DR PRO; PR:Q8VYI0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYI0; baseline and differential.
DR Genevisible; Q8VYI0; AT.
DR GO; GO:0120115; C:Lsm2-8 complex; IMP:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
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; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:ComplexPortal.
DR GO; GO:0016070; P:RNA metabolic process; IBA:GO_Central.
DR CDD; cd01727; LSm8; 1.
DR InterPro; IPR034103; Lsm8.
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 Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..98
FT /note="Sm-like protein LSM8"
FT /id="PRO_0000431651"
SQ SEQUENCE 98 AA; 10706 MW; BF0F341712396F73 CRC64;
MAATTGLETL VDQIISVITN DGRNIVGVLK GFDQATNIIL DESHERVFST KEGVQQHVLG
LYIIRGDNIG VIGELDEELD ASLDFSKLRA HPLKPVVH
