LSM3B_ARATH
ID LSM3B_ARATH Reviewed; 98 AA.
AC Q9C6K5;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Sm-like protein LSM3B {ECO:0000305};
DE Short=AtLSM3B {ECO:0000303|PubMed:23620288};
DE AltName: Full=U6 snRNA-associated Sm-like protein LSM3B {ECO:0000305};
GN Name=LSM3B {ECO:0000303|PubMed:23221597};
GN OrderedLocusNames=At1g76860 {ECO:0000312|Araport:AT1G76860};
GN ORFNames=F7O12.3 {ECO:0000312|EMBL:AAG51149.1};
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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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, SUBUNIT, INTERACTION WITH LSM2; LSM6A AND LSM6B, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, 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 [7]
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 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). LSM3B subunit interacts only with
CC its two neighboring subunits, LSM2 and LSM6A or LSM6B
CC (PubMed:23221597). {ECO:0000269|PubMed:23221597,
CC ECO:0000269|PubMed:23620288}.
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 -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; AC079283; AAG51149.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35896.1; -; Genomic_DNA.
DR EMBL; BT025575; ABF58993.1; -; mRNA.
DR EMBL; AY086266; AAM64339.1; -; mRNA.
DR PIR; D96797; D96797.
DR RefSeq; NP_177812.1; NM_106337.2.
DR AlphaFoldDB; Q9C6K5; -.
DR SMR; Q9C6K5; -.
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-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-1353; LSM2-8 complex, variant LSM3B-LSM6A.
DR ComplexPortal; CPX-1354; LSM2-8 complex, variant LSM3B-LSM6B.
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-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-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-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; Q9C6K5; 1.
DR STRING; 3702.AT1G76860.1; -.
DR iPTMnet; Q9C6K5; -.
DR PaxDb; Q9C6K5; -.
DR PRIDE; Q9C6K5; -.
DR ProteomicsDB; 238803; -.
DR EnsemblPlants; AT1G76860.1; AT1G76860.1; AT1G76860.
DR GeneID; 844021; -.
DR Gramene; AT1G76860.1; AT1G76860.1; AT1G76860.
DR KEGG; ath:AT1G76860; -.
DR Araport; AT1G76860; -.
DR TAIR; locus:2036257; AT1G76860.
DR eggNOG; KOG3460; Eukaryota.
DR HOGENOM; CLU_076902_5_1_1; -.
DR InParanoid; Q9C6K5; -.
DR OMA; SEMIFVR; -.
DR OrthoDB; 1633672at2759; -.
DR PhylomeDB; Q9C6K5; -.
DR PRO; PR:Q9C6K5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6K5; baseline and differential.
DR Genevisible; Q9C6K5; 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:0005739; C:mitochondrion; HDA:TAIR.
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; IBA:GO_Central.
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:0033962; P:P-body assembly; IBA:GO_Central.
DR CDD; cd01730; LSm3; 1.
DR InterPro; IPR034105; Lsm3.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR040002; Sm-like_LSM3.
DR PANTHER; PTHR13110; PTHR13110; 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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..98
FT /note="Sm-like protein LSM3B"
FT /id="PRO_0000431645"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 98 AA; 11286 MW; 7960146D8C0AF9DC CRC64;
MSGEEEATVR EPLDLIRLSL DERIYVKLRS DRELRGKLHA FDQHLNMILG DVEETITTVE
IDDETYEEIV RTTKRTIEFL FVRGDGVILV SPPLRTAA
