LSM11_MOUSE
ID LSM11_MOUSE Reviewed; 361 AA.
AC Q8BUV6;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=U7 snRNA-associated Sm-like protein LSm11 {ECO:0000305};
GN Name=Lsm11 {ECO:0000303|PubMed:12975319, ECO:0000312|MGI:MGI:1919540};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN THE U7 SNRNP
RP COMPLEX, AND INTERACTION WITH ZNF473.
RX PubMed=12975319; DOI=10.1101/gad.274403;
RA Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., Fischer U.,
RA Schuemperli D.;
RT "Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN
RT complex and the role of a new component, Lsm11, in histone RNA
RT processing.";
RL Genes Dev. 17:2321-2333(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP INTERACTION WITH CLNS1A; PRMT5 AND WDR77, AND LACK OF METHYLATION.
RX PubMed=16087681; DOI=10.1074/jbc.m505077200;
RA Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C.,
RA Fischer U., Schuemperli D.;
RT "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm
RT proteins with PRMT5 and SMN complexes.";
RL J. Biol. Chem. 280:34435-34440(2005).
RN [4]
RP FUNCTION, MUTAGENESIS OF 33-PRO--LEU-35; 59-TYR--SER-61; 108-PRO--ARG-110
RP AND 149-MET--LEU-151, AND INTERACTION WITH ZNF473.
RX PubMed=15824063; DOI=10.1093/nar/gki516;
RA Azzouz T.N., Gruber A., Schuemperli D.;
RT "U7 snRNP-specific Lsm11 protein: dual binding contacts with the 100 kDa
RT zinc finger processing factor (ZFP100) and a ZFP100-independent function in
RT histone RNA 3'-end processing.";
RL Nucleic Acids Res. 33:2106-2117(2005).
RN [5]
RP FUNCTION.
RX PubMed=16914750; DOI=10.1128/mcb.00391-06;
RA Wagner E.J., Marzluff W.F.;
RT "ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA
RT processing, is required for entry into S phase.";
RL Mol. Cell. Biol. 26:6702-6712(2006).
RN [6]
RP IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19470752; DOI=10.1128/mcb.00296-09;
RA Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.;
RT "Three proteins of the U7-specific Sm ring function as the molecular ruler
RT to determine the site of 3'-end processing in mammalian histone pre-mRNA.";
RL Mol. Cell. Biol. 29:4045-4056(2009).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-41, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Component of the U7 snRNP complex that is involved in the
CC histone 3'-end pre-mRNA processing (PubMed:12975319, PubMed:15824063).
CC Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing
CC activity, when overexpressed (PubMed:12975319, PubMed:15824063).
CC Required for cell cycle progression from G1 to S phases
CC (PubMed:16914750). Binds specifically to the Sm-binding site of U7
CC snRNA. {ECO:0000269|PubMed:12975319, ECO:0000269|PubMed:15824063,
CC ECO:0000269|PubMed:16914750}.
CC -!- SUBUNIT: Component of the heptameric ring U7 snRNP complex, or U7 Sm
CC protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3,
CC SNRPE, SNRPF, SNRPG and U7 snRNA (PubMed:12975319). Formation of the U7
CC snRNP is an ATP-dependent process mediated by a specialized SMN complex
CC containing at least the Sm protein core complex and additionally, the
CC U7-specific LSM10 and LSM11 proteins (PubMed:12975319). Identified in a
CC histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP,
CC SNRPB, SYNCRIP and YBX1 (PubMed:19470752). Interacts (via the Sm
CC domains) with CLNS1A (PubMed:16087681). Interacts with PRMT5, SMN,
CC ZNF473 and WDR77 (PubMed:12975319, PubMed:16087681, PubMed:15824063).
CC {ECO:0000269|PubMed:12975319, ECO:0000269|PubMed:15824063,
CC ECO:0000269|PubMed:16087681, ECO:0000269|PubMed:19470752}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P83369}.
CC -!- DOMAIN: The C-terminal SM 1 domain is both necessary for the binding to
CC the Sm-binding site of U7 snRNA and U7 snRNP assembly
CC (PubMed:12975319). The N-terminal domain is essential for histone pre-
CC mRNA cleavage (PubMed:12975319). Amino acids 63-82 are sufficient to
CC interact with ZNF473 (PubMed:12975319). {ECO:0000269|PubMed:12975319}.
CC -!- PTM: Not methylated. {ECO:0000269|PubMed:16087681}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; AF514309; AAQ08118.1; -; mRNA.
DR EMBL; AK082292; BAC38456.1; -; mRNA.
DR CCDS; CCDS36131.1; -.
DR RefSeq; NP_082461.1; NM_028185.2.
DR AlphaFoldDB; Q8BUV6; -.
DR SMR; Q8BUV6; -.
DR BioGRID; 215285; 1.
DR IntAct; Q8BUV6; 1.
DR STRING; 10090.ENSMUSP00000117531; -.
DR iPTMnet; Q8BUV6; -.
DR PhosphoSitePlus; Q8BUV6; -.
DR EPD; Q8BUV6; -.
DR MaxQB; Q8BUV6; -.
DR PaxDb; Q8BUV6; -.
DR PRIDE; Q8BUV6; -.
DR ProteomicsDB; 252535; -.
DR Antibodypedia; 48521; 147 antibodies from 22 providers.
DR DNASU; 72290; -.
DR Ensembl; ENSMUST00000062458; ENSMUSP00000057343; ENSMUSG00000044847.
DR Ensembl; ENSMUST00000129820; ENSMUSP00000117531; ENSMUSG00000044847.
DR GeneID; 72290; -.
DR KEGG; mmu:72290; -.
DR UCSC; uc007ins.1; mouse.
DR CTD; 134353; -.
DR MGI; MGI:1919540; Lsm11.
DR VEuPathDB; HostDB:ENSMUSG00000044847; -.
DR eggNOG; ENOG502QS1B; Eukaryota.
DR GeneTree; ENSGT00390000012944; -.
DR HOGENOM; CLU_065821_0_0_1; -.
DR InParanoid; Q8BUV6; -.
DR OMA; QETSECA; -.
DR OrthoDB; 1605022at2759; -.
DR PhylomeDB; Q8BUV6; -.
DR TreeFam; TF326954; -.
DR Reactome; R-MMU-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR BioGRID-ORCS; 72290; 24 hits in 72 CRISPR screens.
DR PRO; PR:Q8BUV6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BUV6; protein.
DR Bgee; ENSMUSG00000044847; Expressed in nucleus pulposus and 203 other tissues.
DR ExpressionAtlas; Q8BUV6; baseline and differential.
DR Genevisible; Q8BUV6; MM.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISO:MGI.
DR GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB.
DR GO; GO:0071209; F:U7 snRNA binding; ISS:UniProtKB.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IDA:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1902275; P:regulation of chromatin organization; ISS:UniProtKB.
DR CDD; cd01739; LSm11_M; 1.
DR InterPro; IPR039267; Lsm11.
DR InterPro; IPR034109; Lsm11_M.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR PANTHER; PTHR21415; PTHR21415; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 2.
PE 1: Evidence at protein level;
KW Isopeptide bond; Methylation; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..361
FT /note="U7 snRNA-associated Sm-like protein LSm11"
FT /id="PRO_0000125588"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..205
FT /note="SM 1"
FT /evidence="ECO:0000303|PubMed:12975319"
FT REGION 268..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..357
FT /note="SM 2"
FT /evidence="ECO:0000303|PubMed:12975319"
FT COMPBIAS 79..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P83369"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P83369"
FT MOD_RES 41
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P83369"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P83369"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P83369"
FT MUTAGEN 33..35
FT /note="PLL->AAA: Does not inhibit interaction with ZNF473.
FT Reduces strongly histone 3' end processing."
FT /evidence="ECO:0000269|PubMed:15824063"
FT MUTAGEN 59..61
FT /note="YES->AAA: Does not inhibit interaction with ZNF473
FT and histone 3'-end processing."
FT /evidence="ECO:0000269|PubMed:15824063"
FT MUTAGEN 108..110
FT /note="PER->AAA: Does not inhibit interaction with ZNF473.
FT Reduces weakly histone 3' end processing."
FT /evidence="ECO:0000269|PubMed:15824063"
FT MUTAGEN 149..151
FT /note="MPL->AAA: Does not inhibit interaction with ZNF473.
FT Reduces weakly histone 3' end processing."
FT /evidence="ECO:0000269|PubMed:15824063"
SQ SEQUENCE 361 AA; 39907 MW; 68777427AC37E10E CRC64;
MEEREWGARS ARAGSPASPP SPRLDVSSYS FDPLLALYAP RLPPIPYPNA PCFNNVAEYE
SFLKGGRTGR GRARGTGEPA SAGTSTGTST GAGSSSRARR RAAPTPDPER IQRLRRLMVV
KEDTDGTAGA RRQGPGRSKK APRNVLTRMP LHEGSPLGEL HRCIREGVKV NVHIRTFKGL
RGVCTGFLVA FDKFWNMALT DVDETYRKPV LGKAYERDSS LTLTRLFDRL KLQDSSKKEA
DSKSAVEDST LSRYSQTSTW KVASVWGRGD TDRSSHRRSR SVPSSLQASA REESRSELSG
RTTRTEGSSV GGTFSRATTL SRGQSRKKKR KPKVDYQQVF TRHINQIFIR GENVLLVHLA
Q
