ID   LSM11_XENLA             Reviewed;         291 AA.
AC   Q7T076; A0A1L8GQX3; Q3KPW8;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=U7 snRNA-associated Sm-like protein LSm11 {ECO:0000305};
GN   Name=lsm11 {ECO:0000303|PubMed:12975319};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J;
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA   Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA   Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA   Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA   Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA   Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA   Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA   Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA   Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA   Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA   Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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   [3] {ECO:0000312|EMBL:AAI06509.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis {ECO:0000312|EMBL:AAI06509.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the U7 snRNP complex that is involved in the
CC       histone 3'-end pre-mRNA processing. Increases U7 snRNA levels but not
CC       histone 3'-end pre-mRNA processing activity, when overexpressed. Binds
CC       specifically to the Sm-binding site of U7 snRNA.
CC       {ECO:0000250|UniProtKB:Q8BUV6}.
CC   -!- SUBUNIT: Component of the heptameric ring U7 snRNP complex.
CC       {ECO:0000250|UniProtKB:Q8BUV6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P83369}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI06509.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AF514310; AAQ08119.1; -; mRNA.
DR   EMBL; CM004471; OCT86263.1; -; Genomic_DNA.
DR   EMBL; BC106508; AAI06509.1; ALT_INIT; mRNA.
DR   RefSeq; XP_018110373.1; XM_018254884.1.
DR   AlphaFoldDB; Q7T076; -.
DR   IntAct; Q7T076; 1.
DR   STRING; 8355.A0A1L8GQX3; -.
DR   GeneID; 100381151; -.
DR   KEGG; xla:100381151; -.
DR   CTD; 100381151; -.
DR   Xenbase; XB-GENE-6255756; lsm11.S.
DR   OMA; QETSECA; -.
DR   OrthoDB; 1605022at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 100381151; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0071209; F:U7 snRNA binding; IEA:InterPro.
DR   GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; 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; 1.
PE   2: Evidence at transcript level;
KW   mRNA processing; Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW   RNA-binding.
FT   CHAIN           1..291
FT                   /note="U7 snRNA-associated Sm-like protein LSm11"
FT                   /id="PRO_0000390505"
FT   REGION          55..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..289
FT                   /note="SM"
FT   REGION          203..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  32749 MW;  9CC2B8D82D991775 CRC64;
     MAEEEDEAPG SCLDVSSESF NPLLALYSPQ TPLPFPDIRC FNNLAEYESF LRGGARGRAR
     GAQRGQSRGP GGKRKGRKPE PDPERIERLK QLMLPVEEGK VPVRPRRSRA PKNVLTRMPL
     HAGSPLGELN RCVQDRIRIR VHIRTFKGLR GVCSGFIVAF DKFWNMAMVD VDETYRKPVL
     GKAFYNEPQL TLTRLFDRLQ LQEPGSHDPA KGRPAGPAET LTAPPSKKST QPSERAAGPP
     VEPGPQGHSG NRPKQRRRNR KEKVDYQQVF TRHLKQIFIR GENVLLVHIA E