ID   LSM6_SCHPO              Reviewed;          75 AA.
AC   Q9UUI1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 144.
DE   RecName: Full=LSM complex subunit lsm6 {ECO:0000305};
GN   Name=lsm6; ORFNames=SPAC2F3.17c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2] {ECO:0007744|PDB:3SWN}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), SUBUNIT, AND IDENTIFICATION IN THE
RP   LSM1-LSM7 AND LSM2-LSM8 COMPLEXES.
RX   PubMed=22001694; DOI=10.1016/j.jmb.2011.09.051;
RA   Mund M., Neu A., Ullmann J., Neu U., Sprangers R.;
RT   "Structure of the LSm657 complex: an assembly intermediate of the LSm1-7
RT   and LSm2-8 rings.";
RL   J. Mol. Biol. 414:165-176(2011).
RN   [3] {ECO:0007744|PDB:4EMK}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   IDENTIFICATION IN THE LSM1-LSM7 AND LSM2-LSM8 COMPLEXES.
RX   PubMed=22615807; DOI=10.1371/journal.pone.0036768;
RA   Wu D., Jiang S., Bowler M.W., Song H.;
RT   "Crystal structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces
RT   pombe.";
RL   PLoS ONE 7:e36768-e36768(2012).
RN   [4] {ECO:0007744|PDB:6PPN, ECO:0007744|PDB:6PPP, ECO:0007744|PDB:6PPQ, ECO:0007744|PDB:6PPV}
RP   X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) IN COMPLEX WITH RNA, FUNCTION,
RP   SUBUNIT, AND IDENTIFICATION IN THE LSM1-LSM7 AND LSM2-LSM8 COMPLEXES.
RX   PubMed=32518066; DOI=10.1261/rna.075879.120;
RA   Montemayor E.J., Virta J.M., Hayes S.M., Nomura Y., Brow D.A.,
RA   Butcher S.E.;
RT   "Molecular basis for the distinct cellular functions of the Lsm1-7 and
RT   Lsm2-8 complexes.";
RL   RNA 26:1400-1413(2020).
CC   -!- FUNCTION: Component of LSm protein complexes, which are involved in RNA
CC       processing and may function in a chaperone-like manner
CC       (PubMed:22615807, PubMed:32518066). Component of the cytoplasmic LSM1-
CC       LSM7 complex which is involved in mRNA degradation by activating the
CC       decapping step (PubMed:32518066). The LSM1-LSM7 complex loads onto the
CC       3'-end of single stranded RNA (PubMed:32518066). Component of the
CC       nuclear LSM2-LSM8 complex, which is involved in spliceosome assembly
CC       (PubMed:32518066). The LSM2-LSM8 complex plays a role in the biogenesis
CC       of the spliceosomal U4/U6-U5 tri-snRNP complex by accelerating prp24-
CC       mediated annealing of U4/U6 di-snRNA (By similarity). The LSM2-LSM8
CC       complex binds U6 snRNA terminating with a cyclic 2',3' phosphate group;
CC       RNA with an unmodified 3' hydroxyl or non-cyclic 3' phosphate is bound
CC       less tightly (PubMed:32518066). {ECO:0000250|UniProtKB:Q06406,
CC       ECO:0000269|PubMed:22615807, ECO:0000269|PubMed:32518066}.
CC   -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex that forms a
CC       seven-membered ring structure with a donut shape (Probable)
CC       (PubMed:32518066). The LSm subunits are arranged in the order lsm1,
CC       lsm2, lsm3, lsm6, lsm5, lsm7 and lsm4 (PubMed:22001694,
CC       PubMed:22615807, PubMed:32518066). Component of the heptameric LSM2-
CC       LSM8 complex that forms a seven-membered ring structure with a donut
CC       shape (Probable) (PubMed:32518066). The LSm subunits are arranged in
CC       the order lsm8, lsm2, lsm3, lsm6, lsm5, lsm7 and lsm4 (PubMed:22001694,
CC       PubMed:22615807, PubMed:32518066). {ECO:0000269|PubMed:22001694,
CC       ECO:0000269|PubMed:22615807, ECO:0000269|PubMed:32518066,
CC       ECO:0000305|PubMed:22001694, ECO:0000305|PubMed:22615807}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06406}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06406}. Note=LSM1 and LSM8
CC       act competitively with respect to the localization of LSM1-LSM7 to the
CC       cytoplasm and LSM2-LSM8 to the nucleus. LSm proteins shift to the
CC       cytoplasm under conditions of stress. {ECO:0000250|UniProtKB:Q06406}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC       subfamily. {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; CU329670; CAB54975.1; -; Genomic_DNA.
DR   PIR; T38534; T38534.
DR   RefSeq; NP_594380.1; NM_001019801.3.
DR   PDB; 3SWN; X-ray; 2.50 A; B/E/Q/T=1-75.
DR   PDB; 4EMK; X-ray; 2.30 A; B=1-75.
DR   PDB; 6PPN; X-ray; 1.91 A; F/N=1-75.
DR   PDB; 6PPP; X-ray; 2.33 A; F/N=1-75.
DR   PDB; 6PPQ; X-ray; 1.81 A; F=1-75.
DR   PDB; 6PPV; X-ray; 2.05 A; F=1-75.
DR   AlphaFoldDB; Q9UUI1; -.
DR   SMR; Q9UUI1; -.
DR   BioGRID; 278481; 3.
DR   ComplexPortal; CPX-26411; U6 small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-26555; LSM2-8 complex.
DR   FunCoup; Q9UUI1; 568.
DR   IntAct; Q9UUI1; 1.
DR   STRING; 284812.Q9UUI1; -.
DR   iPTMnet; Q9UUI1; -.
DR   PaxDb; 284812-Q9UUI1; -.
DR   GeneID; 2541997; -.
DR   KEGG; spo:2541997; -.
DR   PomBase; SPAC2F3.17c; lsm6.
DR   VEuPathDB; FungiDB:SPAC2F3.17c; -.
DR   eggNOG; KOG1783; Eukaryota.
DR   HOGENOM; CLU_076902_7_4_1; -.
DR   InParanoid; Q9UUI1; -.
DR   OMA; EQTVEYV; -.
DR   PhylomeDB; Q9UUI1; -.
DR   Reactome; R-SPO-430039; mRNA decay by 5' to 3' exoribonuclease.
DR   EvolutionaryTrace; Q9UUI1; -.
DR   PRO; PR:Q9UUI1; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:1990726; C:Lsm1-7-Pat1 complex; EXP:PomBase.
DR   GO; GO:0120115; C:Lsm2-8 complex; IPI:ComplexPortal.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0005697; C:telomerase holoenzyme complex; EXP:PomBase.
DR   GO; GO:0005686; C:U2 snRNP; EXP:PomBase.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central.
DR   GO; GO:0005682; C:U5 snRNP; IDA:PomBase.
DR   GO; GO:0005688; C:U6 snRNP; EXP:PomBase.
DR   GO; GO:0008266; F:poly(U) RNA binding; IDA:PomBase.
DR   GO; GO:0030620; F:U2 snRNA binding; IDA:PomBase.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; NAS:ComplexPortal.
DR   GO; GO:1905323; P:telomerase holoenzyme complex assembly; TAS:PomBase.
DR   CDD; cd01726; LSm6; 1.
DR   FunFam; 2.30.30.100:FF:000044; Probable U6 snRNA-associated Sm-like protein LSm6; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR016487; Lsm6/sSmF.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR047575; Sm.
DR   InterPro; IPR001163; Sm_dom_euk/arc.
DR   PANTHER; PTHR11021; SMALL NUCLEAR RIBONUCLEOPROTEIN F SNRNP-F; 1.
DR   PANTHER; PTHR11021:SF1; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM6; 1.
DR   Pfam; PF01423; LSM; 1.
DR   PIRSF; PIRSF006609; snRNP_SmF; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS52002; SM; 1.
DR   PDBsum; 3SWN; -.
DR   PDBsum; 4EMK; -.
DR   PDBsum; 6PPN; -.
DR   PDBsum; 6PPP; -.
DR   PDBsum; 6PPQ; -.
DR   PDBsum; 6PPV; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Ribonucleoprotein; RNA-binding; rRNA processing;
KW   Spliceosome; tRNA processing.
FT   CHAIN           1..75
FT                   /note="LSM complex subunit lsm6"
FT                   /id="PRO_0000125577"
FT   DOMAIN          4..75
FT                   /note="Sm"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
FT   HELIX           4..12
FT                   /evidence="ECO:0007829|PDB:6PPQ"
FT   STRAND          15..21
FT                   /evidence="ECO:0007829|PDB:6PPQ"
FT   STRAND          26..34
FT                   /evidence="ECO:0007829|PDB:6PPQ"
FT   STRAND          40..49
FT                   /evidence="ECO:0007829|PDB:6PPQ"
FT   STRAND          52..62
FT                   /evidence="ECO:0007829|PDB:6PPQ"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:6PPQ"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:6PPQ"
SQ   SEQUENCE   75 AA;  8336 MW;  20B1B1F2E380BCCF CRC64;
     MDSSPNEFLN KVIGKKVLIR LSSGVDYKGI LSCLDGYMNL ALERTEEYVN GKKTNVYGDA
     FIRGNNVLYV SALDD
//