LSM1_SCHPO
ID LSM1_SCHPO Reviewed; 140 AA.
AC P87173;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm1;
GN Name=lsm1; ORFNames=SPBC3D6.08c;
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).
CC -!- FUNCTION: Component of the cytoplasmic LSM1-LSM7 complex which is
CC involved in mRNA degradation by activating the decapping step. The
CC LSM1-LSM7 complex binds RNA with a preference for poly-U ends.
CC {ECO:0000250|UniProtKB:P47017}.
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 Except for LSM1, where a C-terminal helix crosses the ring structure to
CC form additional interactions with LSM3 and LSM6, each subunit interacts
CC only with its two neighboring subunits. The LSM1-LSM7 complex interacts
CC with PAT1; within the complex PAT1 has direct interactions with LSM2
CC and LSM3. {ECO:0000250|UniProtKB:P47017}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P47017}. Cytoplasm
CC {ECO:0000250|UniProtKB:P47017}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:P47017}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR EMBL; CU329671; CAB09117.1; -; Genomic_DNA.
DR PIR; T40368; T40368.
DR RefSeq; NP_595520.1; NM_001021429.2.
DR PDB; 6PPQ; X-ray; 1.81 A; A=1-84.
DR PDB; 6PPV; X-ray; 2.05 A; A=1-84.
DR PDBsum; 6PPQ; -.
DR PDBsum; 6PPV; -.
DR AlphaFoldDB; P87173; -.
DR SMR; P87173; -.
DR BioGRID; 277048; 2.
DR STRING; 4896.SPBC3D6.08c.1; -.
DR MaxQB; P87173; -.
DR PaxDb; P87173; -.
DR EnsemblFungi; SPBC3D6.08c.1; SPBC3D6.08c.1:pep; SPBC3D6.08c.
DR GeneID; 2540520; -.
DR KEGG; spo:SPBC3D6.08c; -.
DR PomBase; SPBC3D6.08c; lsm1.
DR VEuPathDB; FungiDB:SPBC3D6.08c; -.
DR eggNOG; KOG1782; Eukaryota.
DR HOGENOM; CLU_076902_0_1_1; -.
DR InParanoid; P87173; -.
DR OMA; FMVRGEN; -.
DR PhylomeDB; P87173; -.
DR Reactome; R-SPO-430039; mRNA decay by 5' to 3' exoribonuclease.
DR PRO; PR:P87173; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:1990726; C:Lsm1-7-Pat1 complex; IBA:GO_Central.
DR GO; GO:0005845; C:mRNA cap binding complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000932; C:P-body; ISO:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000339; F:RNA cap binding; ISO:PomBase.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; ISO:PomBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0016070; P:RNA metabolic process; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd01728; LSm1; 1.
DR InterPro; IPR034104; Lsm1.
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 3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding.
FT CHAIN 1..140
FT /note="U6 snRNA-associated Sm-like protein LSm1"
FT /id="PRO_0000125590"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:6PPQ"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:6PPQ"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:6PPQ"
FT STRAND 47..58
FT /evidence="ECO:0007829|PDB:6PPQ"
FT STRAND 61..72
FT /evidence="ECO:0007829|PDB:6PPQ"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6PPQ"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:6PPQ"
SQ SEQUENCE 140 AA; 16172 MW; AB4C477FE4B7B432 CRC64;
MNQATQIIPF TTSGSLVDYV DRKVIVVLRD GKKLIGILRS FDQFANLMLQ YTIERIYVDD
MYGDIDRGVY IVRGENVVLL GELDLDKEYD AVKQLRRMPA EELYPLAKLH EEEKKKNIRE
KGKYLHSVGF SVDGGHDDLY
