ID LSM2_DICDI Reviewed; 117 AA.
AC Q54TF6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE RecName: Full=Probable U6 snRNA-associated Sm-like protein LSm2;
GN Name=lsm2; ORFNames=DDB_G0281779;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Plays a role in pre-mRNA splicing as component of the U4/U6-
CC U5 tri-snRNP complex that is involved in spliceosome assembly, and as
CC component of the precatalytic spliceosome (spliceosome B complex). The
CC heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract
CC of U6 snRNA. {ECO:0000250|UniProtKB:Q9Y333}.
CC -!- SUBUNIT: Component of the precatalytic spliceosome (spliceosome B
CC complex). Component of the U4/U6-U5 tri-snRNP complex, a building block
CC of the precatalytic spliceosome (spliceosome B complex). LSM2, LSM3,
CC LSM4, LSM5, LSM6, LSM7 and LSM8 form a heptameric, ring-shaped
CC subcomplex (the LSM2-8 complex) that is part of the U4/U6-U5 tri-snRNP
CC complex and the precatalytic spliceosome.
CC {ECO:0000250|UniProtKB:Q9Y333}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y333}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {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; AAFI02000042; EAL66651.1; -; Genomic_DNA.
DR RefSeq; XP_640635.1; XM_635543.1.
DR AlphaFoldDB; Q54TF6; -.
DR SMR; Q54TF6; -.
DR STRING; 44689.Q54TF6; -.
DR PaxDb; 44689-DDB0233376; -.
DR EnsemblProtists; EAL66651; EAL66651; DDB_G0281779.
DR GeneID; 8623246; -.
DR KEGG; ddi:DDB_G0281779; -.
DR dictyBase; DDB_G0281779; lsm2.
DR eggNOG; KOG3448; Eukaryota.
DR HOGENOM; CLU_130474_3_0_1; -.
DR InParanoid; Q54TF6; -.
DR OMA; DNISCTD; -.
DR PhylomeDB; Q54TF6; -.
DR Reactome; R-DDI-430039; mRNA decay by 5' to 3' exoribonuclease.
DR PRO; PR:Q54TF6; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0005730; C:nucleolus; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0005688; C:U6 snRNP; ISS:dictyBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:dictyBase.
DR CDD; cd01725; LSm2; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR InterPro; IPR016654; U6_snRNA_Lsm2.
DR PANTHER; PTHR13829; SNRNP CORE PROTEIN FAMILY MEMBER; 1.
DR PANTHER; PTHR13829:SF2; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM2; 1.
DR Pfam; PF01423; LSM; 1.
DR PIRSF; PIRSF016394; U6_snRNA_Lsm2; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS52002; SM; 1.
PE 3: Inferred from homology;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..117
FT /note="Probable U6 snRNA-associated Sm-like protein LSm2"
FT /id="PRO_0000328006"
FT DOMAIN 2..76
FT /note="Sm"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
FT REGION 83..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 117 AA; 13582 MW; 5C2BAC511B66BDED CRC64;
MLFFSFYKSL VGKEITVELK NDLSITGLLQ SVDQFLNIKL KDIKVNEEDK YPYMISVKNC
FIRGSVVRYV HLPAEDVDVE TLQDHSRLEA REQKKQNKQH QEQTNQKSSN TTTTTTV
//
