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Database: UniProt
Entry: G1P0U6_MYOLU
LinkDB: G1P0U6_MYOLU
Original site: G1P0U6_MYOLU 
ID   G1P0U6_MYOLU            Unreviewed;       133 AA.
AC   G1P0U6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   08-NOV-2023, entry version 59.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
GN   Name=LSM1 {ECO:0000256|RuleBase:RU365047,
GN   ECO:0000313|Ensembl:ENSMLUP00000003402.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000003402.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000003402.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000003402.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Plays a role in the degradation of histone mRNAs, the only
CC       eukaryotic mRNAs that are not polyadenylated. Probably also part of an
CC       LSm subunits-containing complex involved in the general process of mRNA
CC       degradation. {ECO:0000256|RuleBase:RU365047}.
CC   -!- SUBUNIT: Interacts with SLBP; interaction with SLBP occurs when histone
CC       mRNA is being rapidly degraded during the S phase. LSm subunits form a
CC       heteromer with a donut shape. {ECO:0000256|RuleBase:RU365047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365047}.
CC       Cytoplasm, P-body {ECO:0000256|RuleBase:RU365047}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC       {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365047}.
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DR   EMBL; AAPE02012467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_014309111.1; XM_014453625.1.
DR   AlphaFoldDB; G1P0U6; -.
DR   STRING; 59463.ENSMLUP00000003402; -.
DR   Ensembl; ENSMLUT00000003734.2; ENSMLUP00000003402.2; ENSMLUG00000003734.2.
DR   GeneID; 102420947; -.
DR   KEGG; mlf:102420947; -.
DR   CTD; 27257; -.
DR   eggNOG; KOG1782; Eukaryota.
DR   GeneTree; ENSGT00730000111133; -.
DR   HOGENOM; CLU_076902_0_1_1; -.
DR   InParanoid; G1P0U6; -.
DR   OMA; FMVRGEN; -.
DR   OrthoDB; 1113423at2759; -.
DR   TreeFam; TF105846; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0000339; F:RNA cap binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071044; P:histone mRNA catabolic process; IEA:Ensembl.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR   CDD; cd01728; LSm1; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR034104; Lsm1.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR044642; PTHR15588.
DR   InterPro; IPR047575; Sm.
DR   InterPro; IPR001163; Sm_dom_euk/arc.
DR   PANTHER; PTHR15588; LSM1; 1.
DR   PANTHER; PTHR15588:SF8; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM1; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS52002; SM; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|RuleBase:RU365047};
KW   mRNA processing {ECO:0000256|RuleBase:RU365047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|RuleBase:RU365047};
KW   RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT   DOMAIN          5..80
FT                   /note="Sm"
FT                   /evidence="ECO:0000259|PROSITE:PS52002"
FT   COILED          93..120
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   133 AA;  15222 MW;  F08973DA9447037A CRC64;
     MNYMPGTASL IEDIDKKHLV LLRDGRTLIG FLRSIDQFAN LVLHQTVERI HVGKKYGDIP
     RGIFVVRGEN VVLLGEIDLE KESDTPLQQV SIEEILEEQR VEQQTKLENE KLKVQALKDR
     GLSIPRADTL DEY
//
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