ID A0A2Y9RJ90_TRIMA Unreviewed; 194 AA.
AC A0A2Y9RJ90;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
GN Name=LOC101348284 {ECO:0000313|RefSeq:XP_023593641.1};
GN Synonyms=LSM1 {ECO:0000256|RuleBase:RU365047};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023593641.1};
RN [1] {ECO:0000313|RefSeq:XP_023593641.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_023593641.1; XM_023737873.1.
DR AlphaFoldDB; A0A2Y9RJ90; -.
DR STRING; 127582.A0A2Y9RJ90; -.
DR KEGG; tmu:101348284; -.
DR InParanoid; A0A2Y9RJ90; -.
DR OrthoDB; 1113423at2759; -.
DR Proteomes; UP000248480; Unplaced.
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:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:InterPro.
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:UP000248480};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365047};
KW RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT DOMAIN 66..141
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT COILED 154..181
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 194 AA; 22013 MW; 5AEC73DA9C3A7243 CRC64;
MTPHTPYYLY SAPHPTPSLR QSRSCGIHSW LEERGSRGLN TKNCSNSDLF GIPVLHFQLP
ADFLPRCPDS TSVSQTEKHL VLLRDGRTLI GFLRSIDQFA NLVLHQTVER IHVGKKYGDI
PRGIFVVRGE NVVLLGEIDL EKESDTPLQQ VSIEEILEEQ RVEQQTKLEA EKLKVQALKD
RGLSIPRADT LDEY
//