ID F1KZG4_ASCSU Unreviewed; 130 AA.
AC F1KZG4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm4 {ECO:0000256|RuleBase:RU365049};
GN Name=LSM4 {ECO:0000256|RuleBase:RU365049};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY43268.1};
RN [1] {ECO:0000313|EMBL:ADY43268.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.
CC {ECO:0000256|RuleBase:RU365049}.
CC -!- SUBUNIT: LSm subunits form a heteromer with a doughnut shape.
CC {ECO:0000256|RuleBase:RU365049}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365049}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365049}.
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; JI168547; ADY43268.1; -; mRNA.
DR AlphaFoldDB; F1KZG4; -.
DR EnsemblMetazoa; AgR014X_g188_t01; AgR014X_g188_t01; AgR014X_g188.
DR EnsemblMetazoa; AgR014X_g188_t02; AgR014X_g188_t02; AgR014X_g188.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01723; LSm4; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR034101; Lsm4.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR23338; SMALL NUCLEAR RIBONUCLEOPROTEIN SM; 1.
DR PANTHER; PTHR23338:SF16; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM4; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS52002; SM; 1.
PE 2: Evidence at transcript level;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU365049};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU365049};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365049};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365049};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365049};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|RuleBase:RU365049}.
FT DOMAIN 3..76
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 86..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 130 AA; 14515 MW; C813E656E8883067 CRC64;
MVLPLSLLRT AQNHPMLVEL KNGETYNGHL VSCDAWMNIH LRDAICTSRD GDRFLKMPEV
YVRGSTIKYL RIPDDVVELV KDEVKEVRRQ QKDQQRAKRA MQGGSRGGGQ GGRGALRSGR
GGQQGRGRGK
//
