ID L5M1R2_MYODS Unreviewed; 221 AA.
AC L5M1R2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D1 {ECO:0000256|RuleBase:RU365054};
DE AltName: Full=snRNP core protein D1 {ECO:0000256|RuleBase:RU365054};
GN Name=SNRPD1 {ECO:0000256|RuleBase:RU365054};
GN ORFNames=MDA_GLEAN10025312 {ECO:0000313|EMBL:ELK31648.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK31648.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- FUNCTION: Plays a role in pre-mRNA splicing as a core component of the
CC spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins
CC (snRNPs), the building blocks of the spliceosome. Component of both the
CC pre-catalytic spliceosome B complex and activated spliceosome C
CC complexes. As a component of the minor spliceosome, involved in the
CC splicing of U12-type introns in pre-mRNAs. May act as a charged protein
CC scaffold to promote snRNP assembly or strengthen snRNP-snRNP
CC interactions through non-specific electrostatic contacts with RNA.
CC {ECO:0000256|RuleBase:RU365054}.
CC -!- SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small
CC nuclear ribonucleoproteins (snRNPs), the building blocks of the
CC spliceosome. Most spliceosomal snRNPs contain a common set of Sm
CC proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that
CC assemble in a heptameric protein ring on the Sm site of the small
CC nuclear RNA to form the core snRNP. Component of the U1 snRNP. The U1
CC snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB,
CC SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1
CC snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C.
CC Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and
CC U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200,
CC TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG,
CC DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3,
CC LSM4, LSM5, LSM6, LSM7 and LSM8. Component of the minor spliceosome,
CC which splices U12-type introns. Part of the SMN-Sm complex that
CC contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6,
CC GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2,
CC SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a
CC 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE,
CC SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics
CC additional Sm proteins and which is unable to assemble into the core
CC snRNP. Interacts (via C-terminus) with SMN1 (via Tudor domain); the
CC interaction is direct. Interacts with GEMIN2; the interaction is
CC direct. Interacts with SNRPD2; the interaction is direct.
CC {ECO:0000256|RuleBase:RU365054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|RuleBase:RU365054}. Nucleus
CC {ECO:0000256|RuleBase:RU365054}. Note=SMN-mediated assembly into core
CC snRNPs occurs in the cytosol before SMN-mediated transport to the
CC nucleus to be included in spliceosomes.
CC {ECO:0000256|RuleBase:RU365054}.
CC -!- SIMILARITY: Belongs to the snRNP core protein family.
CC {ECO:0000256|ARBA:ARBA00008146, ECO:0000256|RuleBase:RU365054}.
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DR EMBL; KB105967; ELK31648.1; -; Genomic_DNA.
DR AlphaFoldDB; L5M1R2; -.
DR eggNOG; KOG3428; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:UniProtKB-UniRule.
DR CDD; cd01724; Sm_D1; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR034102; Sm_D1.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR23338; SMALL NUCLEAR RIBONUCLEOPROTEIN SM; 1.
DR PANTHER; PTHR23338:SF18; SMALL NUCLEAR RIBONUCLEOPROTEIN SM D1; 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 Cytoplasm {ECO:0000256|RuleBase:RU365054};
KW mRNA processing {ECO:0000256|RuleBase:RU365054};
KW mRNA splicing {ECO:0000256|RuleBase:RU365054};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365054};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU365054}.
FT DOMAIN 104..176
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 189..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..221
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 221 AA; 23976 MW; F1AAFB87009793E7 CRC64;
MDQKSALVSI SLDEATAVVA KCPQQLQVTP PATRARCGAP RGRKGVRPSA ASAFPLCVRS
APRALYVGGP GGGVSGHSYS VPVVEVVRFC ALSDRNLEIF FRMKLVRFLM KLSHETVTIE
LKNGTQVHGT ITGVDVSMNT HLKAVKMTLK NREPVQLETL SIRGNNIRYF ILPDSLPLDT
LLVDVEPKVK SKKREAVAGR GRGRGRGRGR GRGRGRGGPR R
//