RSMB_NOTEU
ID RSMB_NOTEU Reviewed; 240 AA.
AC Q9N1Q0;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Small nuclear ribonucleoprotein-associated protein B';
DE Short=snRNP-B';
DE Short=snRPB';
DE AltName: Full=Sm protein B';
DE Short=Sm-B';
DE Short=SmB';
GN Name=SNRPB;
OS Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX NCBI_TaxID=9315;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10556313; DOI=10.1093/nar/27.23.4577;
RA Gray T.A., Smithwick M.J., Schaldach M.A., Martone D.L., Graves J.A.,
RA McCarrey J.R., Nicholls R.D.;
RT "Concerted regulation and molecular evolution of the duplicated SNRPB'/B
RT and SNRPN loci.";
RL Nucleic Acids Res. 27:4577-4584(1999).
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 (By similarity).
CC Component of both the pre-catalytic spliceosome B complex and activated
CC spliceosome C complexes (By similarity). Is also a component of the
CC minor U12 spliceosome (By similarity). As part of the U7 snRNP it is
CC involved in histone pre-mRNA 3'-end processing (By similarity).
CC {ECO:0000250|UniProtKB:P14678}.
CC -!- SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small
CC nuclear ribonucleoproteins (snRNPs), the building blocks of the
CC spliceosome (By similarity). Most spliceosomal snRNPs contain a common
CC set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and
CC SNRPG that assemble in a heptameric protein ring on the Sm site of the
CC small nuclear RNA to form the core snRNP (By similarity). Component of
CC the U1 snRNP (By similarity). The U1 snRNP is composed of the U1 snRNA
CC and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF
CC and SNRPG, and at least three U1 snRNP-specific proteins SNRNP70/U1-
CC 70K, SNRPA/U1-A and SNRPC/U1-C (By similarity). Component of the U4/U6-
CC U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least
CC PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB,
CC SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH,
CC SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7
CC and LSM8 (By similarity). Component of the U7 snRNP complex, or U7 Sm
CC protein core complex, that is composed of the U7 snRNA and at least
CC LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex does
CC not contain SNRPD1 and SNRPD2 (By similarity). Component of the U11/U12
CC snRNPs that are part of the U12-type spliceosome (By similarity). Part
CC of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3,
CC GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core
CC snRNPs assembly (By similarity). Forms a 6S pICln-Sm complex composed
CC of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like
CC structure where CLNS1A/pICln mimics additional Sm proteins and which is
CC unable to assemble into the core snRNP (By similarity). Identified in a
CC histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP,
CC SNRPB, SYNCRIP and YBX1 (By similarity). Interacts with TDRD3 and SNUPN
CC (By similarity). Interacts with PRMT5; interaction leads to its
CC symmetric arginine dimethylation (By similarity). Interacts with TDRD6;
CC interaction promotes association with PRMT5 (By similarity). Interacts
CC with SMN1; the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P14678, ECO:0000250|UniProtKB:P27048}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P14678}. Nucleus {ECO:0000250|UniProtKB:P14678}.
CC Note=SMN-mediated assembly into core snRNPs occurs in the cytosol
CC before SMN-mediated transport to the nucleus to be included in
CC spliceosomes. {ECO:0000250|UniProtKB:P14678}.
CC -!- PTM: Methylated by PRMT5 (By similarity). Arg-108 and Arg-112 are
CC dimethylated, probably to asymmetric dimethylarginine (By similarity).
CC {ECO:0000250|UniProtKB:P14678, ECO:0000250|UniProtKB:P27048}.
CC -!- SIMILARITY: Belongs to the snRNP SmB/SmN family. {ECO:0000305}.
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DR EMBL; AF176323; AAF40115.1; -; mRNA.
DR AlphaFoldDB; Q9N1Q0; -.
DR SMR; Q9N1Q0; -.
DR HOGENOM; CLU_076902_1_0_1; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0005687; C:U4 snRNP; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:UniProtKB.
DR GO; GO:0005683; C:U7 snRNP; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR017131; snRNP-assoc_SmB/SmN.
DR Pfam; PF01423; LSM; 1.
DR PIRSF; PIRSF037187; snRNP_SmB/SmN; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methylation; mRNA processing; mRNA splicing; Nucleus; Repeat;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..240
FT /note="Small nuclear ribonucleoprotein-associated protein
FT B'"
FT /id="PRO_0000249872"
FT REPEAT 175..181
FT REPEAT 191..196
FT REPEAT 216..221
FT REPEAT 222..228
FT REPEAT 230..236
FT REGION 161..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..236
FT /note="Repeat-rich region"
FT COMPBIAS 169..240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 108
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 108
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 112
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 112
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 112
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 147
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 172
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P63162"
SQ SEQUENCE 240 AA; 24625 MW; 4467772072F6071A CRC64;
MTVGKSSKML QHIDYRMRCI LQDGRIFIGT FKAFDKHMNL ILCDCDEFRK IKPKNSKQAE
REEKRVLGLV LLRGENLVSM TVEGPPPKDT GIARVPLSGA AGGPGIGRAA GRGVPAGVPM
PQAPAGLAGP VRGVGGPSQQ VMTPQGRGTV AAAAAAATAS IAGAPTQHPP GRGGPPPPMG
RGRPPPGMMA PPPGMRPPMG PPTGMPPGRG APMGIPPPGM RPPPPGMRGP PPPGMRPPRP
