SMD2_BOVIN
ID SMD2_BOVIN Reviewed; 118 AA.
AC Q3SZF8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Small nuclear ribonucleoprotein Sm D2;
DE Short=Sm-D2;
DE AltName: Full=snRNP core protein D2;
GN Name=SNRPD2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. Is also a component of the minor U12 spliceosome.
CC {ECO:0000250|UniProtKB:P62316}.
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 U11/U12 snRNPs that
CC are part of the U12-type spliceosome. 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 with SMN1; the interaction is direct. Interacts with
CC GEMIN2; the interaction is direct. Interacts with SNRPD1; the
CC interaction is direct. Interacts with SNRPF; the interaction is direct.
CC {ECO:0000250|UniProtKB:P62316}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P62316}. Nucleus {ECO:0000250|UniProtKB:P62316}.
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:P62316}.
CC -!- SIMILARITY: Belongs to the snRNP core protein family. {ECO:0000305}.
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DR EMBL; BC102877; AAI02878.1; -; mRNA.
DR RefSeq; NP_001029648.1; NM_001034476.2.
DR AlphaFoldDB; Q3SZF8; -.
DR SMR; Q3SZF8; -.
DR STRING; 9913.ENSBTAP00000016153; -.
DR PaxDb; Q3SZF8; -.
DR PRIDE; Q3SZF8; -.
DR Ensembl; ENSBTAT00000016153; ENSBTAP00000016153; ENSBTAG00000012177.
DR GeneID; 514932; -.
DR KEGG; bta:514932; -.
DR CTD; 6633; -.
DR VEuPathDB; HostDB:ENSBTAG00000012177; -.
DR VGNC; VGNC:35079; SNRPD2.
DR eggNOG; KOG3459; Eukaryota.
DR GeneTree; ENSGT00390000017608; -.
DR HOGENOM; CLU_076902_2_1_1; -.
DR InParanoid; Q3SZF8; -.
DR OMA; PKTEMSQ; -.
DR OrthoDB; 1581611at2759; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000012177; Expressed in semen and 108 other tissues.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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:0034715; C:pICln-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
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:0005682; C:U5 snRNP; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR CDD; cd01720; Sm_D2; 1.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR027248; Sm_D2.
DR PANTHER; PTHR12777; PTHR12777; 1.
DR Pfam; PF01423; LSM; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 3: Inferred from homology;
KW Acetylation; Cytoplasm; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62316"
FT CHAIN 2..118
FT /note="Small nuclear ribonucleoprotein Sm D2"
FT /id="PRO_0000244611"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P62316"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62316"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62316"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62316"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62316"
SQ SEQUENCE 118 AA; 13527 MW; D986059D82B7E045 CRC64;
MSLLNKPKSE MTPEELQKRE EEEFNTGPLS VLTQSVKNNT QVLINCRNNK KLLGRVKAFD
RHCNMVLENV KEMWTEVPKS GKGKKKSKPV NKDRYISKMF LRGDSVIVVL RNPLIAGK
