RU17_BOVIN
ID RU17_BOVIN Reviewed; 439 AA.
AC Q1RMR2;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=U1 small nuclear ribonucleoprotein 70 kDa;
DE Short=U1 snRNP 70 kDa;
DE Short=U1-70K;
DE Short=snRNP70;
GN Name=SNRNP70; Synonyms=SNRP70;
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=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the spliceosomal U1 snRNP, which is essential
CC for recognition of the pre-mRNA 5' splice-site and the subsequent
CC assembly of the spliceosome. SNRNP70 binds to the loop I region of U1-
CC snRNA. {ECO:0000250|UniProtKB:P08621}.
CC -!- SUBUNIT: Component of the U1 snRNP. The U1 snRNP is composed of the U1
CC snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm
CC site of the small nuclear RNA to form the core snRNP, and at least
CC three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and
CC SNRPC/U1-C (By similarity). Interacts with SCNM1 (By similarity). Found
CC in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRNP70, SNRPA1,
CC SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE)
CC complex with SNRNP70, SNRPA1, SRRM1 and TRA2B/SFRS10. Interacts with
CC dephosphorylated SFRS13A and SFPQ. Interacts with NUDT21/CPSF5, CPSF6,
CC SCAF11, and ZRANB2. Interacts with GEMIN5 (By similarity). Interacts
CC with FUS (By similarity). {ECO:0000250|UniProtKB:P08621,
CC ECO:0000250|UniProtKB:Q62376}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q62376}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q62376}. Note=Colocalizes
CC with SCNM1 and LUC7L2 in nuclear speckles.
CC {ECO:0000250|UniProtKB:Q62376}.
CC -!- DOMAIN: The RRM domain mediates interaction with U1 RNA.
CC {ECO:0000250|UniProtKB:P08621}.
CC -!- PTM: Extensively phosphorylated on serine residues in the C-terminal
CC region. {ECO:0000250|UniProtKB:P08621}.
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DR EMBL; BC114762; AAI14763.1; -; mRNA.
DR RefSeq; NP_001069514.1; NM_001076046.2.
DR AlphaFoldDB; Q1RMR2; -.
DR SMR; Q1RMR2; -.
DR PaxDb; Q1RMR2; -.
DR PRIDE; Q1RMR2; -.
DR GeneID; 535113; -.
DR KEGG; bta:535113; -.
DR CTD; 6625; -.
DR eggNOG; KOG0113; Eukaryota.
DR HOGENOM; CLU_045151_1_0_1; -.
DR InParanoid; Q1RMR2; -.
DR OrthoDB; 1430110at2759; -.
DR TreeFam; TF314215; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0017069; F:snRNA binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR CDD; cd12236; RRM_snRNP70; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034143; snRNP70_RRM.
DR InterPro; IPR022023; U1snRNP70_N.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF12220; U1snRNP70_N; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT CHAIN 2..439
FT /note="U1 small nuclear ribonucleoprotein 70 kDa"
FT /id="PRO_0000259962"
FT DOMAIN 103..181
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 48..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..202
FT /note="Required for interaction with U1 RNA"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT REGION 187..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT MOD_RES 126
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT CROSSLNK 349
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08621"
SQ SEQUENCE 439 AA; 51426 MW; 1A0A49B1266FFC60 CRC64;
MTQFLPPNLL ALFAPRDPIP YLPPLEKLPH EKHHNQPYCG IAPYIREFED PRDAPPPTRA
ETREERMERK RREKIERRQQ EVETELKMWD PHNDPNAQGD AFKTLFVARV NYDTTESKLR
REFEVYGPIK RIHMVYSKRS GKPRGYAFIE YEHERDMHSA YKHADGKKID GRRVLVDVER
GRTVKGWRPR RLGGGLGGTR RGGADVNIRH SGRDDTSRYD ERPGPSPLPH RDRDRDRERE
RRERSRERDK ERERRRSRSR DRRRRSRSRD KEERRRSRER SKDKDRDRKR RSSRSRERAR
RERERKEELR GGGGGGGDMA EPSEAGDAPP DDGPPGELGP DGPDGPEEKG RDRDRDRRRS
HRSERERRRD RDRDRDREHK RGERGGDRGR DEARGGGGGG QDNGLEGLGN DGRDMYMESE
GGDGYLAPEN GYLMEAAPE
