RU17_XENTR
ID RU17_XENTR Reviewed; 471 AA.
AC Q66II8; Q28IW1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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; ORFNames=TNeu055c14.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) 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. {ECO:0000250|UniProtKB:P08621}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q62376}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q62376}.
CC -!- DOMAIN: The RRM domain mediates interaction with U1 RNA.
CC {ECO:0000250|UniProtKB:P08621}.
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DR EMBL; CR760195; CAJ82715.1; -; mRNA.
DR EMBL; BC081331; AAH81331.1; -; mRNA.
DR RefSeq; NP_001268699.1; NM_001281770.1.
DR RefSeq; XP_012821930.1; XM_012966476.2.
DR RefSeq; XP_012821931.1; XM_012966477.2.
DR AlphaFoldDB; Q66II8; -.
DR SMR; Q66II8; -.
DR PaxDb; Q66II8; -.
DR DNASU; 493488; -.
DR Ensembl; ENSXETT00000049555; ENSXETP00000049555; ENSXETG00000022919.
DR GeneID; 493488; -.
DR KEGG; xtr:493488; -.
DR CTD; 6625; -.
DR Xenbase; XB-GENE-992818; snrnp70.
DR eggNOG; KOG0113; Eukaryota.
DR HOGENOM; CLU_045151_1_0_1; -.
DR InParanoid; Q66II8; -.
DR OMA; DFKLNEY; -.
DR OrthoDB; 1430110at2759; -.
DR PhylomeDB; Q66II8; -.
DR TreeFam; TF314215; -.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000022919; Expressed in gastrula and 24 other tissues.
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 mRNA processing; Nucleus; Reference proteome; Ribonucleoprotein;
KW RNA-binding.
FT CHAIN 1..471
FT /note="U1 small nuclear ribonucleoprotein 70 kDa"
FT /id="PRO_0000081883"
FT DOMAIN 103..184
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 48..78
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..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 57550 MW; 5BEB8A543985D96C CRC64;
MTQFLPPNLL ALFAPRDPVP YLPPLDKLPH EKHHNQPYCG IAPYIREFED PRDAPPPTRA
ETREERMERK RREKIERRQQ DVENELKIWD PHNDQNAQGD AFKTLFVARV NYDTTESKLR
REFEVYGPIK RIHMVYNKRS GKPRGYAFIE YEHERDMHSA YKHADGKKID GRRVLVDVER
GRTVKGWRPR RLGGGLGGTR RGGADVNIRH SGRDDTSRYD ERDRDRERER DRRERSRERD
KERERRRSRS RERRRRSRSR EKEERKRSRE RSRDKDKDKD KDKDKEKDKD KDRDRKRRSR
SRERKRERDR DREKKEDRVE GEVPESVDVP QDDAQTGDLG IDGIELKQEP EEKNRDRDRE
RDREKDRDKD RDRDRDRRRS HRDRERDKDR ERDRDRRRDR DRDRDRDRDH KRERDRGDRG
EKREERVPDN GMVMEQAEET SQDMYLDQES MQSGDGYLST ENGYMMEPPM E
