ID   RU17_XENLA              Reviewed;         471 AA.
AC   P09406;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 96.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2468488; DOI=10.1002/j.1460-2075.1988.tb03330.x;
RA   Etzerodt M., Vignali R., Scherly D., Mattaj I.W., Ciliberto G.,
RA   Philipson L.;
RT   "Structure and expression of a Xenopus gene encoding an snRNP protein (U1
RT   70K).";
RL   EMBO J. 7:4311-4321(1988).
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; X12430; CAA30972.1; -; mRNA.
DR   PIR; S02016; S02016.
DR   AlphaFoldDB; P09406; -.
DR   SMR; P09406; -.
DR   PRIDE; P09406; -.
DR   Proteomes; UP000186698; Genome assembly.
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:0003723; F:RNA binding; ISS:UniProtKB.
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_0000081882"
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..205
FT                   /note="Required for interaction with U1 RNA"
FT                   /evidence="ECO:0000250|UniProtKB:P08621"
FT   REGION          190..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..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;  57204 MW;  959A8BB3064C3FC3 CRC64;
     MTQFLPPNLL ALFAPRDPVP YLPPLDKLPH EKHHNQPYCG IAPYIREFED PRDAPPPTRA
     ETREERMERK RREKIERRQQ DVENELKIWD PHNDQNAQGD AFKTLFVARV NYDTTESKLR
     REFEVYGPIK RIHIVYNKGS EGSGKPRGYA FIEYEHERDM HSAYKHADGK KIDGRRVLVD
     VERGRTVKGW RPRRLGGGLG GTRRGGADVN IRHSGRDDTS RYDERDRERE RDRRERSRER
     EKEPRERRRS RSRERRRKSR SREKEERKRT REKSKDKDKE KDKDNKDRDR KRRSRSRERK
     RERDRDREKK EERVEAEVPE ADDAPQDDAQ IGDLGIDGIE LKQEPEEKSR ERDRERDRDR
     EKGEKDRDKD RDRDRDRRRS HRDRDREKDR DRDRDRRRDR DRDRERDKDH KRERDRGDRS
     EKREERVPDN GMVMEQAEET SQDMYLDQES MQSGDGYLST ENGYMMEPPM E