RU1C_DANRE
ID RU1C_DANRE Reviewed; 159 AA.
AC Q8JGS0;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=U1 small nuclear ribonucleoprotein C {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1 snRNP C {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1-C {ECO:0000255|HAMAP-Rule:MF_03153};
DE Short=U1C {ECO:0000255|HAMAP-Rule:MF_03153};
GN Name=snrpc {ECO:0000255|HAMAP-Rule:MF_03153};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=12006978; DOI=10.1038/ng896;
RA Golling G., Amsterdam A., Sun Z., Antonelli M., Maldonado E., Chen W.,
RA Burgess S., Haldi M., Artzt K., Farrington S., Lin S.-Y., Nissen R.M.,
RA Hopkins N.;
RT "Insertional mutagenesis in zebrafish rapidly identifies genes essential
RT for early vertebrate development.";
RL Nat. Genet. 31:135-140(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21468032; DOI=10.1038/emboj.2011.106;
RA Roesel T.D., Hung L.-H., Medenbach J., Donde K., Starke S., Benes V.,
RA Raetsch G., Bindereif A.;
RT "RNA-Seq analysis in mutant zebrafish reveals role of U1C protein in
RT alternative splicing regulation.";
RL EMBO J. 30:1965-1976(2011).
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. snrpc/U1-C is directly involved in initial
CC 5' splice-site recognition for both constitutive and regulated
CC alternative splicing. The interaction with the 5' splice-site seems to
CC precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates
CC commitment or early (E) complex formation by stabilizing the base
CC pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
CC {ECO:0000255|HAMAP-Rule:MF_03153, ECO:0000269|PubMed:12006978,
CC ECO:0000269|PubMed:21468032}.
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 3 U1
CC snRNP-specific proteins snrnp70/U1-70K, snrpa/U1-A and snrpc/U1-C.
CC snrpc/U1-C interacts with U1 snRNA and the 5' splice-site region of the
CC pre-mRNA. {ECO:0000255|HAMAP-Rule:MF_03153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03153}.
CC -!- DISRUPTION PHENOTYPE: Still contains stable, but U1-C-deficient U1
CC snRNPs. Changes the alternative splicing patterns of a large set of
CC specific target genes. Results in an early embryonic lethality at about
CC 5 days post-fertilization. {ECO:0000269|PubMed:21468032}.
CC -!- SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C family.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
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DR EMBL; AY099526; AAM28214.1; -; mRNA.
DR EMBL; CR847944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC091442; AAH91442.1; -; mRNA.
DR RefSeq; NP_775358.1; NM_173251.2.
DR AlphaFoldDB; Q8JGS0; -.
DR SMR; Q8JGS0; -.
DR STRING; 7955.ENSDARP00000010253; -.
DR PaxDb; Q8JGS0; -.
DR Ensembl; ENSDART00000017230; ENSDARP00000010253; ENSDARG00000009871.
DR GeneID; 192330; -.
DR KEGG; dre:192330; -.
DR CTD; 6631; -.
DR ZFIN; ZDB-GENE-020419-26; snrpc.
DR eggNOG; KOG3454; Eukaryota.
DR GeneTree; ENSGT00730000110997; -.
DR HOGENOM; CLU_079697_3_0_1; -.
DR InParanoid; Q8JGS0; -.
DR OMA; FLTHDST; -.
DR OrthoDB; 1594407at2759; -.
DR TreeFam; TF313578; -.
DR Reactome; R-DRE-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q8JGS0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000009871; Expressed in mature ovarian follicle and 28 other tissues.
DR ExpressionAtlas; Q8JGS0; baseline and differential.
DR GO; GO:0000243; C:commitment complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR GO; GO:0071004; C:U2-type prespliceosome; IEA:UniProtKB-UniRule.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030627; F:pre-mRNA 5'-splice site binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:ZFIN.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03153; U1_C; 1.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR013085; U1-CZ_Znf_C2H2.
DR InterPro; IPR017340; U1_snRNP-C.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR31148; PTHR31148; 1.
DR Pfam; PF06220; zf-U1; 1.
DR PIRSF; PIRSF037969; U1_snRNP-C; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Zinc; Zinc-finger.
FT CHAIN 1..159
FT /note="U1 small nuclear ribonucleoprotein C"
FT /id="PRO_0000414254"
FT ZN_FING 4..36
FT /note="Matrin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT REGION 61..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 159 AA; 17286 MW; 735CA9D2144466D3 CRC64;
MPKFYCDYCD TYLTHDSPSV RKTHCSGRKH KENVKDYYQK WMEEQAQSLI DKTTAAFQQG
KIPPTPFPGA PPPGGSLLPH PSIGGPPRPG MLPAPPMGGP PMMPMMGPPP HAMMPGGPGP
GMRPPMGGPM QMMPGPHMMR PPARPMMPAV RPGMVRPDR
