RU1C_DROME
ID RU1C_DROME Reviewed; 145 AA.
AC Q9VE17;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
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=snRNP-U1-C {ECO:0000255|HAMAP-Rule:MF_03153}; ORFNames=CG5454;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION IN THE U1 SNRNP COMPLEX, AND PROTEIN SEQUENCE OF 35-51.
RX PubMed=11333025; DOI=10.1017/s1355838201001327;
RA Labourier E., Rio D.C.;
RT "Purification of Drosophila snRNPs and characterization of two populations
RT of functional U1 particles.";
RL RNA 7:457-470(2001).
RN [5]
RP IDENTIFICATION IN THE U1 SNRNP COMPLEX.
RX PubMed=1834995; DOI=10.1093/nar/19.21.5877;
RA Paterson T., Beggs J.D., Finnegan D.J., Luehrmann R.;
RT "Polypeptide components of Drosophila small nuclear ribonucleoprotein
RT particles.";
RL Nucleic Acids Res. 19:5877-5882(1991).
RN [6]
RP FUNCTION.
RX PubMed=15492211; DOI=10.1073/pnas.0407004101;
RA Park J.W., Parisky K., Celotto A.M., Reenan R.A., Graveley B.R.;
RT "Identification of alternative splicing regulators by RNA interference in
RT Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15974-15979(2004).
RN [7]
RP FUNCTION.
RX PubMed=19218244; DOI=10.1074/jbc.m809506200;
RA Katzenberger R.J., Marengo M.S., Wassarman D.A.;
RT "Control of alternative splicing by signal-dependent degradation of
RT splicing-regulatory proteins.";
RL J. Biol. Chem. 284:10737-10746(2009).
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. U1-C is directly involved in initial 5'
CC splice-site recognition for both constitutive and regulated alternative
CC splicing. The interaction with the 5' splice-site seems to precede
CC 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 (By
CC similarity). Regulates alternative splicing of a distinct group of
CC target genes. {ECO:0000255|HAMAP-Rule:MF_03153,
CC ECO:0000269|PubMed:15492211, ECO:0000269|PubMed:19218244}.
CC -!- SUBUNIT: U1 snRNP is composed of the 7 core Sm proteins B/B', D1, D2,
CC D3, E, F and G 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 U1-70K, U1-A and U1-C. U1-C interacts with U1
CC snRNA and the 5' splice-site region of the pre-mRNA.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03153}.
CC -!- SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C family.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
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DR EMBL; AE014297; AAF55616.1; -; Genomic_DNA.
DR EMBL; BT003460; AAO39463.1; -; mRNA.
DR RefSeq; NP_650767.1; NM_142510.3.
DR AlphaFoldDB; Q9VE17; -.
DR BioGRID; 67277; 8.
DR IntAct; Q9VE17; 16.
DR STRING; 7227.FBpp0083134; -.
DR PaxDb; Q9VE17; -.
DR PRIDE; Q9VE17; -.
DR DNASU; 42274; -.
DR EnsemblMetazoa; FBtr0083720; FBpp0083134; FBgn0261792.
DR GeneID; 42274; -.
DR KEGG; dme:Dmel_CG5454; -.
DR UCSC; CG5454-RA; d. melanogaster.
DR CTD; 42274; -.
DR FlyBase; FBgn0261792; snRNP-U1-C.
DR VEuPathDB; VectorBase:FBgn0261792; -.
DR eggNOG; KOG3454; Eukaryota.
DR GeneTree; ENSGT01030000234866; -.
DR HOGENOM; CLU_079697_3_1_1; -.
DR InParanoid; Q9VE17; -.
DR OMA; FLTHDST; -.
DR OrthoDB; 1551234at2759; -.
DR PhylomeDB; Q9VE17; -.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9VE17; -.
DR BioGRID-ORCS; 42274; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42274; -.
DR PRO; PR:Q9VE17; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0261792; Expressed in eye disc (Drosophila) and 36 other tissues.
DR ExpressionAtlas; Q9VE17; baseline and differential.
DR Genevisible; Q9VE17; DM.
DR GO; GO:0000243; C:commitment complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IDA:FlyBase.
DR GO; GO:0005685; C:U1 snRNP; ISS:FlyBase.
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:0000398; P:mRNA splicing, via spliceosome; ISS:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase.
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 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..145
FT /note="U1 small nuclear ribonucleoprotein C"
FT /id="PRO_0000414261"
FT ZN_FING 4..36
FT /note="Matrin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT REGION 67..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..91
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 145 AA; 15760 MW; 3068A1248ABEB02E CRC64;
MPKYYCDYCD TYLTHDSPSV RKTHCTGRKH RDNVKFYYQK WMEEQAQHLI DATTAAFKAG
KITNNPFAGG PGGAPPKPAG VSIPPPNMGA PPRPGMPGMP YMPPLMNPMM GMRPPPIMNP
MAMMGPPPPL GTIPGVRPGI MNGPK
