RU1C_MOUSE
ID RU1C_MOUSE Reviewed; 159 AA.
AC Q62241;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
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}; Synonyms=Snrp1c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphocyte;
RX PubMed=9031639; DOI=10.1016/s0378-1119(96)00612-9;
RA Nelissen R.L.H., Klein Gunnewiek J.M.T., Lambermon M.H.L.,
RA van Venrooij W.J.;
RT "Cloning and characterization of two processed pseudogenes and the cDNA for
RT the murine U1 snRNP-specific protein C.";
RL Gene 184:273-278(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Kidney, and Testis;
RX PubMed=9094092;
RX DOI=10.1002/(sici)1098-2795(199704)46:4<459::aid-mrd3>3.0.co;2-n;
RA Morales C.R., Leyne M., El-Alfy M., Oko R.;
RT "Molecular cloning and developmental expression of a small ribonuclear
RT protein in the mouse testis.";
RL Mol. Reprod. Dev. 46:459-470(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
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 (By similarity). Interacts (via N-terminus) with TIA1 (via C-
CC terminus); thereby promoting spliceosomal U1 snRNP recruitment to 5'
CC splice sites (By similarity). {ECO:0000250|UniProtKB:P09234,
CC ECO:0000255|HAMAP-Rule:MF_03153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03153}.
CC -!- TISSUE SPECIFICITY: Widely expressed. In the testis, expressed in
CC somatic and germinal testicular cells but not in elongated spermatids.
CC -!- DEVELOPMENTAL STAGE: First detected in the testis 18 days after birth.
CC Levels increase successively between days 21-28. On day 42, levels
CC decrease.
CC -!- SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C family.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
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DR EMBL; X96767; CAA65542.1; -; mRNA.
DR EMBL; U70315; AAB08894.1; -; mRNA.
DR EMBL; BC008243; AAH08243.1; -; mRNA.
DR CCDS; CCDS28570.1; -.
DR RefSeq; NP_035562.1; NM_011432.2.
DR AlphaFoldDB; Q62241; -.
DR SMR; Q62241; -.
DR BioGRID; 203373; 23.
DR IntAct; Q62241; 2.
DR STRING; 10090.ENSMUSP00000063976; -.
DR iPTMnet; Q62241; -.
DR PhosphoSitePlus; Q62241; -.
DR EPD; Q62241; -.
DR jPOST; Q62241; -.
DR MaxQB; Q62241; -.
DR PaxDb; Q62241; -.
DR PRIDE; Q62241; -.
DR ProteomicsDB; 256843; -.
DR Antibodypedia; 45711; 71 antibodies from 21 providers.
DR DNASU; 20630; -.
DR Ensembl; ENSMUST00000071006; ENSMUSP00000063976; ENSMUSG00000024217.
DR Ensembl; ENSMUST00000232873; ENSMUSP00000156707; ENSMUSG00000024217.
DR GeneID; 20630; -.
DR KEGG; mmu:20630; -.
DR UCSC; uc008bps.1; mouse.
DR CTD; 6631; -.
DR MGI; MGI:109489; Snrpc.
DR VEuPathDB; HostDB:ENSMUSG00000024217; -.
DR eggNOG; KOG3454; Eukaryota.
DR GeneTree; ENSGT00730000110997; -.
DR HOGENOM; CLU_079697_3_0_1; -.
DR InParanoid; Q62241; -.
DR OMA; FLTHDST; -.
DR OrthoDB; 1594407at2759; -.
DR PhylomeDB; Q62241; -.
DR TreeFam; TF313578; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 20630; 18 hits in 74 CRISPR screens.
DR ChiTaRS; Snrpc; mouse.
DR PRO; PR:Q62241; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q62241; protein.
DR Bgee; ENSMUSG00000024217; Expressed in embryonic brain and 74 other tissues.
DR ExpressionAtlas; Q62241; baseline and differential.
DR Genevisible; Q62241; MM.
DR GO; GO:0015030; C:Cajal body; ISO:MGI.
DR GO; GO:0000243; C:commitment complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
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:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
DR GO; GO:0030619; F:U1 snRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:1990446; F:U1 snRNP binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISO:MGI.
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 Acetylation; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..159
FT /note="U1 small nuclear ribonucleoprotein C"
FT /id="PRO_0000097526"
FT ZN_FING 4..36
FT /note="Matrin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT REGION 62..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..96
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09234"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09234"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09234"
SQ SEQUENCE 159 AA; 17364 MW; F187E13A75B789D0 CRC64;
MPKFYCDYCD TYLTHDSPSV RKTHCSGRKH KENVKDYYQK WMEEQAQSLI DKTTAAFQQG
KIPPAPFSAP PPAGAMIPPP PSLPGPPRPG MMPAPHMGGP PMMPMMGPPP PGMMPVGPAP
GMRPPMGGHM PMMPGPPMMR PPARPMMVPT RPGMTRPDR
