RU1C_POLPP
ID RU1C_POLPP Reviewed; 141 AA.
AC D3B3B7;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 41.
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}; ORFNames=PPL_02883;
OS Polysphondylium pallidum (strain ATCC 26659 / Pp 5 / PN500) (Heterostelium
OS pallidum).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Acytosteliales;
OC Acytosteliaceae; Heterostelium.
OX NCBI_TaxID=670386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26659 / Pp 5 / PN500;
RX PubMed=21757610; DOI=10.1101/gr.121137.111;
RA Heidel A.J., Lawal H.M., Felder M., Schilde C., Helps N.R., Tunggal B.,
RA Rivero F., John U., Schleicher M., Eichinger L., Platzer M., Noegel A.A.,
RA Schaap P., Gloeckner G.;
RT "Phylogeny-wide analysis of social amoeba genomes highlights ancient
RT origins for complex intercellular communication.";
RL Genome Res. 21:1882-1891(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}.
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 -!- SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C family.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
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DR EMBL; ADBJ01000010; EFA83815.1; -; Genomic_DNA.
DR AlphaFoldDB; D3B3B7; -.
DR SMR; D3B3B7; -.
DR STRING; 670386.D3B3B7; -.
DR InParanoid; D3B3B7; -.
DR OMA; CSIYLTH; -.
DR OrthoDB; 1594407at2759; -.
DR Proteomes; UP000001396; Unassembled WGS sequence.
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: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; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Metal-binding; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Zinc; Zinc-finger.
FT CHAIN 1..141
FT /note="U1 small nuclear ribonucleoprotein C"
FT /id="PRO_0000414268"
FT ZN_FING 4..36
FT /note="Matrin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT REGION 69..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 141 AA; 16030 MW; 786F6613EFC66B5A CRC64;
MPKYYCEYCD KYLTHDSPSV RKSHTIGKVH QQAVTLYYKQ FEAEWFKSQM QQKGGQVPMM
PPFGMQPGLL PPNMVPGQFN IPMMPPGQFP FPPPPGQPMG GMPPHQQQPM SFNPHHPYPP
PHLQQSAQQF NSNSPPSNND Q