RU1C_BRAFL
ID RU1C_BRAFL Reviewed; 221 AA.
AC C3Z1P5;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 50.
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 ORFNames=BRAFLDRAFT_69314;
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82; TISSUE=Testis;
RX PubMed=18563158; DOI=10.1038/nature06967;
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG666573; EEN53412.1; -; Genomic_DNA.
DR RefSeq; XP_002597400.1; XM_002597354.1.
DR AlphaFoldDB; C3Z1P5; -.
DR SMR; C3Z1P5; -.
DR STRING; 7739.XP_002597400.1; -.
DR eggNOG; KOG3454; Eukaryota.
DR InParanoid; C3Z1P5; -.
DR OrthoDB; 1594407at2759; -.
DR Proteomes; UP000001554; Partially assembled WGS sequence.
DR GO; GO:0000243; C:commitment complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
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: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; 2.
DR Pfam; PF06220; zf-U1; 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..221
FT /note="U1 small nuclear ribonucleoprotein C"
FT /id="PRO_0000414256"
FT ZN_FING 4..36
FT /note="Matrin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT REGION 100..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 221 AA; 23324 MW; 173C248F85B4BDC1 CRC64;
MPKYFCDYCD TYLTHDSPSV RKTHCNGRKH KENVRVYYQK WMEEQAQQLI DQTTAAFQAG
KIPNNPFPNA AGQVGNEPGA KVLPPAILQA AAFQAGKIAS NPFPTSQAGP GPQGGGTMIP
PPPSLQGPGG PGSAPAPPRM PGPLLMTPPP GAAAPGMAPP GAPTLPQPAR GPILSVGAVM
GPRLCKHSYH INKALFLIKI HTLQKATQSQ LVVYKTVEKS K
