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RU1C_PLAYO
ID   RU1C_PLAYO              Reviewed;         201 AA.
AC   Q7RNM5;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=PY01791;
OS   Plasmodium yoelii yoelii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=73239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17XNL;
RX   PubMed=12368865; DOI=10.1038/nature01099;
RA   Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA   Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA   Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA   Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA   Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D.,
RA   Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W.,
RA   Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA   Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA   Carucci D.J.;
RT   "Genome sequence and comparative analysis of the model rodent malaria
RT   parasite Plasmodium yoelii yoelii.";
RL   Nature 419:512-519(2002).
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}.
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DR   EMBL; AABL01000484; EAA21158.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7RNM5; -.
DR   SMR; Q7RNM5; -.
DR   EnsemblProtists; EAA21158; EAA21158; EAA21158.
DR   InParanoid; Q7RNM5; -.
DR   OMA; NPMMNNF; -.
DR   Proteomes; UP000008553; Unassembled WGS sequence.
DR   GO; GO:0000243; C:commitment complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005685; C:U1 snRNP; IEA:UniProtKB-UniRule.
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..201
FT                   /note="U1 small nuclear ribonucleoprotein C"
FT                   /id="PRO_0000414278"
FT   ZN_FING         4..36
FT                   /note="Matrin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT   REGION          137..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   201 AA;  23897 MW;  53381503B2CCB349 CRC64;
     MPKYYCEYCD IYLTHSSPVG RRQHNQGRKH ISAKIEYFQN LLREEGITPQ NFLGFLGNQG
     YNNALANPMM NNFMPGNYNA YMKYNPMRNY HHSNRNPNYQ HSIGMHNNKY SRAGYVPPGS
     NKYPNNHFHN NKRINNIQKP YNNFDNKNNN YNNKPITNSS YKNDKQDYRN NNENNDNMNS
     NHFSNYQMNK ENANFVNKNN E
 
 
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