RU1C_CRYNJ
ID RU1C_CRYNJ Reviewed; 220 AA.
AC Q5KC16; Q55NM9;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
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 OrderedLocusNames=CNI00630;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017349; AAW45455.1; -; Genomic_DNA.
DR RefSeq; XP_572762.1; XM_572762.1.
DR AlphaFoldDB; Q5KC16; -.
DR SMR; Q5KC16; -.
DR STRING; 5207.AAW45455; -.
DR PaxDb; Q5KC16; -.
DR EnsemblFungi; AAW45455; AAW45455; CNI00630.
DR GeneID; 3259503; -.
DR KEGG; cne:CNI00630; -.
DR VEuPathDB; FungiDB:CNI00630; -.
DR eggNOG; KOG3454; Eukaryota.
DR HOGENOM; CLU_079697_1_0_1; -.
DR InParanoid; Q5KC16; -.
DR OMA; FLTHDST; -.
DR OrthoDB; 1537020at2759; -.
DR Proteomes; UP000002149; Chromosome 9.
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; 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..220
FT /note="U1 small nuclear ribonucleoprotein C"
FT /id="PRO_0000414287"
FT ZN_FING 4..36
FT /note="Matrin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT REGION 88..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 220 AA; 22904 MW; 10FFB00F24D26A99 CRC64;
MGKYYCDYCD IYLTHDSMNA RKAHNSGRNH VANVRDYFAG LGGNQAQSLI DQIIQQHESG
GRNQMMMAPS MRLGAGFMNP LATQPGYPGP PPPGAFPTFP PTAGTPPFRP PFPPSSAPGA
PPPTMPPFLP PNASAGAAPG IGMGSTPPFP PNTASPNPGM PPFRPPMGMG MPPAPAQAQA
QGSPMGMPQQ GQQGTFTPTQ EVPQGAGAGI HPDRLRMLGQ
