RU1C_YEAST
ID RU1C_YEAST Reviewed; 231 AA.
AC Q05900; D6VYU2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
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=YHC1 {ECO:0000255|HAMAP-Rule:MF_03153}; OrderedLocusNames=YLR298C;
GN ORFNames=L8003.21;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP IDENTIFICATION, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=9012791; DOI=10.1073/pnas.94.2.385;
RA Neubauer G., Gottschalk A., Fabrizio P., Seraphin B., Luehrmann R.,
RA Mann M.;
RT "Identification of the proteins of the yeast U1 small nuclear
RT ribonucleoprotein complex by mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:385-390(1997).
RN [5]
RP FUNCTION.
RX PubMed=9233817; DOI=10.1093/emboj/16.13.4082;
RA Tang J., Abovich N., Fleming M.L., Seraphin B., Rosbash M.;
RT "Identification and characterization of a yeast homolog of U1 snRNP-
RT specific protein C.";
RL EMBO J. 16:4082-4091(1997).
RN [6]
RP IDENTIFICATION IN THE U1 SNRNP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9630245;
RA Gottschalk A., Tang J., Puig O., Salgado J., Neubauer G., Colot H.V.,
RA Mann M., Seraphin B., Rosbash M., Luehrmann R., Fabrizio P.;
RT "A comprehensive biochemical and genetic analysis of the yeast U1 snRNP
RT reveals five novel proteins.";
RL RNA 4:374-393(1998).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10072386; DOI=10.1101/gad.13.5.581;
RA Zhang D., Rosbash M.;
RT "Identification of eight proteins that cross-link to pre-mRNA in the yeast
RT commitment complex.";
RL Genes Dev. 13:581-592(1999).
RN [8]
RP MUTAGENESIS OF LEU-13.
RX PubMed=11172727; DOI=10.1016/s1097-2765(01)00170-8;
RA Chen J.Y.-F., Stands L., Staley J.P., Jackups R.R. Jr., Latus L.J.,
RA Chang T.-H.;
RT "Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate
RT the requirement of Prp28p, an essential DEAD box splicing factor.";
RL Mol. Cell 7:227-232(2001).
RN [9]
RP FUNCTION.
RX PubMed=12214237; DOI=10.1038/nature00947;
RA Du H., Rosbash M.;
RT "The U1 snRNP protein U1C recognizes the 5' splice site in the absence of
RT base pairing.";
RL Nature 419:86-90(2002).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP MUTAGENESIS OF LEU-13.
RX PubMed=15465910; DOI=10.1073/pnas.0406319101;
RA Du H., Tardiff D.F., Moore M.J., Rosbash M.;
RT "Effects of the U1C L13 mutation and temperature regulation of yeast
RT commitment complex formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14841-14846(2004).
RN [13]
RP IDENTIFICATION IN THE U1 SNRNP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19941820; DOI=10.1016/j.molcel.2009.09.040;
RA Fabrizio P., Dannenberg J., Dube P., Kastner B., Stark H., Urlaub H.,
RA Luhrmann R.;
RT "The evolutionarily conserved core design of the catalytic activation step
RT of the yeast spliceosome.";
RL Mol. Cell 36:593-608(2009).
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. YHC1/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:0000269|PubMed:10072386, ECO:0000269|PubMed:12214237,
CC ECO:0000269|PubMed:9233817}.
CC -!- SUBUNIT: U1 snRNP is composed of the 7 core Sm proteins SMB1, SMD1,
CC SMD2, SMD3, SME1, SMX3 and SMX2 (Sm proteins B, D1, D2, D3, E, F and G,
CC respectively) that assemble in a heptameric protein ring on the Sm site
CC of the small nuclear RNA to form the core snRNP, and at least 10 U1
CC snRNP-specific proteins SNP1/U1-70K, MUD1/U1-A, YHC1/U1-C, LUC7, NAM8,
CC PRP39, PRP40, PRP42, SNU56 and SNU71. YHC1/U1-C interacts with U1 snRNA
CC and the 5' splice-site region of the pre-mRNA.
CC {ECO:0000269|PubMed:10072386, ECO:0000269|PubMed:19941820,
CC ECO:0000269|PubMed:9630245}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03153,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2140 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C family.
CC {ECO:0000255|HAMAP-Rule:MF_03153}.
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DR EMBL; U17243; AAB67343.1; -; Genomic_DNA.
DR EMBL; AY692761; AAT92780.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09608.1; -; Genomic_DNA.
DR PIR; S50382; S50382.
DR RefSeq; NP_013401.1; NM_001182186.1.
DR PDB; 5ZWN; EM; 3.30 A; R=1-231.
DR PDB; 6G90; EM; 4.00 A; C=1-231.
DR PDB; 6N7P; EM; 3.60 A; B=1-231.
DR PDB; 6N7R; EM; 3.20 A; B=1-231.
DR PDB; 6N7X; EM; 3.60 A; B=1-231.
DR PDB; 7OQC; EM; 4.10 A; C=1-231.
DR PDB; 7OQE; EM; 5.90 A; C=1-231.
DR PDBsum; 5ZWN; -.
DR PDBsum; 6G90; -.
DR PDBsum; 6N7P; -.
DR PDBsum; 6N7R; -.
DR PDBsum; 6N7X; -.
DR PDBsum; 7OQC; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; Q05900; -.
DR SMR; Q05900; -.
DR BioGRID; 31562; 772.
DR ComplexPortal; CPX-23; U1 small nuclear ribonucleoprotein complex.
DR DIP; DIP-6661N; -.
DR IntAct; Q05900; 19.
DR MINT; Q05900; -.
DR STRING; 4932.YLR298C; -.
DR MaxQB; Q05900; -.
DR PaxDb; Q05900; -.
DR PRIDE; Q05900; -.
DR EnsemblFungi; YLR298C_mRNA; YLR298C; YLR298C.
DR GeneID; 851005; -.
DR KEGG; sce:YLR298C; -.
DR SGD; S000004289; YHC1.
DR VEuPathDB; FungiDB:YLR298C; -.
DR eggNOG; KOG3454; Eukaryota.
DR HOGENOM; CLU_104749_0_0_1; -.
DR InParanoid; Q05900; -.
DR OMA; HSYLTHD; -.
DR BioCyc; YEAST:G3O-32391-MON; -.
DR ChiTaRS; YHC1; yeast.
DR PRO; PR:Q05900; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05900; protein.
DR GO; GO:0000243; C:commitment complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005685; C:U1 snRNP; IDA:SGD.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IPI:SGD.
DR GO; GO:0030627; F:pre-mRNA 5'-splice site binding; IDA:SGD.
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; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IPI:SGD.
DR GO; GO:1905216; P:positive regulation of RNA binding; IDA:SGD.
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 SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..231
FT /note="U1 small nuclear ribonucleoprotein C"
FT /id="PRO_0000097528"
FT ZN_FING 4..36
FT /note="Matrin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03153"
FT REGION 49..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 13
FT /note="L->A,D,E,F,G,H,K,P,R,S,T,W,Y: Gives rise to unstable
FT commitment complexes."
FT /evidence="ECO:0000269|PubMed:11172727,
FT ECO:0000269|PubMed:15465910"
FT MUTAGEN 13
FT /note="L->C,I,M,N,Q,V: No effect."
FT /evidence="ECO:0000269|PubMed:11172727,
FT ECO:0000269|PubMed:15465910"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6N7R"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 28..47
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:6N7R"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:5ZWN"
SQ SEQUENCE 231 AA; 27045 MW; 277272AB2A6D273D CRC64;
MTRYYCEYCH SYLTHDTLSV RKSHLVGKNH LRITADYYRN KARDIINKHN HKRRHIGKRG
RKERENSSQN ETLKVTCLSN KEKRHIMHVK KMNQKELAQT SIDTLKLLYD GSPGYSKVFV
DANRFDIGDL VKASKLPQRA NEKSAHHSFK QTSRSRDETC ESNPFPRLNN PKKLEPPKIL
SQWSNTIPKT SIFYSVDILQ TTIKESKKRM HSDGIRKPSS ANGYKRRRYG N
