RU1A_YEAST
ID RU1A_YEAST Reviewed; 298 AA.
AC P32605; D6VQB7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=U1 small nuclear ribonucleoprotein A;
DE Short=U1 snRNP A;
DE Short=U1-A;
DE Short=U1A;
DE AltName: Full=Mutant U1 die protein 1;
GN Name=MUD1; OrderedLocusNames=YBR119W; ORFNames=YBR0915;
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 [GENOMIC DNA], FUNCTION, AND INTERACTION WITH U1 SNRNA.
RC STRAIN=XLY219;
RX PubMed=8449403; DOI=10.1101/gad.7.3.419;
RA Liao X.C., Tang J., Rosbash M.;
RT "An enhancer screen identifies a gene that encodes the yeast U1 snRNP A
RT protein: implications for snRNP protein function in pre-mRNA splicing.";
RL Genes Dev. 7:419-428(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
RP FUNCTION, U1 SNRNA-BINDING, AND MUTAGENESIS OF LEU-4; 6-PHE-GLN-7; LEU-63;
RP 65-VAL--ILE-67; 69-ARG--LYS-72; 74-THR-ASN-75; 79-LEU-THR-80; VAL-228;
RP 230-LEU--GLN-232; 258-VAL--VAL-260; 262-ASN-LEU-263; TYR-268;
RP 291-ASP--THR-293 AND GLY-295.
RX PubMed=8849781;
RA Tang J., Rosbash M.;
RT "Characterization of yeast U1 snRNP A protein: identification of the N-
RT terminal RNA binding domain (RBD) binding site and evidence that the C-
RT terminal RBD functions in splicing.";
RL RNA 2:1058-1070(1996).
RN [6]
RP IDENTIFICATION IN U1 SNRNP BY MASS SPECTROMETRY.
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 [7]
RP IDENTIFICATION IN U1 SNRNP BY MASS SPECTROMETRY.
RX PubMed=11804584; DOI=10.1016/s1097-2765(02)00436-7;
RA Stevens S.W., Ryan D.E., Ge H.Y., Moore R.E., Young M.K., Lee T.D.,
RA Abelson J.;
RT "Composition and functional characterization of the yeast spliceosomal
RT penta-snRNP.";
RL Mol. Cell 9:31-44(2002).
RN [8]
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 [9]
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).
CC -!- FUNCTION: Involved in nuclear mRNA splicing. The principal role of the
CC U1A is to help fold or maintain U1 RNA in an active configuration. It
CC is the first snRNP to interact with pre-mRNA. This interaction is
CC required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-
CC snRNP. {ECO:0000269|PubMed:8449403, ECO:0000269|PubMed:8849781}.
CC -!- SUBUNIT: Component of the spliceosome where it is associated with snRNP
CC U1. {ECO:0000269|PubMed:11804584, ECO:0000269|PubMed:9012791}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 2950 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRM U1 A/B'' family. {ECO:0000305}.
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DR EMBL; X71061; CAA50378.1; -; Genomic_DNA.
DR EMBL; X78993; CAA55621.1; -; Genomic_DNA.
DR EMBL; Z35988; CAA85076.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07237.1; -; Genomic_DNA.
DR PIR; A46301; A46301.
DR RefSeq; NP_009677.1; NM_001178467.1.
DR PDB; 5ZWN; EM; 3.30 A; S=1-298.
DR PDB; 6G90; EM; 4.00 A; A=1-298.
DR PDB; 6N7P; EM; 3.60 A; C=1-298.
DR PDB; 6N7R; EM; 3.20 A; C=1-298.
DR PDB; 6N7X; EM; 3.60 A; C=1-298.
DR PDB; 7OQC; EM; 4.10 A; A=1-298.
DR PDB; 7OQE; EM; 5.90 A; A=1-298.
DR PDBsum; 5ZWN; -.
DR PDBsum; 6G90; -.
DR PDBsum; 6N7P; -.
DR PDBsum; 6N7R; -.
DR PDBsum; 6N7X; -.
DR PDBsum; 7OQC; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; P32605; -.
DR SMR; P32605; -.
DR BioGRID; 32821; 199.
DR ComplexPortal; CPX-23; U1 small nuclear ribonucleoprotein complex.
DR DIP; DIP-223N; -.
DR IntAct; P32605; 13.
DR MINT; P32605; -.
DR STRING; 4932.YBR119W; -.
DR MaxQB; P32605; -.
DR PaxDb; P32605; -.
DR PRIDE; P32605; -.
DR EnsemblFungi; YBR119W_mRNA; YBR119W; YBR119W.
DR GeneID; 852416; -.
DR KEGG; sce:YBR119W; -.
DR SGD; S000000323; MUD1.
DR VEuPathDB; FungiDB:YBR119W; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_057159_0_0_1; -.
DR InParanoid; P32605; -.
DR OMA; DDICAKK; -.
DR BioCyc; YEAST:G3O-29076-MON; -.
DR PRO; PR:P32605; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32605; protein.
DR GO; GO:0000243; C:commitment complex; IC:ComplexPortal.
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:0030619; F:U1 snRNA binding; IGI:SGD.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IGI:SGD.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..298
FT /note="U1 small nuclear ribonucleoprotein A"
FT /id="PRO_0000081891"
FT DOMAIN 2..113
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 227..298
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MUTAGEN 4
FT /note="L->I: Sensitive in DMS protection of U1 snRNA; when
FT associated with 6-I-N-7."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 6..7
FT /note="FQ->IN: Sensitive in DMS protection of U1 snRNA;
FT when associated with I-4."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 63
FT /note="L->I: Sensitive in DMS protection of U1 snRNA; when
FT associated with 65-D--L-67."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 65..67
FT /note="VSI->DIL: Sensitive in DMS protection of U1 snRNA;
FT when associated with I-63."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 69..72
FT /note="RSSK->LKTM: Sensitive in DMS protection of U1
FT snRNA."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 74..75
FT /note="TN->RG: Sensitive in DMS protection of U1 snRNA;
FT when associated with 79-V-I-80."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 79..80
FT /note="LT->VI: Sensitive in DMS protection of U1 snRNA;
FT when associated with 74-R-G-75."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 228
FT /note="V->I: Splicing defects; when associated with 230-F--
FT T-232."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 230..232
FT /note="LIQ->FLT: Splicing defects; when associated with I-
FT 228."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 258..260
FT /note="VSV->PGH: Splicing defects."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 262..263
FT /note="NL->DI: Splicing defects; when associated with F-
FT 268."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 268
FT /note="Y->F: Splicing defects; when associated with 262-D-
FT I-263."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 291..293
FT /note="DVT->AMK: Splicing defects; when associated with S-
FT 295."
FT /evidence="ECO:0000269|PubMed:8849781"
FT MUTAGEN 295
FT /note="G->S: Splicing defects; when associated with 291-A--
FT K-293."
FT /evidence="ECO:0000269|PubMed:8849781"
FT CONFLICT 1..3
FT /note="MSA -> MTNKNR (in Ref. 2; CAA55621)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:6N7R"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:5ZWN"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:6N7R"
SQ SEQUENCE 298 AA; 34378 MW; 42256530BF1C5379 CRC64;
MSALYFQNLP SRPANKENYT RLLLKHINPN NKYAINPSLP LPHNKLQISS QPLMLLDDQM
GLLEVSISRS SKMTNQAFLT FVTQEEADRF LEKYTTTALK VQGRKVRMGK ARTNSLLGLS
IEMQKKKGND ETYNLDIKKV LKARKLKRKL RSDDICAKKF RLKRQIRRLK HKLRSRKVEE
AEIDRIVKEF ETRRLENMKS QQENLKQSQK PLKRAKVSNT MENPPNKVLL IQNLPSGTTE
QLLSQILGNE ALVEIRLVSV RNLAFVEYET VADATKIKNQ LGSTYKLQNN DVTIGFAK
