RU2A_YEAST
ID RU2A_YEAST Reviewed; 238 AA.
AC Q08963; D6W3F7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=U2 small nuclear ribonucleoprotein A';
DE Short=U2 snRNP A';
DE AltName: Full=Looks exceptionally like U2A protein 1;
GN Name=LEA1; OrderedLocusNames=YPL213W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 FUNCTION, AND INTERACTION WITH MSL1.
RX PubMed=9799242; DOI=10.1093/emboj/17.21.6348;
RA Caspary F., Seraphin B.;
RT "The yeast U2A'/U2B complex is required for pre-spliceosome formation.";
RL EMBO J. 17:6348-6358(1998).
RN [5]
RP IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [7]
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 [8]
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 pre-mRNA splicing. Associates to U2 snRNA in a
CC MSL1 dependent manner and is required for normal accumulation of U2
CC snRNA. Required for the spliceosome assembly and the efficient addition
CC of U2 snRNP onto the pre-mRNA. {ECO:0000269|PubMed:9799242}.
CC -!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome
CC composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2,
CC CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24,
CC CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9,
CC PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3,
CC SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts
CC with MSL1. {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:9799242}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the U2 small nuclear ribonucleoprotein A family.
CC {ECO:0000305}.
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DR EMBL; Z73569; CAA97928.1; -; Genomic_DNA.
DR EMBL; AY558137; AAS56463.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11223.1; -; Genomic_DNA.
DR PIR; S65232; S65232.
DR RefSeq; NP_015111.1; NM_001184027.1.
DR PDB; 5GMK; EM; 3.40 A; b=1-238.
DR PDB; 5LJ3; EM; 3.80 A; W=1-238.
DR PDB; 5LJ5; EM; 3.80 A; W=1-238.
DR PDB; 5MQ0; EM; 4.17 A; W=1-238.
DR PDB; 5NRL; EM; 7.20 A; W=1-238.
DR PDB; 5WSG; EM; 4.00 A; Y=1-238.
DR PDB; 5Y88; EM; 3.70 A; o=1-238.
DR PDB; 5YLZ; EM; 3.60 A; o=1-238.
DR PDB; 5ZWM; EM; 3.40 A; o=1-238.
DR PDB; 5ZWO; EM; 3.90 A; o=1-238.
DR PDB; 6BK8; EM; 3.30 A; s=1-238.
DR PDB; 6EXN; EM; 3.70 A; W=1-238.
DR PDB; 6G90; EM; 4.00 A; W=1-238.
DR PDB; 6J6G; EM; 3.20 A; b=1-238.
DR PDB; 6J6H; EM; 3.60 A; b=1-238.
DR PDB; 6J6N; EM; 3.86 A; b=1-238.
DR PDB; 6J6Q; EM; 3.70 A; b=1-238.
DR PDB; 7OQB; EM; 9.00 A; W=1-238.
DR PDB; 7OQE; EM; 5.90 A; W=1-238.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LJ3; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5WSG; -.
DR PDBsum; 5Y88; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR PDBsum; 6G90; -.
DR PDBsum; 6J6G; -.
DR PDBsum; 6J6H; -.
DR PDBsum; 6J6N; -.
DR PDBsum; 6J6Q; -.
DR PDBsum; 7OQB; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; Q08963; -.
DR SMR; Q08963; -.
DR BioGRID; 35972; 693.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR DIP; DIP-2399N; -.
DR IntAct; Q08963; 30.
DR MINT; Q08963; -.
DR STRING; 4932.YPL213W; -.
DR MaxQB; Q08963; -.
DR PaxDb; Q08963; -.
DR PRIDE; Q08963; -.
DR EnsemblFungi; YPL213W_mRNA; YPL213W; YPL213W.
DR GeneID; 855888; -.
DR KEGG; sce:YPL213W; -.
DR SGD; S000006134; LEA1.
DR VEuPathDB; FungiDB:YPL213W; -.
DR eggNOG; KOG1644; Eukaryota.
DR GeneTree; ENSGT00940000153289; -.
DR HOGENOM; CLU_061027_3_0_1; -.
DR OMA; CHLEDYR; -.
DR BioCyc; YEAST:G3O-34103-MON; -.
DR PRO; PR:Q08963; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08963; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005686; C:U2 snRNP; IDA:SGD.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR044640; RU2A.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR PANTHER; PTHR10552; PTHR10552; 1.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Leucine-rich repeat; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Spliceosome.
FT CHAIN 1..238
FT /note="U2 small nuclear ribonucleoprotein A'"
FT /id="PRO_0000074189"
FT REPEAT 53..74
FT /note="LRR 1"
FT REPEAT 75..95
FT /note="LRR 2"
FT REPEAT 97..118
FT /note="LRR 3"
FT DOMAIN 132..170
FT /note="LRRCT"
FT REGION 167..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:5GMK"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 238 AA; 27193 MW; 0E92A1922BFEDC25 CRC64;
MKFTPSIVID APQYYVDHFN GKYNVDKCVI LRDLQLETDS ESMPSSLKHL TKPTHILDLT
NNDLIMIPDL SRRDDIHTLL LGRNNIVEVD GRLLPMNVQN LTLSNNSIRR FEDLQRLRRA
PRTLKNLTLI GNQVCHLANY REHVLRLVPH LETLDFQNVT AEERKSAMSF PRQADGDTLG
PVNTAIRDNG SRDKTMEIMN LVVSKMTVER RNELKKQLAE ATSLEEIARL EKLLSGGV
