ID   SNU71_YEAST             Reviewed;         620 AA.
AC   P53207; D6VUE9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=U1 small nuclear ribonucleoprotein component SNU71;
GN   Name=SNU71; OrderedLocusNames=YGR013W;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9290212;
RX   DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA   Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT   "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT   chromosome VII.";
RL   Yeast 13:1077-1090(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
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   [4]
RP   PROTEIN SEQUENCE OF 26-38; 104-128; 191-197; 232-240; 451-461; 468-479;
RP   505-549 AND 597-613, AND IDENTIFICATION IN U1 SNRNP COMPLEX.
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   [5]
RP   IDENTIFICATION IN U1 SNRNP COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=10504710; DOI=10.1038/13732;
RA   Rigaut G., Shevchenko A., Rutz B., Wilm M., Mann M., Seraphin B.;
RT   "A generic protein purification method for protein complex characterization
RT   and proteome exploration.";
RL   Nat. Biotechnol. 17:1030-1032(1999).
RN   [6]
RP   FUNCTION OF THE U1 SNRNP COMPLEX.
RX   PubMed=11877437; DOI=10.1074/jbc.m112460200;
RA   Libri D., Duconge F., Levy L., Vinauger M.;
RT   "A role for the Psi-U mismatch in the recognition of the 5' splice site of
RT   yeast introns by the U1 small nuclear ribonucleoprotein particle.";
RL   J. Biol. Chem. 277:18173-18181(2002).
RN   [7]
RP   IDENTIFICATION IN U1.U2.U4/U6.U5 PENTA-SNRNP COMPLEX, AND IDENTIFICATION BY
RP   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).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512 AND SER-514, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
CC   -!- FUNCTION: Component of the U1 snRNP particle, which recognizes and
CC       binds the 5'-splice site of pre-mRNA. Together with other non-snRNP
CC       factors, U1 snRNP forms the spliceosomal commitment complex, that
CC       targets pre-mRNA to the splicing pathway.
CC       {ECO:0000269|PubMed:11877437}.
CC   -!- SUBUNIT: Component of the 18S U1 snRNP particle, a subcomplex of the
CC       spliceosome. {ECO:0000269|PubMed:10504710, ECO:0000269|PubMed:11804584,
CC       ECO:0000269|PubMed:9630245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 782 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SNU71 family. {ECO:0000305}.
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DR   EMBL; Z72798; CAA96996.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08110.1; -; Genomic_DNA.
DR   PIR; S64304; S64304.
DR   RefSeq; NP_011527.1; NM_001181142.1.
DR   PDB; 5ZWN; EM; 3.30 A; X=1-619.
DR   PDB; 6G90; EM; 4.00 A; J=1-620.
DR   PDB; 6N7P; EM; 3.60 A; H=1-52.
DR   PDB; 6N7R; EM; 3.20 A; H=1-52.
DR   PDB; 6N7X; EM; 3.60 A; H=1-620.
DR   PDB; 7OQC; EM; 4.10 A; J=1-620.
DR   PDB; 7OQE; EM; 5.90 A; J=1-620.
DR   PDBsum; 5ZWN; -.
DR   PDBsum; 6G90; -.
DR   PDBsum; 6N7P; -.
DR   PDBsum; 6N7R; -.
DR   PDBsum; 6N7X; -.
DR   PDBsum; 7OQC; -.
DR   PDBsum; 7OQE; -.
DR   AlphaFoldDB; P53207; -.
DR   EMDB; EMD-0360; -.
DR   EMDB; EMD-0361; -.
DR   EMDB; EMD-13029; -.
DR   EMDB; EMD-13033; -.
DR   EMDB; EMD-4364; -.
DR   EMDB; EMD-6973; -.
DR   SMR; P53207; -.
DR   BioGRID; 33256; 116.
DR   ComplexPortal; CPX-23; U1 small nuclear ribonucleoprotein complex.
DR   DIP; DIP-5507N; -.
DR   IntAct; P53207; 24.
DR   MINT; P53207; -.
DR   STRING; 4932.YGR013W; -.
DR   iPTMnet; P53207; -.
DR   MaxQB; P53207; -.
DR   PaxDb; 4932-YGR013W; -.
DR   PeptideAtlas; P53207; -.
DR   EnsemblFungi; YGR013W_mRNA; YGR013W; YGR013W.
DR   GeneID; 852896; -.
DR   KEGG; sce:YGR013W; -.
DR   AGR; SGD:S000003245; -.
DR   SGD; S000003245; SNU71.
DR   VEuPathDB; FungiDB:YGR013W; -.
DR   eggNOG; KOG2253; Eukaryota.
DR   HOGENOM; CLU_031562_0_0_1; -.
DR   InParanoid; P53207; -.
DR   OMA; YDHHRSF; -.
DR   OrthoDB; 2027173at2759; -.
DR   BioCyc; YEAST:G3O-30740-MONOMER; -.
DR   BioGRID-ORCS; 852896; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P53207; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53207; Protein.
DR   GO; GO:0000243; C:commitment complex; NAS:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0005681; C:spliceosomal complex; NAS:ComplexPortal.
DR   GO; GO:0005685; C:U1 snRNP; IDA:SGD.
DR   GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IDA:SGD.
DR   GO; GO:0000395; P:mRNA 5'-splice site recognition; NAS:ComplexPortal.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:SGD.
DR   Gene3D; 1.20.1390.10; PWI domain; 1.
DR   InterPro; IPR002483; PWI_dom.
DR   SMART; SM00311; PWI; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome.
FT   CHAIN           1..620
FT                   /note="U1 small nuclear ribonucleoprotein component SNU71"
FT                   /id="PRO_0000202781"
FT   REGION          59..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          296..385
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        246..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..353
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         512
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         514
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:6N7R"
FT   HELIX           9..13
FT                   /evidence="ECO:0007829|PDB:6N7R"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:6N7R"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:6N7R"
FT   HELIX           36..42
FT                   /evidence="ECO:0007829|PDB:6N7R"
FT   HELIX           44..51
FT                   /evidence="ECO:0007829|PDB:6N7R"
SQ   SEQUENCE   620 AA;  71383 MW;  2659AAA62C4993D5 CRC64;
     MRDIVFVSPQ LYLSSQEGWK SDSAKSGFIP ILKNDLQRFQ DSLKHIVDAR NSLSETLLNS
     NDDGSIHNSD QNTGLNKDKE ASIADNNSAN KCATSSSRYQ ELKQFLPISL DQQIHTVSLQ
     GVSSSFSRGQ IESLLDHCLN LALTETQSNS ALKVEAWSSF SSFLDTQDIF IRFSKVDEDE
     AFVNTLNYCK ALFAFIRKLH EDFKIELHLD LNTKEYVEDR TGTIPSVKPE KASEFYSVFK
     NIEDQTDERN SKKEQLDDSS TQYKVDTNTL SDLPSDALDQ LCKDIIEFRT KVVSIEKEKK
     MKSTYEESRR QRHQMQKVFD QIRKNHSGAK GSANTEEEDT NMEDEDEEDD TEDDLALEKR
     KEERDLEESN RRYEDMLHQL HSNTEPKIKS IRADIMSAEN YEEHLEKNRS LYLKELLHLA
     NDVHYDHHRS FKEQEERRDE EDRAKNGNAK ELAPIQLSDG KAISAGKAAA ITLPEGTVKS
     ENYNADKNVS ESSEHVKIKF DFKKAIDHSV ESSSEDEGYR ESELPPTKPS ERSAAEDRLP
     FTADELNIRL TNLKESRYVD ELVREFLGVY EDELVEYILE NIRVNQSKQA LLNELRETFD
     EDGETIADRL WSRKEFRLGT
//