LUC7_YEAST
ID LUC7_YEAST Reviewed; 261 AA.
AC Q07508; D6VRR1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein LUC7;
GN Name=LUC7; Synonyms=EPE1, EXM2; OrderedLocusNames=YDL087C;
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], AND FUNCTION.
RX PubMed=10533282; DOI=10.1016/s1357-2725(99)00044-8;
RA Alexieva K.I., Klis F., Wedler H., Wambutt R., Venkov P.;
RT "Identification of the essential EPE1 gene involved in retention of
RT secreted proteins on the cell surface of Saccharomyces cerevisiae cells.";
RL Int. J. Biochem. Cell Biol. 31:903-914(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 IDENTIFICATION IN THE U1 SNRNP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
RA Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
RA Fabrizio P.;
RT "Identification by mass spectrometry and functional analysis of novel
RT proteins of the yeast [U4/U6.U5] tri-snRNP.";
RL EMBO J. 18:4535-4548(1999).
RN [5]
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 [6]
RP IDENTIFICATION IN THE U1 SNRNP COMPLEX, AND FUNCTION.
RX PubMed=10500099; DOI=10.1101/gad.13.18.2425;
RA Fortes P., Bilbao-Cortes D., Fornerod M., Rigaut G., Raymond W.,
RA Seraphin B., Mattaj I.W.;
RT "Luc7p, a novel yeast U1 snRNP protein with a role in 5' splice site
RT recognition.";
RL Genes Dev. 13:2425-2438(1999).
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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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. {ECO:0000269|PubMed:10500099,
CC ECO:0000269|PubMed:10533282}.
CC -!- SUBUNIT: Component of the 18S U1 snRNP particle, a subcomplex of the
CC spliceosome. {ECO:0000269|PubMed:10449419, ECO:0000269|PubMed:10500099,
CC ECO:0000269|PubMed:11804584}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2270 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Luc7 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z74135; CAA98653.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11771.1; -; Genomic_DNA.
DR PIR; S67623; S67623.
DR RefSeq; NP_010196.1; NM_001180146.1.
DR PDB; 5ZWN; EM; 3.30 A; Y=1-261.
DR PDB; 6G90; EM; 4.00 A; H=1-261.
DR PDB; 6N7P; EM; 3.60 A; I=1-261.
DR PDB; 6N7R; EM; 3.20 A; I=1-261.
DR PDB; 7OQC; EM; 4.10 A; H=1-261.
DR PDB; 7OQE; EM; 5.90 A; H=1-261.
DR PDBsum; 5ZWN; -.
DR PDBsum; 6G90; -.
DR PDBsum; 6N7P; -.
DR PDBsum; 6N7R; -.
DR PDBsum; 7OQC; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; Q07508; -.
DR SMR; Q07508; -.
DR BioGRID; 31973; 130.
DR ComplexPortal; CPX-23; U1 small nuclear ribonucleoprotein complex.
DR DIP; DIP-3003N; -.
DR IntAct; Q07508; 32.
DR MINT; Q07508; -.
DR STRING; 4932.YDL087C; -.
DR iPTMnet; Q07508; -.
DR MaxQB; Q07508; -.
DR PaxDb; Q07508; -.
DR PRIDE; Q07508; -.
DR EnsemblFungi; YDL087C_mRNA; YDL087C; YDL087C.
DR GeneID; 851471; -.
DR KEGG; sce:YDL087C; -.
DR SGD; S000002245; LUC7.
DR VEuPathDB; FungiDB:YDL087C; -.
DR eggNOG; KOG0796; Eukaryota.
DR GeneTree; ENSGT00950000183213; -.
DR HOGENOM; CLU_030397_1_0_1; -.
DR InParanoid; Q07508; -.
DR OMA; LGYVKMR; -.
DR BioCyc; YEAST:G3O-29495-MON; -.
DR PRO; PR:Q07508; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07508; protein.
DR GO; GO:0000243; C:commitment complex; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005685; C:U1 snRNP; IMP:SGD.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IC:ComplexPortal.
DR GO; GO:0006376; P:mRNA splice site selection; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR InterPro; IPR004882; Luc7-rel.
DR PANTHER; PTHR12375; PTHR12375; 1.
DR Pfam; PF03194; LUC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Ribonucleoprotein; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..261
FT /note="Protein LUC7"
FT /id="PRO_0000255959"
FT COILED 123..190
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 92..120
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 125..145
FT /evidence="ECO:0007829|PDB:5ZWN"
FT HELIX 169..195
FT /evidence="ECO:0007829|PDB:5ZWN"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6N7R"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 224..243
FT /evidence="ECO:0007829|PDB:6N7R"
SQ SEQUENCE 261 AA; 30195 MW; F6CFA1947C1C86B1 CRC64;
MSTMSTPAAE QRKLVEQLMG RDFSFRHNRY SHQKRDLGLH DPKICKSYLV GECPYDLFQG
TKQSLGKCPQ MHLTKHKIQY EREVKQGKTF PEFEREYLAI LSRFVNECNG QISVALQNLK
HTAEERMKIQ QVTEELDVLD VRIGLMGQEI DSLIRADEVS MGMLQSVKLQ ELISKRKEVA
KRVRNITENV GQSAQQKLQV CEVCGAYLSR LDTDRRLADH FLGKIHLGYV KMREDYDRLM
KNNRTTNASK TATTLPGRRF V
