LCL3_YEAST
ID LCL3_YEAST Reviewed; 274 AA.
AC P53153; D6VU59;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
DE AltName: Full=Long chronological lifespan protein 3;
GN Name=LCL3; OrderedLocusNames=YGL085W;
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 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 [5]
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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=20421943; DOI=10.1371/journal.pgen.1000921;
RA Matecic M., Smith D.L., Pan X., Maqani N., Bekiranov S., Boeke J.D.,
RA Smith J.S.;
RT "A microarray-based genetic screen for yeast chronological aging factors.";
RL PLoS Genet. 6:E1000921-E1000921(2010).
RN [7]
RP INDUCTION.
RX PubMed=17351896; DOI=10.1002/yea.1446;
RA Lee M.-W., Kim B.-J., Choi H.-K., Ryu M.-J., Kim S.-B., Kang K.-M.,
RA Cho E.-J., Youn H.-D., Huh W.-K., Kim S.-T.;
RT "Global protein expression profiling of budding yeast in response to DNA
RT damage.";
RL Yeast 24:145-154(2007).
CC -!- INTERACTION:
CC P53153; P40073: SHO1; NbExp=2; IntAct=EBI-23857, EBI-18140;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- INDUCTION: By DNA-damaging agent methyl methanesulphonate (MMS) (at
CC protein level). {ECO:0000269|PubMed:17351896}.
CC -!- DISRUPTION PHENOTYPE: Leads to long chronological lifespan.
CC {ECO:0000269|PubMed:20421943}.
CC -!- MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the LCL3 family. {ECO:0000305}.
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DR EMBL; Z72607; CAA96790.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08020.1; -; Genomic_DNA.
DR PIR; S64092; S64092.
DR RefSeq; NP_011430.1; NM_001180950.1.
DR AlphaFoldDB; P53153; -.
DR BioGRID; 33165; 34.
DR IntAct; P53153; 3.
DR MINT; P53153; -.
DR STRING; 4932.YGL085W; -.
DR iPTMnet; P53153; -.
DR MaxQB; P53153; -.
DR PaxDb; P53153; -.
DR PRIDE; P53153; -.
DR EnsemblFungi; YGL085W_mRNA; YGL085W; YGL085W.
DR GeneID; 852795; -.
DR KEGG; sce:YGL085W; -.
DR SGD; S000003053; LCL3.
DR VEuPathDB; FungiDB:YGL085W; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; P53153; -.
DR OMA; IYHTPGG; -.
DR BioCyc; YEAST:G3O-30586-MON; -.
DR PRO; PR:P53153; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53153; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; SSF50199; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 1: Evidence at protein level;
KW Calcium; Endonuclease; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW Nuclease; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..274
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000215285"
FT TRANSMEM 15..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 53..261
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 274 AA; 32112 MW; 38C1B01FEF4838A0 CRC64;
MREGDSNSKK SADVAVLSII LTGSTLTLIY TYKRYLTQFK RTNDIPRRIF RKHWLYGKVT
SVGDGDNFHF FHMPGGIRGG WGWLRPVPQM IKNDSTAEKL VGDSRNMRFF NFNWITHGRS
TKSKIQKAKS QFLKLNVPYK NRKNLPTIPI RLCGIDAPER AHFGNPAQPF GNEALIWLQN
RILGKKVWVK PLSIDQYNRC VARVSYWDWF GGWKDLSLEM LKDGLAVVYE GKVNTEFDDR
EDKYRYYEFL ARSRKKGLWI QNKFETPGEY KKRI
