ID   UTH1_YEAS1              Reviewed;         362 AA.
AC   B3LRC2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Probable secreted beta-glucosidase UTH1;
DE            EC=3.2.1.-;
DE   AltName: Full=Youth protein 1;
DE   Flags: Precursor;
GN   Name=UTH1; ORFNames=SCRG_04058;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in aging, oxidative stress response, and in the
CC       regulation of mitochondrial biogenesis. Inactivation of UTH1 increases
CC       life span, leads to higher resistance to heat stress and to hydrogen
CC       peroxide, and increases sensitivity to the superoxide radical-
CC       generating drug paraquat and to copper. Also required for the selective
CC       autophagic degradation of mitochondria (mitophagy) in response to
CC       nitrogen starvation. Involved in the remodeling of the cell wall during
CC       the various phases of yeast culture development and under various
CC       environmental conditions and plays a role in septation. Involved in
CC       cell sensitivity to boric acid (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P36135}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P36135}. Secreted, cell wall
CC       {ECO:0000250|UniProtKB:P36135}. Note=Non-covalently bound to the cell
CC       wall. {ECO:0000250|UniProtKB:P36135}.
CC   -!- SIMILARITY: Belongs to the SUN family. {ECO:0000305}.
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DR   EMBL; CH408051; EDV13125.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LRC2; -.
DR   EnsemblFungi; EDV13125; EDV13125; SCRG_04058.
DR   HOGENOM; CLU_033459_0_0_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005556; SUN.
DR   Pfam; PF03856; SUN; 1.
PE   3: Inferred from homology;
KW   Autophagy; Carbohydrate metabolism; Cell cycle; Cell division; Cell wall;
KW   Cell wall biogenesis/degradation; Glycosidase; Hydrolase; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Polysaccharide degradation;
KW   Secreted; Septation; Signal; Stress response.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..362
FT                   /note="Probable secreted beta-glucosidase UTH1"
FT                   /id="PRO_0000377651"
SQ   SEQUENCE   362 AA;  36737 MW;  BFB70DA7CB0CCB4D CRC64;
     MKLSALLALS ASTAVLAAPA VHHSDNHHHN DKRAVVTVTQ YVNADGTVVI PAANTATSAA
     ADGKVESVAA ATTTLSSTAA AATTSAAASS SSSSSSSSSS VGSGDFEDGT ISCSDFPSGQ
     GAVSLDWLGL GGWASIMDMN GNTATSCQDG YYCSYACSPG YAKTQWPSEQ PSDGRSVGGL
     YCKNGKLYRS NTDTNSLCVE GQGSAQAVNK VSGSIAICGT DYPGSENMVV PTVVGAGSSQ
     PINVIKEDSY YQWQGKKTSA QYYVNNAGVS VEDGCIWGTE GSGVGNWAPV VLGAGYTDGI
     TYLSIIPNPN NKEAPNFNIK IVATDGSTVN GACSYENGVY SGSGSDGCTV SVTSGSANFV
     FY