SIM1_YEAST
ID SIM1_YEAST Reviewed; 476 AA.
AC P40472; A2TBN1; D6VVG4; Q45U06; Q870H1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Probable secreted beta-glucosidase SIM1;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=SIM1; Synonyms=PBP3; OrderedLocusNames=YIL123W;
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 VARIANTS 60-SER--ALA-66 DEL AND
RP 174-PRO--THR-185 DEL.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 85-88.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-81.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-72.
RC STRAIN=ATCC 204508 / S288c;
RA Zhang Z., Dietrich F.S.;
RT "YIL123W (SIM1) mRNA.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION.
RX PubMed=8574583; DOI=10.1016/s0960-9822(95)00252-1;
RA Dahmann C., Diffley J.F.X., Nasmyth K.A.;
RT "S-phase-promoting cyclin-dependent kinases prevent re-replication by
RT inhibiting the transition of replication origins to a pre-replicative
RT state.";
RL Curr. Biol. 5:1257-1269(1995).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11958935; DOI=10.1111/j.1574-6968.2002.tb11046.x;
RA Velours G.M., Boucheron C., Manon S., Camougrand N.M.;
RT "Dual cell wall/mitochondria localization of the 'SUN' family proteins.";
RL FEMS Microbiol. Lett. 207:165-172(2002).
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 SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=24040106; DOI=10.1371/journal.pone.0073882;
RA Kuznetsov E., Kucerova H., Vachova L., Palkova Z.;
RT "SUN family proteins Sun4p, Uth1p and Sim1p are secreted from Saccharomyces
RT cerevisiae and produced dependently on oxygen level.";
RL PLoS ONE 8:E73882-E73882(2013).
CC -!- FUNCTION: Involved in the remodeling of the cell wall during the
CC various phases of yeast culture development and under various
CC environmental conditions. Required for the maintenance of the CLB5
CC kinase activity. {ECO:0000269|PubMed:24040106}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:11958935,
CC ECO:0000269|PubMed:24040106}. Note=Non-covalently bound to the cell
CC wall.
CC -!- INDUCTION: Expression is repressed by anoxia. Expression is decreased
CC during transition to slow growing or stationary phases.
CC {ECO:0000269|PubMed:24040106}.
CC -!- DISRUPTION PHENOTYPE: Leads to increased resistance to zymolyase
CC treatment. {ECO:0000269|PubMed:24040106}.
CC -!- MISCELLANEOUS: Present with 1800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SUN family. {ECO:0000305}.
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DR EMBL; DQ115392; AAZ22504.1; -; Genomic_DNA.
DR EMBL; Z46833; CAA86869.1; -; Genomic_DNA.
DR EMBL; AY245795; AAP04345.1; -; mRNA.
DR EMBL; EF123134; ABM97478.1; -; mRNA.
DR EMBL; BK006942; DAA08430.2; -; Genomic_DNA.
DR PIR; S49886; S49886.
DR RefSeq; NP_012143.2; NM_001179471.2.
DR AlphaFoldDB; P40472; -.
DR BioGRID; 34868; 90.
DR IntAct; P40472; 1.
DR STRING; 4932.YIL123W; -.
DR MaxQB; P40472; -.
DR PaxDb; P40472; -.
DR PRIDE; P40472; -.
DR EnsemblFungi; YIL123W_mRNA; YIL123W; YIL123W.
DR GeneID; 854683; -.
DR KEGG; sce:YIL123W; -.
DR SGD; S000001385; SIM1.
DR VEuPathDB; FungiDB:YIL123W; -.
DR eggNOG; ENOG502QPVV; Eukaryota.
DR GeneTree; ENSGT00940000176328; -.
DR HOGENOM; CLU_033459_2_0_1; -.
DR InParanoid; P40472; -.
DR OMA; CSYACQS; -.
DR BioCyc; YEAST:G3O-31376-MON; -.
DR PRO; PR:P40472; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40472; protein.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR005556; SUN.
DR Pfam; PF03856; SUN; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall; Cell wall biogenesis/degradation;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..476
FT /note="Probable secreted beta-glucosidase SIM1"
FT /id="PRO_0000033465"
FT REGION 111..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 60..66
FT /note="Missing (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 174..185
FT /note="Missing (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT CONFLICT 85..88
FT /note="ADSS -> GIA (in Ref. 2; CAA86869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 48190 MW; 75644489473C08A3 CRC64;
MKFSTAVTTL ISSGAIVSAL PHVDVHQEDA HQHKRAVAYK YVYETVVVDS DGHTVTPAAS
EVATAATSAI ITTSVLAPTS SAAAADSSAS IAVSSAALAK NEKISDAAAS ATASTSQGAS
SSSSSSSATS TLESSSVSSS SEEAAPTSTV VSTSSATQSS ASSATKSSTS STSPSTSTST
STSSTSSSSS SSSSSSSSSS GSGSIYGDLA DFSGPSEKFQ DGTIPCDKFP SGQGVISIDW
IGEGGWSGVE NTDTSTGGSC KEGSYCSYSC QPGMSKTQWP SDQPSDGRSV GGLLCKNGYL
YRSNTDADYL CEWGVEAAYV VSKLSKGVAI CRTDYPGTEN MVIPTYVEGG SSLPLTVVDQ
DTYFTWEGKK TSAQYYVNNA GVSVEDGCIW GTSGSGIGNW APLNFGAGST GGVTYLSLIP
NPNNSDALNY NVKIVAADDS SNVIGECVYE NGEFSGGADG CTVSVTSGKA HFVLYN
