EXG2_YEAST
ID EXG2_YEAST Reviewed; 562 AA.
AC P52911; D6VSP1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Glucan 1,3-beta-glucosidase 2;
DE EC=3.2.1.58;
DE AltName: Full=Exo-1,3-beta-glucanase 2;
DE Flags: Precursor;
GN Name=EXG2; OrderedLocusNames=YDR261C; ORFNames=YD9320A.12C;
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 204510 / AB320;
RA Correa J., Vazquez de Aldana C., San Segundo P., del Rey F.;
RT "EXG2, a gene coding for a exo-1,3-B-glucanase with a GPI anchor attachment
RT site in the carboxy terminus.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
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 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 2410 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; Z46870; CAA86950.1; -; Genomic_DNA.
DR EMBL; Z70202; CAA94100.1; -; Genomic_DNA.
DR EMBL; Z68329; CAA92719.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12101.1; -; Genomic_DNA.
DR PIR; S55516; S55516.
DR RefSeq; NP_010547.1; NM_001180569.1.
DR AlphaFoldDB; P52911; -.
DR SMR; P52911; -.
DR BioGRID; 32311; 54.
DR IntAct; P52911; 1.
DR STRING; 4932.YDR261C; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR MaxQB; P52911; -.
DR PaxDb; P52911; -.
DR PRIDE; P52911; -.
DR EnsemblFungi; YDR261C_mRNA; YDR261C; YDR261C.
DR GeneID; 851848; -.
DR KEGG; sce:YDR261C; -.
DR SGD; S000002669; EXG2.
DR VEuPathDB; FungiDB:YDR261C; -.
DR eggNOG; ENOG502QW42; Eukaryota.
DR GeneTree; ENSGT00940000176313; -.
DR HOGENOM; CLU_004624_0_0_1; -.
DR InParanoid; P52911; -.
DR OMA; KSINYEH; -.
DR BioCyc; YEAST:YDR261C-MON; -.
DR PRO; PR:P52911; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P52911; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IDA:SGD.
DR GO; GO:0006073; P:cellular glucan metabolic process; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IC:SGD.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..562
FT /note="Glucan 1,3-beta-glucosidase 2"
FT /id="PRO_0000007894"
FT ACT_SITE 254
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 562 AA; 63508 MW; 5814509CC3D93F73 CRC64;
MPLKSFFFSA FLVLCLSKFT QGVGTTEKEE SLSPLELNIL QNKFASYYAN DTITVKGITI
GGWLVTEPYI TPSLYRNATS LAKQQNSSSN ISIVDEFTLC KTLGYNTSLT LLDNHFKTWI
TEDDFEQIKT NGFNLVRIPI GYWAWKQNTD KNLYIDNITF NDPYVSDGLQ LKYLNNALEW
AQKYELNVWL DLHGAPGSQN GFDNSGERIL YGDLGWLRLN NTKELTLAIW RDMFQTFLNK
GDKSPVVGIQ IVNEPLGGKI DVSDITEMYY EAFDLLKKNQ NSSDNTTFVI HDGFQGIGHW
NLELNPTYQN VSHHYFNLTG ANYSSQDILV DHHHYEVFTD AQLAETQFAR IENIINYGDS
IHKELSFHPA VVGEWSGAIT DCATWLNGVG VGARYDGSYY NTTLFTTNDK PVGTCISQNS
LADWTQDYRD RVRQFIEAQL ATYSSKTTGW IFWNWKTEDA VEWDYLKLKE ANLFPSPFDN
YTYFKADGSI EEKFSSSLSA QAFPRTTSSV LSSTTTSRKS KNAAISNKLT TSQLLPIKNM
SLTWKASVCA LAITIAALCA SL
