GLU2A_YEAST
ID GLU2A_YEAST Reviewed; 954 AA.
AC P38138;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Glucosidase 2 subunit alpha;
DE EC=3.2.1.207 {ECO:0000305|PubMed:16373354, ECO:0000305|PubMed:8910335};
DE AltName: Full=Alpha-glucosidase II subunit alpha;
DE AltName: Full=Glucosidase II subunit alpha;
DE AltName: Full=Reversal of TOR2 lethality protein 2;
DE Flags: Precursor;
GN Name=ROT2; Synonyms=GLS2; OrderedLocusNames=YBR229C; ORFNames=YBR1526;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
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 [3]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6216253; DOI=10.1016/s0021-9258(19)45358-1;
RA Saunier B., Kilker R.D. Jr., Tkacz J.S., Quaroni A., Herscovics A.;
RT "Inhibition of N-linked complex oligosaccharide formation by 1-
RT deoxynojirimycin, an inhibitor of processing glucosidases.";
RL J. Biol. Chem. 257:14155-14161(1982).
RN [4]
RP FUNCTION.
RX PubMed=8910335; DOI=10.1074/jbc.271.44.27509;
RA Trombetta E.S., Simons J.F., Helenius A.;
RT "Endoplasmic reticulum glucosidase II is composed of a catalytic subunit,
RT conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-
RT containing subunit.";
RL J. Biol. Chem. 271:27509-27516(1996).
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 FUNCTION, INTERACTION WITH GTB1, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=16373354; DOI=10.1074/jbc.m510455200;
RA Wilkinson B.M., Purswani J., Stirling C.J.;
RT "Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein
RT processing in the endoplasmic reticulum.";
RL J. Biol. Chem. 281:6325-6333(2006).
CC -!- FUNCTION: Catalytic subunit of glucosidase 2, which cleaves
CC sequentially the 2 innermost alpha-1,3-linked glucose residues from the
CC Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature
CC glycoproteins. {ECO:0000269|PubMed:16373354,
CC ECO:0000269|PubMed:8910335}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein] = beta-D-glucose + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein] (N-glucan mannose isomer 9A1,2,3B1,2,3);
CC Xref=Rhea:RHEA:56000, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59080,
CC ChEBI:CHEBI:139493; EC=3.2.1.207;
CC Evidence={ECO:0000305|PubMed:16373354, ECO:0000305|PubMed:8910335};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-
CC asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc)-L-asparaginyl-[protein]; Xref=Rhea:RHEA:55996,
CC Rhea:RHEA-COMP:14355, Rhea:RHEA-COMP:14357, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:59080, ChEBI:CHEBI:59082;
CC EC=3.2.1.207; Evidence={ECO:0000305|PubMed:16373354,
CC ECO:0000305|PubMed:8910335};
CC -!- ACTIVITY REGULATION: Inhibited by glucose, maltose and nigerose, and by
CC the antibiotic deoxynojirimycin.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.8-6.8. {ECO:0000269|PubMed:6216253};
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC -!- SUBUNIT: Heterodimer of a catalytic subunit alpha (ROT2) and a subunit
CC beta (GTB1).
CC -!- INTERACTION:
CC P38138; Q04924: GTB1; NbExp=2; IntAct=EBI-21021, EBI-37493;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16373354}.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; Z36098; CAA85192.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07344.1; -; Genomic_DNA.
DR PIR; S46105; S46105.
DR RefSeq; NP_009788.3; NM_001178577.3.
DR AlphaFoldDB; P38138; -.
DR SMR; P38138; -.
DR BioGRID; 32924; 202.
DR ComplexPortal; CPX-417; Glucosidase II complex.
DR DIP; DIP-5754N; -.
DR IntAct; P38138; 3.
DR MINT; P38138; -.
DR STRING; 4932.YBR229C; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR MaxQB; P38138; -.
DR PaxDb; P38138; -.
DR PRIDE; P38138; -.
DR EnsemblFungi; YBR229C_mRNA; YBR229C; YBR229C.
DR GeneID; 852530; -.
DR KEGG; sce:YBR229C; -.
DR SGD; S000000433; ROT2.
DR VEuPathDB; FungiDB:YBR229C; -.
DR eggNOG; KOG1066; Eukaryota.
DR GeneTree; ENSGT00940000168086; -.
DR HOGENOM; CLU_000631_7_0_1; -.
DR InParanoid; P38138; -.
DR OMA; QAGIWYP; -.
DR BioCyc; MetaCyc:YBR229C-MON; -.
DR BioCyc; YEAST:YBR229C-MON; -.
DR UniPathway; UPA00957; -.
DR PRO; PR:P38138; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38138; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:SGD.
DR GO; GO:0017177; C:glucosidase II complex; IPI:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0090599; F:alpha-glucosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; IMP:SGD.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0070880; P:fungal-type cell wall beta-glucan biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006491; P:N-glycan processing; IDA:ComplexPortal.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IC:ComplexPortal.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..954
FT /note="Glucosidase 2 subunit alpha"
FT /id="PRO_0000185370"
FT ACT_SITE 537
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT ACT_SITE 540
FT /evidence="ECO:0000250"
FT ACT_SITE 614
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 867
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 954 AA; 110266 MW; 92E93572F04FB009 CRC64;
MVLLKWLVCQ LVFFTAFSHA FTDYLLKKCA QSGFCHRNRV YAENIAKSHH CYYKVDAESI
AHDPLENVLH ATIIKTIPRL EGDDIAVQFP FSLSFLQDHS VRFTINEKER MPTNSSGLLI
SSQRFNETWK YAFDKKFQEE ANRTSIPQFH FLKQKQTVNS FWSKISSFLS LSNSTADTFH
LRNGDVSVEI FAEPFQLKVY WQNALKLIVN EQNFLNIEHH RTKQENFAHV LPEETTFNMF
KDNFLYSKHD SMPLGPESVA LDFSFMGSTN VYGIPEHATS LRLMDTSGGK EPYRLFNVDV
FEYNIGTSQP MYGSIPFMFS SSSTSIFWVN AADTWVDIKY DTSKNKTMTH WISENGVIDV
VMSLGPDIPT IIDKFTDLTG RPFLPPISSI GYHQCRWNYN DEMDVLTVDS QMDAHMIPYD
FIWLDLEYTN DKKYFTWKQH SFPNPKRLLS KLKKLGRNLV VLIDPHLKKD YEISDRVINE
NVAVKDHNGN DYVGHCWPGN SIWIDTISKY GQKIWKSFFE RFMDLPADLT NLFIWNDMNE
PSIFDGPETT APKDLIHDNY IEERSVHNIY GLSVHEATYD AIKSIYSPSD KRPFLLTRAF
FAGSQRTAAT WTGDNVANWD YLKISIPMVL SNNIAGMPFI GADIAGFAED PTPELIARWY
QAGLWYPFFR AHAHIDTKRR EPYLFNEPLK SIVRDIIQLR YFLLPTLYTM FHKSSVTGFP
IMNPMFIEHP EFAELYHIDN QFYWSNSGLL VKPVTEPGQS ETEMVFPPGI FYEFASLHSF
INNGTDLIEK NISAPLDKIP LFIEGGHIIT MKDKYRRSSM LMKNDPYVIV IAPDTEGRAV
GDLYVDDGET FGYQRGEYVE TQFIFENNTL KNVRSHIPEN LTGIHHNTLR NTNIEKIIIA
KNNLQHNITL KDSIKVKKNG EESSLPTRSS YENDNKITIL NLSLDITEDW EVIF
