CWH41_YEAST
ID CWH41_YEAST Reviewed; 833 AA.
AC P53008; D6VUB1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Mannosyl-oligosaccharide glucosidase {ECO:0000305};
DE EC=3.2.1.106 {ECO:0000269|PubMed:23536181};
DE AltName: Full=Processing A-glucosidase I {ECO:0000305};
DE Short=Glucosidase I {ECO:0000303|PubMed:9363442};
GN Name=CWH41; Synonyms=GLS1; OrderedLocusNames=YGL027C;
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], SUBCELLULAR LOCATION, GLYCOSYLATION,
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8576053; DOI=10.1128/jb.178.4.1162-1171.1996;
RA Jiang B., Sheraton J., Ram A.F.J., Dijkgraaf G.J.P., Klis F.M., Bussey H.;
RT "CWH41 encodes a novel endoplasmic reticulum membrane N-glycoprotein
RT involved in beta 1,6-glucan assembly.";
RL J. Bacteriol. 178:1162-1171(1996).
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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9363442; DOI=10.1093/glycob/7.7.997;
RA Romero P.A., Dijkgraaf G.J.P., Shahinian S., Herscovics A., Bussey H.;
RT "The yeast CWH41 gene encodes glucosidase I.";
RL Glycobiology 7:997-1004(1997).
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 X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 35-833, DISULFIDE BOND, CATALYTIC
RP ACTIVITY, ACTIVE SITE, SUBSTRATE-BINDING, MUTAGENESIS OF ASP-601 AND
RP GLU-804, AND ACTIVITY REGULATION.
RX PubMed=23536181; DOI=10.1074/jbc.m113.460436;
RA Barker M.K., Rose D.R.;
RT "Specificity of Processing alpha-glucosidase I is guided by the substrate
RT conformation: crystallographic and in silico studies.";
RL J. Biol. Chem. 288:13563-13574(2013).
CC -!- FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the
CC Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor highly specifically
CC (PubMed:9363442). Seems to play a role in beta-1,6-glucan synthesis
CC (PubMed:8576053). {ECO:0000269|PubMed:8576053,
CC ECO:0000269|PubMed:9363442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-
CC (1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose +
CC N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-
CC beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein]; Xref=Rhea:RHEA:55988, Rhea:RHEA-COMP:12806, Rhea:RHEA-
CC COMP:14355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59082,
CC ChEBI:CHEBI:132537; EC=3.2.1.106;
CC Evidence={ECO:0000269|PubMed:23536181};
CC -!- ACTIVITY REGULATION: Miglitol is an effective inhibitor at 1 mM.
CC {ECO:0000269|PubMed:23536181}.
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8576053}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:8576053}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8576053}.
CC -!- DISRUPTION PHENOTYPE: Displays phenotypes characteristic of cell wall
CC defects such as hypersensitivity to calcofluor white and resistance to
CC K1 killer toxin, and results in a 50% reduction of cell wall beta-1,6-
CC glucan level (PubMed:9363442). Abolishes glucosidase I activity
CC (PubMed:9363442). {ECO:0000269|PubMed:8576053,
CC ECO:0000269|PubMed:9363442}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.
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DR EMBL; U35669; AAC49157.1; -; Genomic_DNA.
DR EMBL; Z72549; CAA96728.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08072.1; -; Genomic_DNA.
DR PIR; S62136; S62136.
DR RefSeq; NP_011488.1; NM_001180892.1.
DR PDB; 4J5T; X-ray; 2.04 A; A=35-833.
DR PDBsum; 4J5T; -.
DR AlphaFoldDB; P53008; -.
DR SMR; P53008; -.
DR BioGRID; 33220; 202.
DR DIP; DIP-5301N; -.
DR IntAct; P53008; 1.
DR MINT; P53008; -.
DR STRING; 4932.YGL027C; -.
DR BindingDB; P53008; -.
DR CAZy; GH63; Glycoside Hydrolase Family 63.
DR iPTMnet; P53008; -.
DR MaxQB; P53008; -.
DR PaxDb; P53008; -.
DR PRIDE; P53008; -.
DR EnsemblFungi; YGL027C_mRNA; YGL027C; YGL027C.
DR GeneID; 852857; -.
DR KEGG; sce:YGL027C; -.
DR SGD; S000002995; CWH41.
DR VEuPathDB; FungiDB:YGL027C; -.
DR eggNOG; KOG2161; Eukaryota.
DR GeneTree; ENSGT00390000017452; -.
DR HOGENOM; CLU_007380_2_0_1; -.
DR InParanoid; P53008; -.
DR OMA; YWKAPLY; -.
DR BioCyc; MetaCyc:YGL027C-MON; -.
DR BioCyc; YEAST:YGL027C-MON; -.
DR UniPathway; UPA00280; -.
DR PRO; PR:P53008; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53008; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004573; F:Glc3Man9GlcNAc2 oligosaccharide glucosidase activity; IDA:SGD.
DR GO; GO:0070880; P:fungal-type cell wall beta-glucan biosynthetic process; IGI:SGD.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:SGD.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:SGD.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.110; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR031335; Glyco_hydro_63_C.
DR InterPro; IPR031631; Glyco_hydro_63N.
DR InterPro; IPR038518; Glyco_hydro_63N_sf.
DR InterPro; IPR004888; Glycoside_hydrolase_63.
DR PANTHER; PTHR10412; PTHR10412; 1.
DR Pfam; PF03200; Glyco_hydro_63; 1.
DR Pfam; PF16923; Glyco_hydro_63N; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Glycosidase; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..833
FT /note="Mannosyl-oligosaccharide glucosidase"
FT /id="PRO_0000057713"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..833
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 601
FT /evidence="ECO:0000269|PubMed:23536181"
FT ACT_SITE 804
FT /evidence="ECO:0000269|PubMed:23536181"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23536181"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23536181"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23536181"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 669..685
FT /evidence="ECO:0000269|PubMed:23536181"
FT MUTAGEN 601
FT /note="D->A,N: Abrogates catalytic activity."
FT /evidence="ECO:0000269|PubMed:23536181"
FT MUTAGEN 804
FT /note="E->A,N: Abrogates catalytic activity."
FT /evidence="ECO:0000269|PubMed:23536181"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:4J5T"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:4J5T"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:4J5T"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 193..203
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 241..256
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 286..295
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 320..341
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 354..370
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 373..381
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 401..410
FT /evidence="ECO:0007829|PDB:4J5T"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 423..436
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 438..449
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 466..470
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 489..505
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 534..558
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 567..572
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 576..578
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 616..635
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 639..658
FT /evidence="ECO:0007829|PDB:4J5T"
FT TURN 663..666
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 670..673
FT /evidence="ECO:0007829|PDB:4J5T"
FT TURN 675..677
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 681..684
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 689..696
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 706..715
FT /evidence="ECO:0007829|PDB:4J5T"
FT TURN 717..720
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 725..729
FT /evidence="ECO:0007829|PDB:4J5T"
FT TURN 734..737
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 742..745
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 749..762
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 764..767
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 776..798
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:4J5T"
FT TURN 808..810
FT /evidence="ECO:0007829|PDB:4J5T"
FT STRAND 813..818
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 822..825
FT /evidence="ECO:0007829|PDB:4J5T"
FT HELIX 826..831
FT /evidence="ECO:0007829|PDB:4J5T"
SQ SEQUENCE 833 AA; 96507 MW; 710F1355DC039ECA CRC64;
MLISKSKMFK TFWILTSIVL LASATVDISK LQEFEEYQKF TNESLLWAPY RSNCYFGMRP
RYVHESPLIM GIMWFNSLSQ DGLHSLRHFA TPQDKLQKYG WEVYDPRIGG KEVFIDEKNN
LNLTVYFVKS KNGENWSVRV QGEPLDPKRP STASVVLYFS QNGGEIDGKS SLAMIGHDGP
NDMKFFGYSK ELGEYHLTVK DNFGHYFKNP EYETMEVAPG SDCSKTSHLS LQIPDKEVWK
ARDVFQSLVS DSIRDILEKE ETKQRPADLI PSVLTIRNLY NFNPGNFHYI QKTFDLTKKD
GFQFDITYNK LGTTQSISTR EQVTELITWS LNEINARFDK QFSFGEGPDS IESVEVKRRF
ALETLSNLLG GIGYFYGNQL IDRETEFDES QFTEIKLLNA KEEGPFELFT SVPSRGFFPR
GFYWDEGFHL LQIMEYDFDL AFEILASWFE MIEDDSGWIA REIILGNEAR SKVPQEFQVQ
NPNIANPPTL LLAFSEMLSR AIENIGDFNS DSYHQVMFNS RTAKFMTNNL EANPGLLTEY
AKKIYPKLLK HYNWFRKSQT GLIDEYEEIL EDEGIWDKIH KNEVYRWVGR TFTHCLPSGM
DDYPRAQPPD VAELNVDALA WVGVMTRSMK QIAHVLKLTQ DEQRYAQIEQ EVVENLDLLH
WSENDNCYCD ISIDPEDDEI REFVCHEGYV SVLPFALKLI PKNSPKLEKV VALMSDPEKI
FSDYGLLSLS RQDDYFGKDE NYWRGPIWMN INYLCLDAMR YYYPEVILDV AGEASNAKKL
YQSLKINLSN NIYKVWEEQG YCYENYSPID GHGTGAEHFT GWTALVVNIL GRF
