GLU2A_SCHPO
ID GLU2A_SCHPO Reviewed; 923 AA.
AC Q9US55;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Glucosidase 2 subunit alpha {ECO:0000250|UniProtKB:P38138};
DE EC=3.2.1.207 {ECO:0000269|PubMed:9774332, ECO:0000269|PubMed:9813085};
DE AltName: Full=Alpha-glucosidase II subunit alpha {ECO:0000250|UniProtKB:P38138};
DE AltName: Full=Glucosidase II gls2 {ECO:0000312|EMBL:CAB65603.1};
DE AltName: Full=Glucosidase II subunit alpha {ECO:0000250|UniProtKB:P38138};
DE Flags: Precursor;
GN Name=gls2 {ECO:0000312|EMBL:CAB65603.1}; ORFNames=SPAC1002.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=9774332; DOI=10.1093/emboj/17.20.5877;
RA Fernandez F., D'Alessio C., Fanchiotti S., Parodi A.J.;
RT "A misfolded protein conformation is not a sufficient condition for in vivo
RT glucosylation by the UDP-Glc:glycoprotein glucosyltransferase.";
RL EMBO J. 17:5877-5886(1998).
RN [3]
RP CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=9813085; DOI=10.1083/jcb.143.3.625;
RA Fanchiotti S., Fernandez F., D'Alessio C., Parodi A.J.;
RT "The UDP-Glc:Glycoprotein glucosyltransferase is essential for
RT Schizosaccharomyces pombe viability under conditions of extreme endoplasmic
RT reticulum stress.";
RL J. Cell Biol. 143:625-635(1998).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(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:0000250|UniProtKB:P38138}.
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:0000269|PubMed:9774332, ECO:0000269|PubMed:9813085};
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:0000269|PubMed:9774332,
CC ECO:0000269|PubMed:9813085};
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC -!- SUBUNIT: Heterodimer of a catalytic subunit alpha (gls2) and a subunit
CC beta (gtb1). {ECO:0000250|UniProtKB:P38138}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Gls2 and alg6 double mutant cells that transfer
CC Man(9)GlcNAc(2) and that are unable to remove the glucose units as they
CC lack gls2, grow at 37 degrees Celsius, but are characterized by swollen
CC cells, displaying pear, lemon and round shapes and have, when grown at
CC 28 degrees Celsius, a phenotype of growth and morphology almost
CC identical to that of wild-type cells, indicating that facilitation of
CC glycoprotein folding mediated by the interaction of calnexin and
CC monoglucosylated oligosaccharides does not necessarily require cycles
CC of reglucosylation and deglucosylation. The gls2 and alg6 double mutant
CC cells grown in the absence of exogenous stress show an induction of the
CC binding protein (BiP)-encoding mRNA. An incubation of intact gls2 and
CC alg6 mutant cells with [(14)C]glucose for 15 minutes in the absence of
CC 1-deoxynojirimycin (DNJ) leads to the production of protein-linked
CC Glc(1)Man(9)GlcNAc(2), Man(9)GlcNAc(2) and Man(8)GlcNAc(2).
CC {ECO:0000269|PubMed:9774332, ECO:0000269|PubMed:9813085}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000255}.
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DR EMBL; CU329670; CAB65603.1; -; Genomic_DNA.
DR RefSeq; NP_593490.1; NM_001018924.2.
DR AlphaFoldDB; Q9US55; -.
DR SMR; Q9US55; -.
DR BioGRID; 279705; 27.
DR STRING; 4896.SPAC1002.03c.1; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR MaxQB; Q9US55; -.
DR PaxDb; Q9US55; -.
DR PRIDE; Q9US55; -.
DR EnsemblFungi; SPAC1002.03c.1; SPAC1002.03c.1:pep; SPAC1002.03c.
DR GeneID; 2543277; -.
DR KEGG; spo:SPAC1002.03c; -.
DR PomBase; SPAC1002.03c; gls2.
DR VEuPathDB; FungiDB:SPAC1002.03c; -.
DR eggNOG; KOG1066; Eukaryota.
DR HOGENOM; CLU_000631_7_0_1; -.
DR InParanoid; Q9US55; -.
DR OMA; QAGIWYP; -.
DR PhylomeDB; Q9US55; -.
DR BRENDA; 3.2.1.207; 5613.
DR UniPathway; UPA00957; -.
DR PRO; PR:Q9US55; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
DR GO; GO:0017177; C:glucosidase II complex; ISO:PomBase.
DR GO; GO:0090599; F:alpha-glucosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:PomBase.
DR GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; ISO:PomBase.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; IDA:PomBase.
DR GO; GO:0006491; P:N-glycan processing; IDA:PomBase.
DR GO; GO:0006487; P:protein N-linked glycosylation; IC:PomBase.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..923
FT /note="Glucosidase 2 subunit alpha"
FT /id="PRO_0000372782"
FT ACT_SITE 524
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9C0Y4"
FT ACT_SITE 527
FT /evidence="ECO:0000250|UniProtKB:Q9C0Y4"
FT ACT_SITE 600
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9C0Y4"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 923 AA; 106282 MW; C2377CCD961B4AAF CRC64;
MRYHGICWFI FQAAIIFAIF GSCQGAFRHQ FKTAEQDGFA RRNRDLAKFQ KENLNWNGLF
QLNSISYNSG VVSGVFEQQS ENGENQHLFP FSISFLKNDV VRFQMDEKSR LEGTVEYEKN
ILTKRRFDAS TELGFNERAE VYGKDAHLLE QTSTSLTIRY GSHGRFTVIV TFSPFKVEFQ
RDGEPQVVLN ERHLLNMEYY RPKSSRTPEQ EANGMWDETF DNFHDSKPKG PESVGLDIKF
VDYGNVYGVP EHTSSLSLKE TNNSDAGYTE PYRLYNVDLF EYEVDSPMSQ YGAIPFMQAH
KPNSDVAVFW SNAAATWIDV EKESGPSPHS QSTSTHWYSE SGTLDLFIFL GPKASDVYES
YSALVGRPLL PPLFSIGYHQ CRWNYVSEED VLNVDAKFDE VDMPYDTIWL DIEYASKRRY
FTWDKATFPN PKAMLEKLDS KSRKLIVILD PHIKNDPNYF VSKELIDYNY AVKDKSGVDN
YNADCWPGNS VWVDFFNPEA QAWWGSLYEF DRFESDKNLW IWNDMNEPSV FRGPETSMHR
DAIHYGGWEH RDIHNIYGHK CINGTYNGLI KRGEGAVRPF ILTRSFFAGT SALAANWIGD
TMTTWEHLRG SIPTVLTNGI SGMAFSGADV AGFFGNPDAE LFVRWYETAI FYPFFRAHAH
IDTKRREPWL YGEPYTSLVR ELLRIRYRLL PTWYTAFYNS HTHGFPILYP QFLMHPEDEE
GFAIDDQFYV GDSGLLVKPV THPSIDKITI YLADDEVYFD LHDHTEYAGK GHQVVPAPLG
RVPVLLRGGN ILITRERIRR AAELTRNDPF TLTIAVSKIG KNASGFLYLD DGVTFNYKKG
EYLIRHFSYE NGILTMKDSH SNPPVSPKYS SSQKHLKVER INIYGEQTRK SIKIRKIIDS
EVTEWDVSVD DSGCIRNPQL FLV
