GCS1_SCHPO
ID GCS1_SCHPO Reviewed; 808 AA.
AC O14255; Q9US71;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable mannosyl-oligosaccharide glucosidase;
DE EC=3.2.1.106;
DE AltName: Full=Processing A-glucosidase I;
GN ORFNames=SPAC6G10.09;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 381-530, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
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: Cleaves the distal alpha 1,2-linked glucose residue from the
CC Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor highly specifically.
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB11295.1; -; Genomic_DNA.
DR EMBL; AB028004; BAA87308.1; -; Genomic_DNA.
DR PIR; T39059; T39059.
DR RefSeq; NP_594106.1; NM_001019530.2.
DR AlphaFoldDB; O14255; -.
DR SMR; O14255; -.
DR BioGRID; 278992; 3.
DR STRING; 4896.SPAC6G10.09.1; -.
DR CAZy; GH63; Glycoside Hydrolase Family 63.
DR iPTMnet; O14255; -.
DR MaxQB; O14255; -.
DR PaxDb; O14255; -.
DR PRIDE; O14255; -.
DR EnsemblFungi; SPAC6G10.09.1; SPAC6G10.09.1:pep; SPAC6G10.09.
DR GeneID; 2542534; -.
DR KEGG; spo:SPAC6G10.09; -.
DR PomBase; SPAC6G10.09; -.
DR VEuPathDB; FungiDB:SPAC6G10.09; -.
DR eggNOG; KOG2161; Eukaryota.
DR HOGENOM; CLU_007380_1_0_1; -.
DR InParanoid; O14255; -.
DR OMA; YWKAPLY; -.
DR PhylomeDB; O14255; -.
DR PRO; PR:O14255; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; IDA:PomBase.
DR GO; GO:0004573; F:Glc3Man9GlcNAc2 oligosaccharide glucosidase activity; IMP:PomBase.
DR GO; GO:0006491; P:N-glycan processing; IMP:PomBase.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:PomBase.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..808
FT /note="Probable mannosyl-oligosaccharide glucosidase"
FT /id="PRO_0000057714"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..808
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 808 AA; 92890 MW; 31871729E6F95254 CRC64;
MVSDMLGGNK RWILFGLLSF LLNCVLVSCS VEDIEKAAND SFLWGPYRPN LYVGIRPKIP
DSLMTGLMWS NVDDYARFSK MRHSAEHGDD IGAFGWKHYD VRRGGQQVID DFLMGIKLET
DFVKLPEGNW ALRVHGIPLP GAPTDLTTSL FFYAYVEGEG KVGTKVNHAN HVYMEGKTPD
LGKFRIQTFN RLGEHPVSPA SVDLESMVMD KDFFAGFNVK KEGAWRTSEL ILYLLDTKMK
VISDKEGYES LKDLPPAYST LTLPNLPSEE GLQFIQKVFK GEFMFDIVFN YASSKKISEE
MISQAIDKNL QEFEEKFQAT FPLKAPYDTE KAHQIFAHTA FSNLFGNVGF FTGDSIVSKN
PIELDDEDYE FMQGFESAAG KLAEGTAFHD IERSLFTIVP SRPHFPRGFY WDEGFHLLPV
GLWDNDFSLE ILKSWFSLVN EDGWVGREQI LGEEARSKVP DEFQTQYPDI ANPPTLILAL
KGYIERLQEQ QGKLNNRFSG EGEDYSLDDL EYLRSVSISN PEKSVQFLRD LFPLLLRHYE
WFRETQKGDF ETWERECFSQ VEGYRWRGRT YQHCLASGLD DYPRAQPPST AELHVDLLSW
MTSFTRSLHF VAEFLGETEE AEKLAGYENA MLRNLEDNHW DEEVQAYCDS SVDEYDDPIN
VCHKGYVTLL PMMLGLLPAD SGRLTSLLKL IRDENELWSP YGIRSLSMND VYFGTGENYW
RGPIWINMNY LILSSLYQNY INTPGPNQNL ARSIYEELRT NVVNNVFENW RQTGIFWEQY
DPTTGKGQRT KDFTGWTSLV VNIMSENY
