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Protein

Glucosidase 2 subunit alpha

Gene

gls2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalytic subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature glycoproteins.By similarity

Catalytic activityi

Hydrolysis of terminal (1->3)-alpha-D-glucosidic links in (1->3)-alpha-D-glucans.2 Publications

Pathwayi: N-glycan metabolism

This protein is involved in the pathway N-glycan metabolism, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway N-glycan metabolism and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei524 – 5241NucleophileBy similarity
Active sitei527 – 5271By similarity
Active sitei600 – 6001Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

UniPathwayiUPA00957.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucosidase 2 subunit alphaBy similarity (EC:3.2.1.84)
Alternative name(s):
Alpha-glucosidase II subunit alphaBy similarity
Glucosidase II gls2Imported
Glucosidase II subunit alphaBy similarity
Gene namesi
Name:gls2Imported
ORF Names:SPAC1002.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1002.03c.
PomBaseiSPAC1002.03c. gls2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: PomBase
  • glucosidase II complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Gls2 and alg6 double mutant cells that transfer Man9GlcNAc2 and that are unable to remove the glucose units as they lack gls2, grow at 37 degrees Celsius, but are characterized by swollen cells, displaying pear, lemon and round shapes and have, when grown at 28 degrees Celsius, a phenotype of growth and morphology almost identical to that of wild-type cells, indicating that facilitation of glycoprotein folding mediated by the interaction of calnexin and monoglucosylated oligosaccharides does not necessarily require cycles of reglucosylation and deglucosylation. The gls2 and alg6 double mutant cells grown in the absence of exogenous stress show an induction of the binding protein (BiP)-encoding mRNA. An incubation of intact gls2 and alg6 mutant cells with [(14)C]glucose for 15 minutes in the absence of 1-deoxynojirimycin (DNJ) leads to the production of protein-linked Glc1Man9GlcNAc2, Man9GlcNAc2 and Man8GlcNAc2.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 923898Glucosidase 2 subunit alphaPRO_0000372782Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence analysis
Glycosylationi563 – 5631N-linked (GlcNAc...)Sequence analysis
Glycosylationi822 – 8221N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9US55.

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit alpha (gls2) and a subunit beta (gtb1).By similarity

Protein-protein interaction databases

BioGridi279705. 26 interactions.
MINTiMINT-4707783.

Structurei

3D structure databases

ProteinModelPortaliQ9US55.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000115864.
InParanoidiQ9US55.
KOiK05546.
OMAiVNYEFAN.
OrthoDBiEOG7G7KXG.
PhylomeDBiQ9US55.

Family and domain databases

InterProiIPR033403. DUF5110.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF17137. DUF5110. 1 hit.
PF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 3 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9US55-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYHGICWFI FQAAIIFAIF GSCQGAFRHQ FKTAEQDGFA RRNRDLAKFQ
60 70 80 90 100
KENLNWNGLF QLNSISYNSG VVSGVFEQQS ENGENQHLFP FSISFLKNDV
110 120 130 140 150
VRFQMDEKSR LEGTVEYEKN ILTKRRFDAS TELGFNERAE VYGKDAHLLE
160 170 180 190 200
QTSTSLTIRY GSHGRFTVIV TFSPFKVEFQ RDGEPQVVLN ERHLLNMEYY
210 220 230 240 250
RPKSSRTPEQ EANGMWDETF DNFHDSKPKG PESVGLDIKF VDYGNVYGVP
260 270 280 290 300
EHTSSLSLKE TNNSDAGYTE PYRLYNVDLF EYEVDSPMSQ YGAIPFMQAH
310 320 330 340 350
KPNSDVAVFW SNAAATWIDV EKESGPSPHS QSTSTHWYSE SGTLDLFIFL
360 370 380 390 400
GPKASDVYES YSALVGRPLL PPLFSIGYHQ CRWNYVSEED VLNVDAKFDE
410 420 430 440 450
VDMPYDTIWL DIEYASKRRY FTWDKATFPN PKAMLEKLDS KSRKLIVILD
460 470 480 490 500
PHIKNDPNYF VSKELIDYNY AVKDKSGVDN YNADCWPGNS VWVDFFNPEA
510 520 530 540 550
QAWWGSLYEF DRFESDKNLW IWNDMNEPSV FRGPETSMHR DAIHYGGWEH
560 570 580 590 600
RDIHNIYGHK CINGTYNGLI KRGEGAVRPF ILTRSFFAGT SALAANWIGD
610 620 630 640 650
TMTTWEHLRG SIPTVLTNGI SGMAFSGADV AGFFGNPDAE LFVRWYETAI
660 670 680 690 700
FYPFFRAHAH IDTKRREPWL YGEPYTSLVR ELLRIRYRLL PTWYTAFYNS
710 720 730 740 750
HTHGFPILYP QFLMHPEDEE GFAIDDQFYV GDSGLLVKPV THPSIDKITI
760 770 780 790 800
YLADDEVYFD LHDHTEYAGK GHQVVPAPLG RVPVLLRGGN ILITRERIRR
810 820 830 840 850
AAELTRNDPF TLTIAVSKIG KNASGFLYLD DGVTFNYKKG EYLIRHFSYE
860 870 880 890 900
NGILTMKDSH SNPPVSPKYS SSQKHLKVER INIYGEQTRK SIKIRKIIDS
910 920
EVTEWDVSVD DSGCIRNPQL FLV
Length:923
Mass (Da):106,282
Last modified:May 1, 2000 - v1
Checksum:iC2377CCD961B4AAF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB65603.1.
RefSeqiNP_593490.1. NM_001018924.2.

Genome annotation databases

EnsemblFungiiSPAC1002.03c.1; SPAC1002.03c.1:pep; SPAC1002.03c.
GeneIDi2543277.
KEGGispo:SPAC1002.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB65603.1.
RefSeqiNP_593490.1. NM_001018924.2.

3D structure databases

ProteinModelPortaliQ9US55.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279705. 26 interactions.
MINTiMINT-4707783.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Proteomic databases

MaxQBiQ9US55.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1002.03c.1; SPAC1002.03c.1:pep; SPAC1002.03c.
GeneIDi2543277.
KEGGispo:SPAC1002.03c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1002.03c.
PomBaseiSPAC1002.03c. gls2.

Phylogenomic databases

HOGENOMiHOG000115864.
InParanoidiQ9US55.
KOiK05546.
OMAiVNYEFAN.
OrthoDBiEOG7G7KXG.
PhylomeDBiQ9US55.

Enzyme and pathway databases

UniPathwayiUPA00957.

Miscellaneous databases

PROiQ9US55.

Family and domain databases

InterProiIPR033403. DUF5110.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF17137. DUF5110. 1 hit.
PF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase."
    Fernandez F., D'Alessio C., Fanchiotti S., Parodi A.J.
    EMBO J. 17:5877-5886(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, DISRUPTION PHENOTYPE.
  3. "The UDP-Glc:Glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress."
    Fanchiotti S., Fernandez F., D'Alessio C., Parodi A.J.
    J. Cell Biol. 143:625-635(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, DISRUPTION PHENOTYPE.
  4. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGLU2A_SCHPO
AccessioniPrimary (citable) accession number: Q9US55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.