GLU2B_SCHPO
ID GLU2B_SCHPO Reviewed; 506 AA.
AC Q9USH8; P78894;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Glucosidase 2 subunit beta;
DE AltName: Full=Alpha-glucosidase 2 subunit beta;
DE Flags: Precursor;
GN Name=gtb1; Synonyms=gls2-beta; ORFNames=SPCC825.02;
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 MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
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 [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10464333; DOI=10.1074/jbc.274.36.25899;
RA D'Alessio C., Fernandez F., Trombetta E.S., Parodi A.J.;
RT "Genetic evidence for the heterodimeric structure of glucosidase II. The
RT effect of disrupting the subunit-encoding genes on glycoprotein folding.";
RL J. Biol. Chem. 274:25899-25905(1999).
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).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19605557; DOI=10.1091/mbc.e09-04-0316;
RA Stigliano I.D., Caramelo J.J., Labriola C.A., Parodi A.J., D'Alessio C.;
RT "Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts
RT and mammals.";
RL Mol. Biol. Cell 20:3974-3984(2009).
RN [6]
RP FUNCTION, DOMAIN, INTERACTION WITH GLS2, AND MUTAGENESIS OF GLU-73;
RP GLU-114; GLU-456 AND TYR-462.
RX PubMed=21471007; DOI=10.1091/mbc.e11-01-0019;
RA Stigliano I.D., Alculumbre S.G., Labriola C.A., Parodi A.J., D'Alessio C.;
RT "Glucosidase II and N-glycan mannose content regulate the half-lives of
RT monoglucosylated species in vivo.";
RL Mol. Biol. Cell 22:1810-1823(2011).
CC -!- FUNCTION: Subunit of glucosidase 2, which cleaves sequentially the 2
CC innermost alpha-1,3-linked glucose residues from the
CC Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature
CC glycoproteins in the endoplasmic reticulum (ER). Specifically required
CC for the cleavage of the final glucose. The subunit beta retains the
CC catalytic subunit alpha in the ER. {ECO:0000269|PubMed:10464333,
CC ECO:0000269|PubMed:19605557, ECO:0000269|PubMed:21471007}.
CC -!- SUBUNIT: Heterodimer of a catalytic subunit alpha (gls2) and a subunit
CC beta (gtb1).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The N-terminal conserved region (G2B region) is required for
CC the interaction with gls2 and its translocation to the endoplasmic
CC reticulum, whereas the C-terminal conserved region (MRH region) is
CC involved in the recognition of N-glycans bearing from 5 to 9 mannose
CC units. {ECO:0000269|PubMed:21471007}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13906.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D89245; BAA13906.1; ALT_INIT; mRNA.
DR EMBL; CU329672; CAB58410.1; -; Genomic_DNA.
DR PIR; T41623; T41623.
DR PIR; T43152; T43152.
DR RefSeq; NP_588052.1; NM_001023044.2.
DR PDB; 2LVX; NMR; -; A=380-473.
DR PDB; 2N1H; NMR; -; A=380-473.
DR PDB; 4XQM; X-ray; 1.62 A; A=380-473.
DR PDBsum; 2LVX; -.
DR PDBsum; 2N1H; -.
DR PDBsum; 4XQM; -.
DR AlphaFoldDB; Q9USH8; -.
DR BMRB; Q9USH8; -.
DR SMR; Q9USH8; -.
DR BioGRID; 275309; 3.
DR STRING; 4896.SPCC825.02.1; -.
DR MaxQB; Q9USH8; -.
DR PaxDb; Q9USH8; -.
DR PRIDE; Q9USH8; -.
DR EnsemblFungi; SPCC825.02.1; SPCC825.02.1:pep; SPCC825.02.
DR GeneID; 2538725; -.
DR KEGG; spo:SPCC825.02; -.
DR PomBase; SPCC825.02; -.
DR VEuPathDB; FungiDB:SPCC825.02; -.
DR eggNOG; KOG2397; Eukaryota.
DR HOGENOM; CLU_016834_2_1_1; -.
DR InParanoid; Q9USH8; -.
DR OMA; KCVYRME; -.
DR PhylomeDB; Q9USH8; -.
DR BRENDA; 3.2.1.207; 5613.
DR PRO; PR:Q9USH8; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA: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:0033919; F:glucan 1,3-alpha-glucosidase activity; IDA:PomBase.
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; ISO:PomBase.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR026874; Glucosidase_2_bsu.
DR InterPro; IPR039794; Gtb1-like.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR036607; PRKCSH.
DR InterPro; IPR028146; PRKCSH_N.
DR PANTHER; PTHR12630; PTHR12630; 1.
DR PANTHER; PTHR12630:SF1; PTHR12630:SF1; 1.
DR Pfam; PF12999; PRKCSH-like; 1.
DR Pfam; PF13015; PRKCSH_1; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS51914; MRH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Disulfide bond; Endoplasmic reticulum;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..506
FT /note="Glucosidase 2 subunit beta"
FT /id="PRO_0000014209"
FT DOMAIN 279..474
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT COILED 172..243
FT /evidence="ECO:0000255"
FT COILED 338..374
FT /evidence="ECO:0000255"
FT MOTIF 503..506
FT /note="ER retrieval sequence"
FT DISULFID 86..108
FT /evidence="ECO:0000250"
FT DISULFID 431..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 445..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT MUTAGEN 73
FT /note="E->A: Impairs interaction with gls2."
FT /evidence="ECO:0000269|PubMed:21471007"
FT MUTAGEN 114
FT /note="E->A: Impairs interaction with gls2."
FT /evidence="ECO:0000269|PubMed:21471007"
FT MUTAGEN 456
FT /note="E->Q: Impairs N-glycan recognition; when associated
FT with Phe-462."
FT /evidence="ECO:0000269|PubMed:21471007"
FT MUTAGEN 462
FT /note="Y->F: Impairs N-glycan recognition; when associated
FT with Gln-456."
FT /evidence="ECO:0000269|PubMed:21471007"
FT CONFLICT 112
FT /note="S -> A (in Ref. 1; BAA13906)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="K -> T (in Ref. 1; BAA13906)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="L -> F (in Ref. 1; BAA13906)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="L -> S (in Ref. 1; BAA13906)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="D -> N (in Ref. 1; BAA13906)"
FT /evidence="ECO:0000305"
FT CONFLICT 489..491
FT /note="NEN -> YED (in Ref. 1; BAA13906)"
FT /evidence="ECO:0000305"
FT TURN 381..385
FT /evidence="ECO:0007829|PDB:4XQM"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:4XQM"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:4XQM"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:4XQM"
FT STRAND 410..419
FT /evidence="ECO:0007829|PDB:4XQM"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:4XQM"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:2LVX"
FT STRAND 438..445
FT /evidence="ECO:0007829|PDB:4XQM"
FT STRAND 450..458
FT /evidence="ECO:0007829|PDB:4XQM"
FT STRAND 461..468
FT /evidence="ECO:0007829|PDB:4XQM"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:4XQM"
SQ SEQUENCE 506 AA; 57075 MW; F7CA7C65B4035C56 CRC64;
MKFSQWYTLT APLLISSLYT VNAANDLRGV ASDKSDLYKP DAKGNWKCLG SDKLISFNQV
NDDYCDCPDG SDEPGTSACH NGKFFCKNTG YISSYIPSNR VDDTVCDCCD GSDESLIKCP
NTCAQKAREY LATLEEHNRL VKNGLKIREQ WALESAKKTD EVKARYKEIS DSLVAVSAEK
TQLSEKVEKM KRSTDLGAEA VLPLDFQDLR VALLSLVDER NEMQERLDIL TNLLDELTLL
YETDKFDETM KEAILSFEDL KEQEIRRKVS SDDVHNYLES CNNHLSMLTG PSEDITFSSL
IKDIKKILNS LVWNIKLSLI NFGILSPSAS STPLTDSESY RRFEAAQRDL DAAEENEKSL
EKEHTKLMHE LEYHHGWDLY RAIKGMETKR EIGGYTYKVV FYENVFQDSI LLGNFASQEG
NVLKYENGQS CWNGPHRSAI VTVECGVENE IVSVLEAQKC EYLIKMKSPA ACSPDQLKQS
LLNTQNSANE NAVNGMEDKE SSVDEL
