GLU2B_YEAST
ID GLU2B_YEAST Reviewed; 702 AA.
AC Q04924; D6VSK3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glucosidase 2 subunit beta;
DE AltName: Full=Alpha-glucosidase 2 subunit beta;
DE AltName: Full=Alpha-glucosidase II subunit beta;
DE AltName: Full=Glucosidase II subunit beta;
DE Flags: Precursor;
GN Name=GTB1; OrderedLocusNames=YDR221W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
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 [5]
RP FUNCTION, INTERACTION WITH ROT2, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=16373354; DOI=10.1074/jbc.m510455200;
RA Wilkinson B.M., Purswani J., Stirling C.J.;
RT "Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein
RT processing in the endoplasmic reticulum.";
RL J. Biol. Chem. 281:6325-6333(2006).
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. Specifically required for the cleavage of the final
CC glucose. {ECO:0000269|PubMed:16373354}.
CC -!- SUBUNIT: Heterodimer of a catalytic subunit alpha (ROT2) and a subunit
CC beta (GTB1).
CC -!- INTERACTION:
CC Q04924; P38138: ROT2; NbExp=2; IntAct=EBI-37493, EBI-21021;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16373354}.
CC -!- MISCELLANEOUS: Present with 9760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z48612; CAA88501.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12063.1; -; Genomic_DNA.
DR PIR; S59428; S59428.
DR RefSeq; NP_010507.3; NM_001180529.3.
DR AlphaFoldDB; Q04924; -.
DR SMR; Q04924; -.
DR BioGRID; 32273; 91.
DR ComplexPortal; CPX-417; Glucosidase II complex.
DR DIP; DIP-4429N; -.
DR IntAct; Q04924; 1.
DR MINT; Q04924; -.
DR STRING; 4932.YDR221W; -.
DR iPTMnet; Q04924; -.
DR MaxQB; Q04924; -.
DR PaxDb; Q04924; -.
DR PRIDE; Q04924; -.
DR EnsemblFungi; YDR221W_mRNA; YDR221W; YDR221W.
DR GeneID; 851807; -.
DR KEGG; sce:YDR221W; -.
DR SGD; S000002629; GTB1.
DR VEuPathDB; FungiDB:YDR221W; -.
DR eggNOG; KOG2397; Eukaryota.
DR GeneTree; ENSGT00510000047770; -.
DR HOGENOM; CLU_419754_0_0_1; -.
DR InParanoid; Q04924; -.
DR OMA; VCDCCDC; -.
DR BioCyc; MetaCyc:G3O-29801-MON; -.
DR BioCyc; YEAST:G3O-29801-MON; -.
DR PRO; PR:Q04924; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04924; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:SGD.
DR GO; GO:0017177; C:glucosidase II complex; IPI:SGD.
DR GO; GO:0070880; P:fungal-type cell wall beta-glucan biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006491; P:N-glycan processing; IDA:ComplexPortal.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IMP:SGD.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR026874; Glucosidase_2_bsu.
DR InterPro; IPR039794; Gtb1-like.
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 Coiled coil; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..702
FT /note="Glucosidase 2 subunit beta"
FT /id="PRO_0000245572"
FT DOMAIN 537..689
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 435..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 163..228
FT /evidence="ECO:0000255"
FT COILED 478..517
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 539..552
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 646..675
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 660..687
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 702 AA; 79907 MW; 237D9756939D57DD CRC64;
MVSMFSLFLL LIEQSPLVAS LQQSQRHIVG VPWEKQHLYD SNEPDLTKWH CLNHEDIVLD
ISQINDGVCD CPDGSDEPGS AACVEDIFKS VAEGGGKVNK YFYCDNKGFI PRYIRKSEVA
DGICDCCDCS DELLSGYELF DAGSNCSQLK NEFDIMASKE LSSYREGKEA LEELERKYGT
KEEAITRGNC LEEDKEKASA EIKVLSNRLS ENRAKLEQLR GEYFNQLSHD PILYQFEQLN
STRLGSDILT SFTMVSRVSK GYQDIFKILS DLSEAYTPSL NDKVVNDNIK KFRKVRRRAE
KAKINADSKI DDEQADNLYL YFTEEVPQIF LKRESENTLR YVIGKSNFVQ ALVEGKINYT
NDILEYIREF RLIMDDISQN YNVNFQDAGV KSAVDSYKNY LGEYGELAEL EPAHPSESLL
RSLSEVTSFV NENAPKVLPP DAVESEQDTN SDHIGTSGDL RNKLKEILSK LNIFSSRKDL
VSLEKRFRSC ESQVSLLENE LKQKMDYKKL LDETEDEGTN STAGNLTELL ELMGSQSYCL
DDILDNYVYT ICFQRPMTEG VIYQAEDKVD GKKVLIGRFK TSGFNVDLNM EKYAEHLKAT
YDEKSDLISN LAAIQDDDGN MQHYVFGNLN ELNNGLVLEY ENGDQCWNGP RRSATVFVRC
SDKFKIRSVH EATKCNYIFD VVGPLGCNKT FEYEPPKFNL SE
