GLG2_YEAST
ID GLG2_YEAST Reviewed; 380 AA.
AC P47011; D6VW47;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Glycogenin-2 {ECO:0000303|PubMed:8524228};
DE EC=2.4.1.186 {ECO:0000305|PubMed:8524228};
DE AltName: Full=Glycogen synthesis initiator protein 2 {ECO:0000303|PubMed:8524228};
DE AltName: Full=Glycogenin glucosyltransferase 2 {ECO:0000303|PubMed:8524228};
GN Name=GLG2 {ECO:0000303|PubMed:8524228}; OrderedLocusNames=YJL137C;
GN ORFNames=J0663;
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 [GENOMIC DNA], FUNCTION, AND INTERACTION WITH GSY2.
RX PubMed=8524228; DOI=10.1128/mcb.15.12.6632;
RA Cheng C., Mu J., Farkas I., Huang D., Goebl M.G., Roach P.J.;
RT "Requirement of the self-glucosylating initiator proteins Glg1p and Glg2p
RT for glycogen accumulation in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 15:6632-6640(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8813765;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT chromosome X reveals 14 known genes and 13 new open reading frames
RT including homologues of genes clustered on the right arm of chromosome
RT XI.";
RL Yeast 12:787-797(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 228-234 AND 239-244, FUNCTION, AND MUTAGENESIS OF
RP TYR-230; TYR-232 AND TYR-367.
RX PubMed=8900126; DOI=10.1074/jbc.271.43.26554;
RA Mu J., Cheng C., Roach P.J.;
RT "Initiation of glycogen synthesis in yeast. Requirement of multiple
RT tyrosine residues for function of the self-glucosylating Glg proteins in
RT vivo.";
RL J. Biol. Chem. 271:26554-26560(1996).
RN [6]
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 [7]
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 [8]
RP FUNCTION, AND GLYCOSYLATION AT TYR-230 AND TYR-232.
RX PubMed=15479227; DOI=10.1111/j.1432-1033.2004.04333.x;
RA Albrecht T., Haebel S., Koch A., Krause U., Eckermann N., Steup M.;
RT "Yeast glycogenin (Glg2p) produced in Escherichia coli is simultaneously
RT glucosylated at two vicinal tyrosine residues but results in a reduced
RT bacterial glycogen accumulation.";
RL Eur. J. Biochem. 271:3978-3989(2004).
CC -!- FUNCTION: Self-glucosylating initiator of glycogen synthesis. Catalyzes
CC the formation of a short alpha (1,4)-glucosyl chain covalently attached
CC via a glucose 1-O-tyrosyl linkage to internal tyrosine residues. These
CC chains act as primers for the elongation reaction catalyzed by glycogen
CC synthase. Capable of transferring glucosyl residues to unbound
CC acceptors such as free oligoglucans or oligoglucan derivatives.
CC {ECO:0000269|PubMed:15479227, ECO:0000269|PubMed:8524228,
CC ECO:0000269|PubMed:8900126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-
CC glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360,
CC Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140573; EC=2.4.1.186;
CC Evidence={ECO:0000305|PubMed:8524228};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-
CC D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + H(+)
CC + UDP; Xref=Rhea:RHEA:56560, Rhea:RHEA-COMP:14606, Rhea:RHEA-
CC COMP:14607, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140574; EC=2.4.1.186;
CC Evidence={ECO:0000305|PubMed:8524228};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P46976};
CC -!- SUBUNIT: Interacts with glycogen synthase GSY2.
CC {ECO:0000269|PubMed:8524228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 981 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
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DR EMBL; U25436; AAA91644.1; -; Genomic_DNA.
DR EMBL; X87371; CAA60818.1; -; Genomic_DNA.
DR EMBL; Z49412; CAA89432.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08663.1; -; Genomic_DNA.
DR PIR; S55176; S55176.
DR RefSeq; NP_012398.1; NM_001181570.1.
DR AlphaFoldDB; P47011; -.
DR SMR; P47011; -.
DR BioGRID; 33620; 53.
DR DIP; DIP-1345N; -.
DR IntAct; P47011; 2.
DR MINT; P47011; -.
DR STRING; 4932.YJL137C; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR MaxQB; P47011; -.
DR PaxDb; P47011; -.
DR PRIDE; P47011; -.
DR EnsemblFungi; YJL137C_mRNA; YJL137C; YJL137C.
DR GeneID; 853304; -.
DR KEGG; sce:YJL137C; -.
DR SGD; S000003673; GLG2.
DR VEuPathDB; FungiDB:YJL137C; -.
DR eggNOG; KOG1950; Eukaryota.
DR GeneTree; ENSGT00940000175485; -.
DR HOGENOM; CLU_017171_4_1_1; -.
DR InParanoid; P47011; -.
DR OMA; QIEPVIP; -.
DR BioCyc; YEAST:MON3O-4031; -.
DR Reactome; R-SCE-3322077; Glycogen synthesis.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-70221; Glycogen breakdown (glycogenolysis).
DR PRO; PR:P47011; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47011; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0008466; F:glycogenin glucosyltransferase activity; IGI:SGD.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102751; F:UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IGI:SGD.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycogen biosynthesis; Glycoprotein;
KW Manganese; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..380
FT /note="Glycogenin-2"
FT /id="PRO_0000215182"
FT REGION 331..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 120..122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 158..160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 185..189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 249..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 249
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT SITE 104
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT CARBOHYD 230
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000269|PubMed:15479227"
FT CARBOHYD 232
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000269|PubMed:15479227"
FT CARBOHYD 367
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000255"
FT MUTAGEN 230
FT /note="Y->F: Eliminates glycogen accumulation; when
FT associated with F-232 and F-367."
FT /evidence="ECO:0000269|PubMed:8900126"
FT MUTAGEN 232
FT /note="Y->F: Eliminates glycogen accumulation; when
FT associated with F-230 and F-367."
FT /evidence="ECO:0000269|PubMed:8900126"
FT MUTAGEN 367
FT /note="Y->F: Eliminates glycogen accumulation; when
FT associated with F-230 and F-232."
FT /evidence="ECO:0000269|PubMed:8900126"
FT CONFLICT 241
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 44546 MW; 36BDF556DEF397C0 CRC64;
MAKKVAICTL LYSRDYLPGA LTLAYQLQKL LKHAVVEDEI TLCLLIEKKL FGDEFKPQEI
ALIRSLFKEI IIIEPLKDQE KSIEKNKANL ELLKRPELSH TLLKARLWEL VQFDQVLFLD
ADTLPLNKEF FEILRLYPEQ TRFQIAAVPD IGWPDMFNTG VLLLIPDLDM ATSLQDFLIK
TVSIDGADQG IFNQFFNPIC NYSKEVLHKV SPLMEWIRLP FTYNVTMPNY GYQSSPAMNF
FQQHIRLIHF IGTFKPWSRN TTDYDDHYYQ LWRSTQRELY SECHLSNYFT HLQLGNIETE
TNFYHEPPCL QDLLNHGKRE NQKHVDLDIT SVDRNASQKS TAEKHDIEKP TSKPQSAFKF
DWESTDYLDR VQRAFPKPDT
