GLG1_YEAST
ID GLG1_YEAST Reviewed; 616 AA.
AC P36143; D6VXB9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 4.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Glycogenin-1 {ECO:0000303|PubMed:8524228};
DE EC=2.4.1.186 {ECO:0000269|PubMed:8524228};
DE AltName: Full=Glycogen synthesis initiator protein 1 {ECO:0000303|PubMed:8524228};
DE AltName: Full=Glycogenin glucosyltransferase 1 {ECO:0000303|PubMed:8524228};
GN Name=GLG1 {ECO:0000303|PubMed:8524228}; OrderedLocusNames=YKR058W;
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 CATALYTIC ACTIVITY.
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP FUNCTION, AND MUTAGENESIS OF TYR-230 AND TYR-598.
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 [5]
RP INDUCTION.
RX PubMed=10077186;
RX DOI=10.1002/(sici)1097-0061(199902)15:3<191::aid-yea358>3.0.co;2-o;
RA Parrou J.L., Enjalbert B., Plourde L., Bauche A., Gonzalez B., Francois J.;
RT "Dynamic responses of reserve carbohydrate metabolism under carbon and
RT nitrogen limitations in Saccharomyces cerevisiae.";
RL Yeast 15:191-203(1999).
RN [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [7]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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:8524228, 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:0000269|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:0000269|PubMed:8524228};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P46976};
CC -!- INDUCTION: Induced during the diauxic transition.
CC {ECO:0000269|PubMed:10077186}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA91646.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA82136.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA82136.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U25546; AAA91646.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z28283; CAA82136.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006944; DAA09209.1; -; Genomic_DNA.
DR PIR; S38134; S38134.
DR RefSeq; NP_012984.2; NM_001179848.1.
DR AlphaFoldDB; P36143; -.
DR SMR; P36143; -.
DR BioGRID; 34189; 64.
DR IntAct; P36143; 2.
DR MINT; P36143; -.
DR STRING; 4932.YKR058W; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR iPTMnet; P36143; -.
DR MaxQB; P36143; -.
DR PaxDb; P36143; -.
DR PRIDE; P36143; -.
DR EnsemblFungi; YKR058W_mRNA; YKR058W; YKR058W.
DR GeneID; 853932; -.
DR KEGG; sce:YKR058W; -.
DR SGD; S000001766; GLG1.
DR VEuPathDB; FungiDB:YKR058W; -.
DR eggNOG; KOG1950; Eukaryota.
DR GeneTree; ENSGT00940000175485; -.
DR HOGENOM; CLU_017171_4_1_1; -.
DR InParanoid; P36143; -.
DR OMA; KEWLTTF; -.
DR BioCyc; YEAST:MON3O-4054; -.
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:P36143; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36143; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 Glycogen biosynthesis; Glycoprotein; Manganese; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..616
FT /note="Glycogenin-1"
FT /id="PRO_0000215181"
FT REGION 283..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..575
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 247..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 247
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:0000250|UniProtKB:P46976"
FT CARBOHYD 598
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000305"
FT MUTAGEN 230
FT /note="Y->F: Eliminates glycogen accumulation; when
FT associated with F-598."
FT /evidence="ECO:0000269|PubMed:8900126"
FT MUTAGEN 598
FT /note="Y->F: Eliminates glycogen accumulation; when
FT associated with F-230."
FT /evidence="ECO:0000269|PubMed:8900126"
SQ SEQUENCE 616 AA; 69724 MW; 35DFF4A1E043FC8B CRC64;
MYKKLAIATL LYSADYLPGV FALGHQVNKL LEEAGKKGDI ETCLIVTTSL FNGTLSELAK
NILQSIYTKI VLVEPLNCQE ESIQKNSENL ALLERPELSF ALIKARLWEL TQFEQVLYLD
SDTLPLNKEF LKLFDIMSKQ TTSQVGAIAD IGWPDMFNSG VMMLIPDADT ASVLQNYIFE
NTSIDGSDQG ILNQFFNQNC CTDELVKDSF SREWVQLSFT YNVTIPNLGY QSSPAMNYFK
PSIKLIHFIG KHKPWSLWSQ KNFIKNEYHD QWNEVYEEFK EEHQLNNEVS KPKISDSDKT
ETPETITPVD APPSNEPTTN QEIDTISTVE ENVDNQNAEP VPNSDHSPAP NPVPLDFTKW
LTTFINKDHL TNQPVNESRE YSKENDNNII NSSSNRDQES PPNSTQELNS SYSVVSTQAD
SDEHQNAEEE DSTTDNASNS GEESHLDDIS TAASSNNNVS NQPDGKNFSN SKENNISVES
SPSNPEQKRS TDNIQKPSVS TNDLPDDVEP HTSVDDNIQY LEKDKEGYEE FLPDVYESNA
IDNEEEFFDD DARDATEGET KTSAVADKQE DMKLTAEETN QPQQEMPNFK FDWEDSDYLS
KVERCFPDDI FEYAVE
