GLYG_MOUSE
ID GLYG_MOUSE Reviewed; 333 AA.
AC Q9R062; Q3TWR9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Glycogenin-1;
DE Short=GN-1;
DE Short=GN1;
DE EC=2.4.1.186 {ECO:0000250|UniProtKB:P46976};
GN Name=Gyg1; Synonyms=Gyg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=10542328; DOI=10.1016/s0167-4781(99)00159-1;
RA van Maanen M.-H., Fournier P.A., Palmer T.N., Abraham L.J.;
RT "Characterization of mouse glycogenin-1 cDNA and promoter region.";
RL Biochim. Biophys. Acta 1447:284-290(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE35197.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH GYS2, AND MUTAGENESIS OF LYS-305; TRP-308; TYR-315;
RP PHE-321; ILE-324; LEU-328 AND LEU-332.
RX PubMed=24982189; DOI=10.1073/pnas.1402926111;
RA Zeqiraj E., Tang X., Hunter R.W., Garcia-Rocha M., Judd A., Deak M.,
RA von Wilamowitz-Moellendorff A., Kurinov I., Guinovart J.J., Tyers M.,
RA Sakamoto K., Sicheri F.;
RT "Structural basis for the recruitment of glycogen synthase by glycogenin.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E2831-2840(2014).
CC -!- FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an
CC oligosaccharide primer that serves as substrate for glycogen synthase.
CC {ECO:0000250|UniProtKB:P46976}.
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:0000250|UniProtKB:P46976};
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:0000250|UniProtKB:P46976};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P13280};
CC Note=Divalent metal ions. Required for self-glucosylation. Manganese is
CC the most effective. {ECO:0000250|UniProtKB:P13280};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000250|UniProtKB:P46976}.
CC -!- SUBUNIT: Homodimer. Interacts (via C-terminus) with glycogen synthase
CC GYS1 (By similarity). Interacts (via C-terminus) with GYS2; required
CC for GYS2-mediated glycogen synthesis (PubMed:24982189).
CC {ECO:0000250|UniProtKB:P13280, ECO:0000250|UniProtKB:P46976,
CC ECO:0000269|PubMed:24982189}.
CC -!- TISSUE SPECIFICITY: Skeletal muscle, heart, to a lesser extent in
CC kidney, lung and brain. {ECO:0000269|PubMed:10542328}.
CC -!- PTM: Self-glycosylated by the transfer of glucose residues from UDP-
CC glucose to itself, forming an alpha-1,4-glycan of around 10 residues
CC attached to Tyr-195. {ECO:0000250|UniProtKB:P13280}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:P13280}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
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DR EMBL; AF114031; AAD48901.1; -; mRNA.
DR EMBL; AK159576; BAE35197.1; -; mRNA.
DR EMBL; CH466530; EDL34894.1; -; Genomic_DNA.
DR EMBL; BC029903; AAH29903.1; -; mRNA.
DR CCDS; CCDS50873.1; -.
DR RefSeq; NP_038783.1; NM_013755.3.
DR AlphaFoldDB; Q9R062; -.
DR SMR; Q9R062; -.
DR BioGRID; 205166; 6.
DR IntAct; Q9R062; 1.
DR STRING; 10090.ENSMUSP00000114019; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR GlyGen; Q9R062; 1 site.
DR iPTMnet; Q9R062; -.
DR PhosphoSitePlus; Q9R062; -.
DR REPRODUCTION-2DPAGE; Q9R062; -.
DR EPD; Q9R062; -.
DR MaxQB; Q9R062; -.
DR PaxDb; Q9R062; -.
DR PeptideAtlas; Q9R062; -.
DR PRIDE; Q9R062; -.
DR ProteomicsDB; 267636; -.
DR Antibodypedia; 33551; 210 antibodies from 28 providers.
DR DNASU; 27357; -.
DR Ensembl; ENSMUST00000178328; ENSMUSP00000136035; ENSMUSG00000019528.
DR GeneID; 27357; -.
DR KEGG; mmu:27357; -.
DR UCSC; uc056zrp.1; mouse.
DR CTD; 27357; -.
DR MGI; MGI:1351614; Gyg.
DR VEuPathDB; HostDB:ENSMUSG00000019528; -.
DR eggNOG; KOG1950; Eukaryota.
DR GeneTree; ENSGT00940000154674; -.
DR HOGENOM; CLU_017171_0_0_1; -.
DR InParanoid; Q9R062; -.
DR OMA; DYKAGED; -.
DR OrthoDB; 1424146at2759; -.
DR PhylomeDB; Q9R062; -.
DR BRENDA; 2.4.1.186; 3474.
DR Reactome; R-MMU-3322077; Glycogen synthesis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR UniPathway; UPA00164; -.
DR BioGRID-ORCS; 27357; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Gyg; mouse.
DR PRO; PR:Q9R062; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9R062; protein.
DR Bgee; ENSMUSG00000019528; Expressed in endocardial cushion and 257 other tissues.
DR ExpressionAtlas; Q9R062; baseline and differential.
DR Genevisible; Q9R062; MM.
DR GO; GO:0005536; F:glucose binding; ISO:MGI.
DR GO; GO:0008466; F:glycogenin glucosyltransferase activity; IMP:MGI.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0102751; F:UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:MGI.
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 Acetylation; Glycogen biosynthesis; Glycoprotein; Manganese; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT CHAIN 2..333
FT /note="Glycogenin-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000215177"
FT REGION 284..316
FT /note="Interaction with GYS1"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT REGION 290..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9..15
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 102..104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 133..135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 160..164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 212..218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 212
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT SITE 86
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT CARBOHYD 195
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT MUTAGEN 305
FT /note="K->A: No loss of interaction with GYS2."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 308
FT /note="W->A: No loss of interaction with GYS2."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 315
FT /note="Y->A: Severe loss of interaction with GYS2."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 321
FT /note="F->A: Severe loss of interaction with GYS2."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 324
FT /note="I->A: Severe loss of interaction with GYS2."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 328
FT /note="L->A: Severe loss of interaction with GYS2."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 332
FT /note="L->A: No loss of interaction with GYS2."
FT /evidence="ECO:0000269|PubMed:24982189"
SQ SEQUENCE 333 AA; 37402 MW; 2CE3F0C23166F2CB CRC64;
MTDQAFVTLT TNDAYAKGAL VLGSSLKQHR TTRRMVVLTS PQVSDSMRKV LETVFDDVIM
VDVLDSGDSA HLTLMKRPEL GITLTKLHCW SLTQYSKCVF MDADTLVLSN IDDLFEREEL
SAAPDPGWPD CFNSGVFVYQ PSIETYNQLL HLASEQGSFD GGDQGLLNTY FSGWATTDIT
KHLPFVYNLS SISIYSYLPA FKAFGKNAKV VHFLGRTKPW NYTYNPQTKS VNCDSQDPTV
SHPEFLNLWW DTFTTNVLPL LQHHGLVKDA SSYLMMEHVS GALSDLSFGE APAAPQPSMS
SEERKERWEQ GQADYMGADS FDNIKRKLDT YLQ
