GLGB_MOUSE
ID GLGB_MOUSE Reviewed; 702 AA.
AC Q9D6Y9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=1,4-alpha-glucan-branching enzyme;
DE EC=2.4.1.18 {ECO:0000250|UniProtKB:Q04446};
DE AltName: Full=Brancher enzyme;
DE AltName: Full=Glycogen-branching enzyme;
GN Name=Gbe1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Required for normal glycogen accumulation. The alpha 1-6
CC branches of glycogen play an important role in increasing the
CC solubility of the molecule. {ECO:0000250|UniProtKB:Q04446}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC Evidence={ECO:0000250|UniProtKB:Q04446};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000250|UniProtKB:Q04446}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q04446}.
CC -!- DOMAIN: Binds its carbohydrate substrate close to the active site, but
CC also via regions close to the N-terminus; this may result in increased
CC affinity and therefore increased catalytic efficiency.
CC {ECO:0000250|UniProtKB:Q04446}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; AK009815; BAB26519.1; -; mRNA.
DR EMBL; AK050365; BAC34210.1; -; mRNA.
DR EMBL; BC017541; AAH17541.1; -; mRNA.
DR RefSeq; NP_083079.1; NM_028803.4.
DR AlphaFoldDB; Q9D6Y9; -.
DR SMR; Q9D6Y9; -.
DR BioGRID; 216557; 4.
DR IntAct; Q9D6Y9; 1.
DR MINT; Q9D6Y9; -.
DR STRING; 10090.ENSMUSP00000132603; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR iPTMnet; Q9D6Y9; -.
DR PhosphoSitePlus; Q9D6Y9; -.
DR SwissPalm; Q9D6Y9; -.
DR EPD; Q9D6Y9; -.
DR jPOST; Q9D6Y9; -.
DR MaxQB; Q9D6Y9; -.
DR PaxDb; Q9D6Y9; -.
DR PRIDE; Q9D6Y9; -.
DR ProteomicsDB; 271229; -.
DR Antibodypedia; 32014; 383 antibodies from 28 providers.
DR DNASU; 74185; -.
DR Ensembl; ENSMUST00000163832; ENSMUSP00000132603; ENSMUSG00000022707.
DR GeneID; 74185; -.
DR KEGG; mmu:74185; -.
DR UCSC; uc007zqu.2; mouse.
DR CTD; 2632; -.
DR MGI; MGI:1921435; Gbe1.
DR VEuPathDB; HostDB:ENSMUSG00000022707; -.
DR eggNOG; KOG0470; Eukaryota.
DR GeneTree; ENSGT00390000017040; -.
DR InParanoid; Q9D6Y9; -.
DR OrthoDB; 165238at2759; -.
DR PhylomeDB; Q9D6Y9; -.
DR TreeFam; TF300783; -.
DR Reactome; R-MMU-3322077; Glycogen synthesis.
DR UniPathway; UPA00164; -.
DR BioGRID-ORCS; 74185; 2 hits in 33 CRISPR screens.
DR ChiTaRS; Gbe1; mouse.
DR PRO; PR:Q9D6Y9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9D6Y9; protein.
DR Bgee; ENSMUSG00000022707; Expressed in intercostal muscle and 227 other tissues.
DR ExpressionAtlas; Q9D6Y9; baseline and differential.
DR Genevisible; Q9D6Y9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; ISS:UniProtKB.
DR GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IMP:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR43651; PTHR43651; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF02922; CBM_48; 1.
DR PIRSF; PIRSF000463; GlgB; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Acetylation; Glycogen biosynthesis; Glycogen storage disease;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
FT CHAIN 2..702
FT /note="1,4-alpha-glucan-branching enzyme"
FT /id="PRO_0000188776"
FT ACT_SITE 357
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 412
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 62..63
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
FT BINDING 91..93
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
FT BINDING 118..121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
FT BINDING 333..336
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
FT MOD_RES 173
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
SQ SEQUENCE 702 AA; 80364 MW; BE2284A5CED7C060 CRC64;
MAAPAAPAAG ETGPDARLEA ALADVPELAR LLEIDPYLKP FAADFQRRYK KFSQVLHDIG
ENEGGIDKFS RGYESFGIHR CSDGGIYCKE WAPGAEGVFL TGEFSGWNPF SHPYKKLEYG
KWELYIPPKQ NKSPLIPHGS KLKVVITSKS GEILYRISPW AKYVVRENNN VNYDWIHWAP
EDPYKFKHSR PKKPRSLRIY ESHVGISSHE GKIASYKHFT SNVLPRIKDL GYNCIQLMAI
MEHAYYASFG YQITSFFAAS SRYGTPEELK ELVDTAHSMG IVVLLDVVHS HASKNSEDGL
NMFDGTDSCY FHSGPRGTHD LWDSRLFIYS SWEVLRFLLS NIRWWLEEYC FDGFRFDGVT
SMLYHHHGMG QGFSGDYNEY FGLQVDEDAL IYLMLANHLA HTLYPDSITI AEDVSGMPAL
CSPTSQGGGG FDYRLAMAIP DKWIQLLKEF KDEDWNMGNI VYTLTNRRYL EKCVAYAESH
DQALVGDKTL AFWLMDAEMY TNMSVLAPFT PVIDRGIQLH KMIRLITHGL GGEGYLNFMG
NEFGHPEWLD FPRKGNNESY HYARRQFNLT DDDLLRYKFL NNFDRDMNRL EERCGWLSAP
QAYVSEKHEA NKTITFERAG LLFIFNFHPS KSYTDYRVGT ATPGKFKIVL DSDAAEYGGH
QRLDHNTNYF AEAFEHNGRP YSLLVYIPSR VALILQNVDL QN
