PYGL_MOUSE
ID PYGL_MOUSE Reviewed; 850 AA.
AC Q9ET01; Q3UKJ0;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Glycogen phosphorylase, liver form {ECO:0000250|UniProtKB:P06737};
DE EC=2.4.1.1 {ECO:0000250|UniProtKB:P06737};
GN Name=Pygl {ECO:0000312|MGI:MGI:97829};
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].
RC STRAIN=BTBR T+ tf/J; TISSUE=Liver;
RA McInerney M.M., Hurt C.B., Laipis P.J., Frost S.C.;
RT "Expression and regulation of glycogen phosphorylase in 3T3-L1
RT adipocytes.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Placenta;
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 PROTEIN SEQUENCE OF 2-10; 162-170; 173-185; 279-290; 353-359; 388-395;
RP 492-507 AND 643-650, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Kanor S., Bienvenut W.V.;
RL Submitted (OCT-2005) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524 AND SER-527, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, 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).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-364, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000250|UniProtKB:P06737}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000250|UniProtKB:P06737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733;
CC Evidence={ECO:0000250|UniProtKB:P06737};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P06737};
CC -!- ACTIVITY REGULATION: Allosterically regulated through the non-covalent
CC binding of metabolites, being activated by AMP and inhibited by ATP,
CC ADP, and glucose-6-phosphate. The activity is also controlled by post-
CC translational modifications including phosphorylation and acetylation.
CC {ECO:0000250|UniProtKB:P06737}.
CC -!- SUBUNIT: Homodimer; enzymatically active. Interacts with PPP1R3B;
CC recruits the phosphatase PP1 which dephosphorylates and inactivates
CC PYGL/glycogen phosphorylase. {ECO:0000250|UniProtKB:P06737}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P06737}.
CC -!- PTM: Acetylation, which is up-regulated by glucose and insulin and
CC down-regulated by glucagon, inhibits the glycogen phosphorylase
CC activity by promoting PPP1R3B-mediated recruitment of phosphatase PP1
CC and Ser-15 dephosphorylation. {ECO:0000250|UniProtKB:P06737}.
CC -!- PTM: Phosphorylation at Ser-15 converts inactive phosphorylase b into
CC active phosphorylase a. Dephosphorylation of Ser-15 by phosphatase PP1
CC inactivates the enzyme. {ECO:0000250|UniProtKB:P06737}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF288783; AAG00588.1; -; mRNA.
DR EMBL; AK140321; BAE24332.1; -; mRNA.
DR EMBL; AK145989; BAE26811.1; -; mRNA.
DR CCDS; CCDS25957.1; -.
DR RefSeq; NP_573461.2; NM_133198.2.
DR AlphaFoldDB; Q9ET01; -.
DR SMR; Q9ET01; -.
DR BioGRID; 225292; 13.
DR IntAct; Q9ET01; 2.
DR STRING; 10090.ENSMUSP00000071231; -.
DR BindingDB; Q9ET01; -.
DR ChEMBL; CHEMBL3008; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; Q9ET01; -.
DR PhosphoSitePlus; Q9ET01; -.
DR SwissPalm; Q9ET01; -.
DR CPTAC; non-CPTAC-3937; -.
DR EPD; Q9ET01; -.
DR jPOST; Q9ET01; -.
DR MaxQB; Q9ET01; -.
DR PaxDb; Q9ET01; -.
DR PeptideAtlas; Q9ET01; -.
DR PRIDE; Q9ET01; -.
DR ProteomicsDB; 301983; -.
DR Antibodypedia; 25; 317 antibodies from 31 providers.
DR Ensembl; ENSMUST00000071250; ENSMUSP00000071231; ENSMUSG00000021069.
DR GeneID; 110095; -.
DR KEGG; mmu:110095; -.
DR UCSC; uc007ntm.2; mouse.
DR CTD; 5836; -.
DR MGI; MGI:97829; Pygl.
DR VEuPathDB; HostDB:ENSMUSG00000021069; -.
DR eggNOG; KOG2099; Eukaryota.
DR GeneTree; ENSGT00950000183148; -.
DR HOGENOM; CLU_010198_1_0_1; -.
DR InParanoid; Q9ET01; -.
DR OMA; KHKRTFT; -.
DR OrthoDB; 240595at2759; -.
DR PhylomeDB; Q9ET01; -.
DR TreeFam; TF300309; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR BioGRID-ORCS; 110095; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Pygl; mouse.
DR PRO; PR:Q9ET01; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9ET01; protein.
DR Bgee; ENSMUSG00000021069; Expressed in granulocyte and 229 other tissues.
DR ExpressionAtlas; Q9ET01; baseline and differential.
DR Genevisible; Q9ET01; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016208; F:AMP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0032052; F:bile acid binding; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0005536; F:glucose binding; ISO:MGI.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0002060; F:purine nucleobase binding; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019842; F:vitamin binding; ISO:MGI.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR GO; GO:0005980; P:glycogen catabolic process; IMP:MGI.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:MGI.
DR GO; GO:0070266; P:necroptotic process; IGI:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; Carbohydrate metabolism; Cytoplasm;
KW Direct protein sequencing; Glycogen metabolism; Glycosyltransferase;
KW Nucleotide-binding; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..850
FT /note="Glycogen phosphorylase, liver form"
FT /id="PRO_0000188525"
FT BINDING 43..45
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P06737"
FT BINDING 76
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P06737"
FT BINDING 310
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P06737"
FT SITE 109
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT SITE 143
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT SITE 156
FT /note="May be involved in allosteric control"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 15
FT /note="Phosphoserine; by PHK; in form phosphorylase a"
FT /evidence="ECO:0000250|UniProtKB:P06737"
FT MOD_RES 364
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 470
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06737"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09811"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06737"
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P06737"
FT MOD_RES 796
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06737"
FT CONFLICT 198
FT /note="M -> V (in Ref. 1; AAG00588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 850 AA; 97463 MW; C4BFF6A9AA4E181E CRC64;
MAKPLTDQEK RRQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR DYYFALAHTV
RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IREGWQVEEA
DDWLRHGNPW EKARPEFMLP VHFYGRVEHT QTGTKWVDTQ VVLALPYDTP VPGYMNNTVN
TMRLWSARAP NDFNLQDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDVIR RFKASKFGSK DGMGTVFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL
PWAKAWEITK KTFAYTNHTV LPEALERWPV ELVEKLLPRH LEIIYEINQK HLDRIVALFP
KDISRMRRMS LIEEEGGKRI NMAHLCIVGC HAVNGVAKIH SDIVKTQVFK DFSELEPDKF
QNKTNGITPR RWLLLCNPGL ADLIAEKIGE DYVKDLSQLT KLHSFVSDDI FLREIAKVKQ
ENKLKFSQFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVITMYNR IKKDPKKFFV
PRTVIIGGKA APGYHMAKMI IKLITSVAEV VNNDPMVGSK LKVIFLENYR VSLAEKVIPA
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVDDVA
ALDKKGYEAK EYYEALPELK LVIDQIDNGF FSPNQPDLFK DIINMLFYHD RFKVFADYEA
YVKCQEKVSQ LYMNQKAWNT MVLKNIAASG KFSSDRTIKE YAKDIWNMEP SDLKISLSNE
SSNGVSANGK
