PYGL_RAT
ID PYGL_RAT Reviewed; 850 AA.
AC P09811;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Glycogen phosphorylase, liver form {ECO:0000305|PubMed:1339293};
DE EC=2.4.1.1 {ECO:0000250|UniProtKB:P06737};
GN Name=Pygl {ECO:0000312|RGD:620687}; Synonyms=Lgp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1339293; DOI=10.1016/0167-4781(92)90453-7;
RA Schiebel K., Pekel E., Mayer D.;
RT "The nucleotide sequence of rat liver glycogen phosphorylase cDNA.";
RL Biochim. Biophys. Acta 1130:349-351(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8482535; DOI=10.1016/0378-1119(93)90368-d;
RA Herrick K.R., Gorin F.A., Park E.A., Tait R.C.;
RT "Characterization of the 5' flanking region of the gene encoding rat liver
RT glycogen phosphorylase.";
RL Gene 126:203-211(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 333-430.
RX PubMed=2575583; DOI=10.1016/0888-7543(89)90017-7;
RA Glaser T., Matthews K.E., Hudson J.W., Seth P., Houseman D.E., Crerar M.M.;
RT "Localization of the muscle, liver, and brain glycogen phosphorylase genes
RT on linkage maps of mouse chromosomes 19, 12, and 2, respectively.";
RL Genomics 5:510-521(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 441-850.
RC TISSUE=Liver;
RX PubMed=2424788; DOI=10.1016/0014-5793(86)80702-5;
RA Osawa S., Chiu R.H., McDonough A., Miller T.B. Jr., Johnson G.L.;
RT "Isolation of partial cDNAs for rat liver and muscle glycogen phosphorylase
RT isozymes.";
RL FEBS Lett. 202:282-288(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 835-850.
RC STRAIN=Zucker;
RX PubMed=1765272; DOI=10.1016/0378-1119(91)90620-q;
RA Froman B.E., Tait R.C., Gorin F.A., Horwitz B.A., Stern J.S.;
RT "The gene encoding rat liver glycogen phosphorylase contains multiple
RT polyadenylation signal sequences.";
RL Gene 109:269-274(1991).
RN [7]
RP INTERACTION WITH PPP1R3B.
RX PubMed=7720853; DOI=10.1016/0014-5793(95)00197-h;
RA Moorhead G., MacKintosh C., Morrice N., Cohen P.;
RT "Purification of the hepatic glycogen-associated form of protein
RT phosphatase-1 by microcystin-Sepharose affinity chromatography.";
RL FEBS Lett. 362:101-105(1995).
RN [8]
RP INTERACTION WITH PPP1R3B.
RX PubMed=7498521; DOI=10.1016/0014-5793(95)01184-g;
RA Doherty M.J., Moorhead G., Morrice N., Cohen P., Cohen P.T.W.;
RT "Amino acid sequence and expression of the hepatic glycogen-binding (GL)-
RT subunit of protein phosphatase-1.";
RL FEBS Lett. 375:294-298(1995).
RN [9]
RP INTERACTION WITH PPP1R3B.
RX PubMed=9841883; DOI=10.1042/bj3360699;
RA Armstrong C.G., Doherty M.J., Cohen P.T.W.;
RT "Identification of the separate domains in the hepatic glycogen-targeting
RT subunit of protein phosphatase 1 that interact with phosphorylase a,
RT glycogen and protein phosphatase 1.";
RL Biochem. J. 336:699-704(1998).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561 AND SER-639, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). Interacts
CC with PPP1R3B; recruits the phosphatase PP1 which dephosphorylates and
CC inactivates PYGL/glycogen phosphorylase (PubMed:7720853,
CC PubMed:7498521, PubMed:9841883). {ECO:0000250|UniProtKB:P06737,
CC ECO:0000269|PubMed:7498521, ECO:0000269|PubMed:7720853,
CC ECO:0000269|PubMed:9841883}.
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}.
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DR EMBL; X63515; CAA45083.1; -; mRNA.
DR EMBL; BC070901; AAH70901.1; -; mRNA.
DR EMBL; M85280; AAA41254.1; -; Genomic_DNA.
DR EMBL; J03080; AAA41986.1; -; mRNA.
DR EMBL; X04069; CAA27704.1; -; mRNA.
DR EMBL; M59460; AAA41987.1; -; mRNA.
DR PIR; S22338; S22338.
DR RefSeq; NP_071604.1; NM_022268.1.
DR AlphaFoldDB; P09811; -.
DR SMR; P09811; -.
DR BioGRID; 248952; 1.
DR IntAct; P09811; 2.
DR MINT; P09811; -.
DR STRING; 10116.ENSRNOP00000009183; -.
DR BindingDB; P09811; -.
DR ChEMBL; CHEMBL3239; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; P09811; -.
DR PhosphoSitePlus; P09811; -.
DR jPOST; P09811; -.
DR PaxDb; P09811; -.
DR PRIDE; P09811; -.
DR Ensembl; ENSRNOT00000009183; ENSRNOP00000009183; ENSRNOG00000006388.
DR GeneID; 64035; -.
DR KEGG; rno:64035; -.
DR UCSC; RGD:620687; rat.
DR CTD; 5836; -.
DR RGD; 620687; Pygl.
DR eggNOG; KOG2099; Eukaryota.
DR GeneTree; ENSGT00950000183148; -.
DR HOGENOM; CLU_010198_1_0_1; -.
DR InParanoid; P09811; -.
DR OMA; KHKRTFT; -.
DR OrthoDB; 240595at2759; -.
DR PhylomeDB; P09811; -.
DR TreeFam; TF300309; -.
DR BRENDA; 2.4.1.1; 5301.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-70221; Glycogen breakdown (glycogenolysis).
DR PRO; PR:P09811; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000006388; Expressed in liver and 18 other tissues.
DR Genevisible; P09811; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016208; F:AMP binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0032052; F:bile acid binding; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
DR GO; GO:0005536; F:glucose binding; ISO:RGD.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0002060; F:purine nucleobase binding; ISO:RGD.
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:RGD.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IMP:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0005980; P:glycogen catabolic process; IDA:RGD.
DR GO; GO:0005977; P:glycogen metabolic process; IDA:RGD.
DR GO; GO:0070266; P:necroptotic process; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
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 Glycogen metabolism; Glycosyltransferase; Nucleotide-binding;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06737"
FT CHAIN 2..850
FT /note="Glycogen phosphorylase, liver form"
FT /id="PRO_0000188526"
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:0000250|UniProtKB:P06737"
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:0000250|UniProtKB:Q9ET01"
FT MOD_RES 470
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06737"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ET01"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 667
FT /note="I -> V (in Ref. 5; CAA27704)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 850 AA; 97483 MW; 0BE9A641DFFF3E0D CRC64;
MAKPLTDQEK RRQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR DYYFALAHTV
RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IREGWQVEEA
DDWLRHGNPW EKARPEFMLP VHFYGRVEHT QAGTKWVDTQ VVLALPYDTP VPGYMNNTVN
TMRLWSARAP NDFNLQDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDVIR RFKASKFGSK DGVGTVFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL
PWSKAWEITK KTFAYTNHTV LPEALERWPV DLVEKLLPRH LQIIYEINQK HLDRIVALFP
KDIDRMRRMS LIEEEGGKRI NMAHLCIVGC HAVNGVAKIH SDIVKTQVFK DFSELEPDKF
QNKTNGITPR RWLLLCNPGL ADLIAEKIGE DYVKDLSQLT KLHSFVGDDI FLREIAKVKQ
ENKLKFSQFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVITMYNR IKKDPKKFFV
PRTVIIGGKA APGYHMAKMI IKLVTSVAEV VNNDPMVGSK LKVIFLENYR VSLAEKVIPA
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVDDVA
ALDKKGYEAK EYYEALPELK LVIDQIDNGF FSPNQPDLFK DIINMLFYHD RFKVFADYEA
YVKCQEKVSQ LYMNQKAWNT MVLRNIAASG KFSSDRTIRE YAKDIWNMEP SDLKISLSKE
SSNGVNANGK
