PYGM_RAT
ID PYGM_RAT Reviewed; 842 AA.
AC P09812;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glycogen phosphorylase, muscle form {ECO:0000305|PubMed:7916624};
DE EC=2.4.1.1 {ECO:0000250|UniProtKB:P11217};
DE AltName: Full=Myophosphorylase;
GN Name=Pygm {ECO:0000312|RGD:3461};
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].
RX PubMed=7916624; DOI=10.1016/0167-4838(93)90248-p;
RA Hudson J.W., Hefferon K.L., Crerar M.M.;
RT "Comparative analysis of species-independent, isozyme-specific amino-acid
RT substitutions in mammalian muscle, brain and liver glycogen
RT phosphorylases.";
RL Biochim. Biophys. Acta 1164:197-208(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 566-762.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 763-842.
RX PubMed=3840433; DOI=10.1111/j.1432-1033.1985.tb09193.x;
RA Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J.,
RA Crerar M.M.;
RT "Comparative sequence analysis of rat, rabbit, and human muscle glycogen
RT phosphorylase cDNAs.";
RL Eur. J. Biochem. 152:267-274(1985).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; TYR-204; TYR-227;
RP TYR-473; SER-514; SER-747 AND SER-748, AND IDENTIFICATION BY MASS
RP 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:P11217}.
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:P11217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733;
CC Evidence={ECO:0000250|UniProtKB:P11217};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P00489};
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.
CC {ECO:0000250|UniProtKB:P11217}.
CC -!- SUBUNIT: Homodimer. Homotetramer; to form the enzymatically active
CC phosphorylase A. {ECO:0000250|UniProtKB:P11217}.
CC -!- PTM: Phosphorylation of Ser-15 converts phosphorylase B
CC (unphosphorylated) to phosphorylase A. {ECO:0000250|UniProtKB:P11217}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; L10669; AAA41253.1; -; mRNA.
DR EMBL; X03032; CAA26835.1; -; mRNA.
DR PIR; S34624; S34624.
DR AlphaFoldDB; P09812; -.
DR SMR; P09812; -.
DR IntAct; P09812; 2.
DR MINT; P09812; -.
DR STRING; 10116.ENSRNOP00000028636; -.
DR BindingDB; P09812; -.
DR ChEMBL; CHEMBL4105822; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; P09812; -.
DR PhosphoSitePlus; P09812; -.
DR jPOST; P09812; -.
DR PaxDb; P09812; -.
DR PRIDE; P09812; -.
DR UCSC; RGD:3461; rat.
DR RGD; 3461; Pygm.
DR eggNOG; KOG2099; Eukaryota.
DR InParanoid; P09812; -.
DR PhylomeDB; P09812; -.
DR BRENDA; 2.4.1.1; 5301.
DR Reactome; R-RNO-70221; Glycogen breakdown (glycogenolysis).
DR PRO; PR:P09812; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
DR GO; GO:0016208; F:AMP binding; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:RGD.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0097159; F:organic cyclic compound binding; IDA:RGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:RGD.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:RGD.
DR GO; GO:0005980; P:glycogen catabolic process; IDA:RGD.
DR GO; GO:0005977; P:glycogen metabolic process; IDA:RGD.
DR GO; GO:0051591; P:response to cAMP; IDA:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:RGD.
DR GO; GO:0010033; P:response to organic substance; IDA: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;
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:P00489"
FT CHAIN 2..842
FT /note="Glycogen phosphorylase, muscle form"
FT /id="PRO_0000188533"
FT BINDING 43
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P11217"
FT BINDING 76
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT BINDING 310..319
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P11217"
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-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT MOD_RES 15
FT /note="Phosphoserine; by PHK; in form phosphorylase A"
FT /evidence="ECO:0000250|UniProtKB:P11217"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 204
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUB3"
FT MOD_RES 473
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P00489"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 640..641
FT /note="RF -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="Q -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="V -> L (in Ref. 3; CAA26835)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 842 AA; 97273 MW; EA30BBB63FE69700 CRC64;
MSRPLSDQDK RKQISVRGLA GVENVSDLKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV
RDHLVDRWIR TQQHYYAKDP KRIYYLSLEL YMGRTLQNTM VNLALENACD EATYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ICGGWQMEEA
DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN
TMRLWSAKAP PYFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDKFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL IRILVDLERL
DWDKAWDVTV KTCAYTNHTV LPEALERWPV HLMETLLPRH LQIIYEINQR FLNRVAAAFP
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF
QNKTNGITPR RWLVLCNPGL AEVIAERIGE EYISDLDQLR KLLSYLDDQA FIRDVAKVKQ
ENKLKFSAYL ETEYKVHINP NSLFDVQVKR IHEYKRQLLN CLHIITLYNR IKREPNRFMV
PRTIMIGGKA APGYHMAKMI IKLITAIGDV VNHDPAVGDR FRVIFLENYR VSLAEKVIPA
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEDNFF IFGMRVEDVE
RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF FSPKQPDLFK DIVNMVMHHD RFKVFADYEE
YIKCQDKVSE LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGLEP SRQRLPAPDE
KI
