PYGM_MOUSE
ID PYGM_MOUSE Reviewed; 842 AA.
AC Q9WUB3;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Glycogen phosphorylase, muscle form {ECO:0000250|UniProtKB:P11217};
DE EC=2.4.1.1 {ECO:0000250|UniProtKB:P11217};
DE AltName: Full=Myophosphorylase;
GN Name=Pygm {ECO:0000312|MGI:MGI:97830};
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=BALB/cJ; TISSUE=Skeletal muscle;
RX PubMed=10318868; DOI=10.1074/jbc.274.20.14429;
RA Murdock D.G., Boone B.E., Esposito L.A., Wallace D.C.;
RT "Up-regulation of nuclear and mitochondrial genes in the skeletal muscle of
RT mice lacking the heart/muscle isoform of the adenine nucleotide
RT translocator.";
RL J. Biol. Chem. 274:14429-14433(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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: 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; AF124787; AAD30476.1; -; mRNA.
DR EMBL; BC012961; AAH12961.1; -; mRNA.
DR CCDS; CCDS29504.1; -.
DR RefSeq; NP_035354.1; NM_011224.2.
DR AlphaFoldDB; Q9WUB3; -.
DR SMR; Q9WUB3; -.
DR BioGRID; 202528; 21.
DR IntAct; Q9WUB3; 6.
DR STRING; 10090.ENSMUSP00000047564; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; Q9WUB3; -.
DR PhosphoSitePlus; Q9WUB3; -.
DR SwissPalm; Q9WUB3; -.
DR EPD; Q9WUB3; -.
DR jPOST; Q9WUB3; -.
DR MaxQB; Q9WUB3; -.
DR PaxDb; Q9WUB3; -.
DR PeptideAtlas; Q9WUB3; -.
DR PRIDE; Q9WUB3; -.
DR ProteomicsDB; 300365; -.
DR Antibodypedia; 29416; 325 antibodies from 30 providers.
DR Ensembl; ENSMUST00000035269; ENSMUSP00000047564; ENSMUSG00000032648.
DR GeneID; 19309; -.
DR KEGG; mmu:19309; -.
DR UCSC; uc008gio.1; mouse.
DR CTD; 5837; -.
DR MGI; MGI:97830; Pygm.
DR VEuPathDB; HostDB:ENSMUSG00000032648; -.
DR eggNOG; KOG2099; Eukaryota.
DR GeneTree; ENSGT00950000183148; -.
DR HOGENOM; CLU_010198_1_1_1; -.
DR InParanoid; Q9WUB3; -.
DR OMA; IYDINWR; -.
DR OrthoDB; 240595at2759; -.
DR PhylomeDB; Q9WUB3; -.
DR TreeFam; TF300309; -.
DR BRENDA; 2.4.1.1; 3474.
DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR BioGRID-ORCS; 19309; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Pygm; mouse.
DR PRO; PR:Q9WUB3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9WUB3; protein.
DR Bgee; ENSMUSG00000032648; Expressed in hindlimb stylopod muscle and 126 other tissues.
DR ExpressionAtlas; Q9WUB3; baseline and differential.
DR Genevisible; Q9WUB3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0016208; F:AMP binding; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:MGI.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0097159; F:organic cyclic compound binding; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0005980; P:glycogen catabolic process; IDA:MGI.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:MGI.
DR GO; GO:0051591; P:response to cAMP; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0010033; P:response to organic substance; ISO: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;
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_0000188531"
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:P11217"
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 204
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 473
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
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:0000250|UniProtKB:P09812"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09812"
SQ SEQUENCE 842 AA; 97286 MW; B55CC8EFF517DCD9 CRC64;
MSRPLSDQDK RKQISVRGLA GVENVSELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV
RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ICGGWQMEEA
DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN
TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGSR DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDLERL
DWDKAWDVTV KTCAYTNHTV LPEALERWPV HLMETLLPRH LQIIYEINQR FLNRVAAAFP
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF
QNKTNGITPR RWLVLCNPGL AEVIAERIGE DYISDLDQLR KLLSYVDDEA FIRDVAKVKQ
ENKLKFSAYL EREYKVHINP NSLFDVQVKR IHEYKRQLLN CLHIITLYNR IKREPNRFMV
PRTIMIGGKA APGYHMAKMI IKLITAIGDV VNHDPAVGDR LRVIFLENYR VSLAEKVIPA
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVE
RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYEE
YIKCQDKVSE LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE
KI
