ID   PYGM_BOVIN              Reviewed;         842 AA.
AC   P79334;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 145.
DE   RecName: Full=Glycogen phosphorylase, muscle form {ECO:0000305|PubMed:8845714};
DE            EC=2.4.1.1 {ECO:0000305|PubMed:8845714};
DE   AltName: Full=Myophosphorylase;
GN   Name=PYGM {ECO:0000250|UniProtKB:P11217};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT GSD-V TRP-490, DISEASE, FUNCTION, AND
RP   CATALYTIC ACTIVITY.
RC   TISSUE=Skeletal muscle;
RX   PubMed=8845714; DOI=10.1016/0960-8966(95)00014-3;
RA   Tsujino S., Shanske S., Valberg S.J., Cardinet G.H. III, Smith B.P.,
RA   DiMauro S.;
RT   "Cloning of bovine muscle glycogen phosphorylase cDNA and identification of
RT   a mutation in cattle with myophosphorylase deficiency, an animal model for
RT   McArdle's disease.";
RL   Neuromuscul. Disord. 6:19-26(1996).
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:0000305|PubMed:8845714}.
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:0000305|PubMed:8845714};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733;
CC         Evidence={ECO:0000305|PubMed:8845714};
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   -!- DISEASE: Note=Defects in PYGM are the cause of glycogen storage disease
CC       V (GSD-V); also known as McArdle disease. {ECO:0000269|PubMed:8845714}.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; S82859; AAB46846.1; -; mRNA.
DR   RefSeq; NP_786980.1; NM_175786.2.
DR   AlphaFoldDB; P79334; -.
DR   SMR; P79334; -.
DR   FunCoup; P79334; 850.
DR   STRING; 9913.ENSBTAP00000001373; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PaxDb; 9913-ENSBTAP00000001373; -.
DR   PeptideAtlas; P79334; -.
DR   GeneID; 327664; -.
DR   KEGG; bta:327664; -.
DR   CTD; 5837; -.
DR   eggNOG; KOG2099; Eukaryota.
DR   InParanoid; P79334; -.
DR   OrthoDB; 9215500at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0005980; P:glycogen catabolic process; ISS:UniProtKB.
DR   CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR   FunFam; 3.40.50.2000:FF:000005; Alpha-1,4 glucan phosphorylase; 1.
DR   FunFam; 3.40.50.2000:FF:000153; Alpha-1,4 glucan phosphorylase; 1.
DR   FunFam; 3.40.50.2000:FF:000197; Alpha-1,4 glucan phosphorylase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   NCBIfam; TIGR02093; P_ylase; 1.
DR   PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11468:SF32; GLYCOGEN PHOSPHORYLASE, MUSCLE FORM; 1.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; Carbohydrate metabolism; Disease variant;
KW   Glycogen metabolism; Glycogen storage disease; Glycosyltransferase;
KW   Nucleotide-binding; Phosphoprotein; Pyridoxal phosphate;
KW   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_0000188528"
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         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:0000250|UniProtKB:Q9WUB3"
FT   MOD_RES         473
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WUB3"
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"
FT   VARIANT         490
FT                   /note="R -> W (in GSD-V)"
FT                   /evidence="ECO:0000269|PubMed:8845714"
SQ   SEQUENCE   842 AA;  97293 MW;  DFCEF2D8ADBF878E CRC64;
     MSRPLTDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAYTV
     RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YIGRTLQNTM VNLALENACD EATYQLGLDM
     EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA
     DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN
     TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
     VAATLQDIIR RFKSSKFGCL DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDQERL
     EWEKAWEVTV KTCAYTNHTV LPEALERWPV HLIETLLPRH LQIIYEINQR FLNRVAAAFP
     GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF
     QNKTNGITPR RWLVMCNPGL AEIIAERIGE EYIADLDQLR KLLSYVDDES FIRDVAKVKQ
     ENKLKFSAYL EKEYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKKEPNKFFV
     PRTVMIGGKA APGYHMAKMI IKLITAIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA
     ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVE
     RLDQKGYNAQ EYYDRIPELR HVIDQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYEE
     YIKCQERVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP TRQRMPAPDE
     KI
//