PYGM_SHEEP
ID PYGM_SHEEP Reviewed; 842 AA.
AC O18751;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
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:0000250|UniProtKB:P11217};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Merino; TISSUE=Muscle;
RX PubMed=9267848; DOI=10.1016/s0960-8966(97)00062-x;
RA Tan P., Allen J.G., Wilton S.D., Akkari P.A., Huxtable C.R., Laing N.G.;
RT "A splice-site mutation causing ovine McArdle's disease.";
RL Neuromuscul. Disord. 7:336-342(1997).
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; AF001899; AAB68800.1; -; mRNA.
DR RefSeq; NP_001009192.1; NM_001009192.2.
DR AlphaFoldDB; O18751; -.
DR SMR; O18751; -.
DR STRING; 9940.ENSOARP00000009662; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR PRIDE; O18751; -.
DR Ensembl; ENSOART00000009802; ENSOARP00000009662; ENSOARG00000008997.
DR Ensembl; ENSOART00020017871; ENSOARP00020014763; ENSOARG00020011417.
DR GeneID; 442998; -.
DR KEGG; oas:442998; -.
DR CTD; 5837; -.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_1_1; -.
DR OMA; IYDINWR; -.
DR OrthoDB; 240595at2759; -.
DR Proteomes; UP000002356; Chromosome 21.
DR Bgee; ENSOARG00000008997; Expressed in longissimus thoracis muscle and 55 other tissues.
DR GO; GO:0008184; F:glycogen phosphorylase activity; ISS:UniProtKB.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Allosteric enzyme; Carbohydrate metabolism;
KW Glycogen metabolism; Glycosyltransferase; Phosphoprotein;
KW 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_0000188534"
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"
SQ SEQUENCE 842 AA; 97307 MW; E0EDEE3591DFA81C 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 AEVIAERIGE EYIADLDQLR KLLSYVDDES FIRDVAKVKQ
ENKLKFSAYL EKEYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKKEPNKFFV
PRTVMIGGKA APGYHMAKMI IRLITAIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVE
RLDQKGYNAQ EYYDRIPELR HIIDQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYEE
YVKCQERVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP TRQRMPAPDE
KI
