PYGL_SHEEP
ID PYGL_SHEEP Reviewed; 851 AA.
AC Q5MIB5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Glycogen phosphorylase, liver form {ECO:0000250|UniProtKB:P06737};
DE EC=2.4.1.1 {ECO:0000250|UniProtKB:P06737};
GN Name=PYGL {ECO:0000250|UniProtKB:P06737};
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 TISSUE=Liver;
RA Walker K.R., Blechynden L.M., Binz N., Laing N.G.;
RT "Characterization of ovine brain and liver glycogen phosphorylases.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Interacts with PPP1R3B;
CC recruits the phosphatase PP1 which dephosphorylates and inactivates
CC PYGL/glycogen phosphorylase. {ECO:0000250|UniProtKB:P06737}.
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; AY827551; AAV87309.1; -; mRNA.
DR RefSeq; NP_001020032.1; NM_001024861.1.
DR AlphaFoldDB; Q5MIB5; -.
DR SMR; Q5MIB5; -.
DR STRING; 9940.ENSOARP00000022235; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR PRIDE; Q5MIB5; -.
DR GeneID; 554320; -.
DR KEGG; oas:554320; -.
DR CTD; 5836; -.
DR eggNOG; KOG2099; Eukaryota.
DR OrthoDB; 240595at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
PE 2: Evidence at transcript 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..851
FT /note="Glycogen phosphorylase, liver form"
FT /id="PRO_0000188527"
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:0000250|UniProtKB:P09811"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06737"
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"
SQ SEQUENCE 851 AA; 97468 MW; 636386ADAA307A5C CRC64;
MAKPLTDQEK RRQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR DYFFALAHTV
RDHLVGRWIR TQQYYYEKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IRDGWQIEEA
DDWLRHGNPW EKARPEFMLP VHFYGRVEHT EAGTKWIDTQ VVLALPYDTP VPGYLNNTVN
TMRLWSARAP NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDVIR RFKASKFDSS NSAETAFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL
PWSKAWEITQ KTFAYTNHTV LPEALERWPV ELVENLLPRH LQIIYEINQK HLDKIAALFP
KDVDRLRRMS LIEEEGVKRI NMAHLCIVGS HAVNGVAKIH SDIVKTQVFK DFSELEPDKF
QNKTNGITPR RWLLLCNPGL AELIAEKIGE DYVKDLSQLT KLNSFLGDDI FLREISNVKQ
ENKLKFSQFL EKEYKVKINP SSMFDVQVKR IHEYKRQLLN CLHVVTMYNR IKKDPKKLFV
PRTVIIGGKA APGYYMAKLI IKLITSVAEV VNNDPMVGSK LKLIFLENYR VSLAEKVIPA
TDLSEQISTA GTEASGTGNM KFMQNGALTI GTMDGANVEM AEEAGEENLF IFGMRVEDVA
ALDKKGYEAK EYYEALPELK LAIDQIDKGF FSPKQPDLFK DLVNMLFYHD RFKVFADYEA
YVKCQEKVSQ LYMNPKAWNI MVLKNIAASG KFSSDRTIKE YARDIWNMEP SDIKISLSGE
PSGGANKANG K
