PYGL_BOVIN
ID PYGL_BOVIN Reviewed; 851 AA.
AC Q0VCM4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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; BC120097; AAI20098.1; -; mRNA.
DR RefSeq; NP_001068671.1; NM_001075203.2.
DR RefSeq; XP_005211715.1; XM_005211658.2.
DR AlphaFoldDB; Q0VCM4; -.
DR SMR; Q0VCM4; -.
DR STRING; 9913.ENSBTAP00000015277; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR PaxDb; Q0VCM4; -.
DR PeptideAtlas; Q0VCM4; -.
DR PRIDE; Q0VCM4; -.
DR Ensembl; ENSBTAT00000015277; ENSBTAP00000015277; ENSBTAG00000011494.
DR GeneID; 505472; -.
DR KEGG; bta:505472; -.
DR CTD; 5836; -.
DR VEuPathDB; HostDB:ENSBTAG00000011494; -.
DR VGNC; VGNC:33588; PYGL.
DR eggNOG; KOG2099; Eukaryota.
DR GeneTree; ENSGT00950000183148; -.
DR HOGENOM; CLU_010198_1_1_1; -.
DR InParanoid; Q0VCM4; -.
DR OMA; KHKRTFT; -.
DR OrthoDB; 240595at2759; -.
DR TreeFam; TF300309; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000011494; Expressed in parenchyma of mammary gland and 103 other tissues.
DR ExpressionAtlas; Q0VCM4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
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; 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_0000272607"
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; 97456 MW; A81FBC5224A71350 CRC64;
MAKPLTDQEK RRQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR DYFFALAHTV
RDHLVGRWIR TQQYYYEKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IRDGWQIEEA
DDWLRHGNPW EKARPEFMLP VHFYGRVEHT EAGTKWTDTQ VVLALPYDTP VPGYLNNTVN
TMRLWSARAP NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDVIR RFKASKFDSS NSTKTAFDAF PDQVAIQLND THPSLAIPEL MRIFVDIEKL
PWSKAWEITQ KTFAYTNHTV LPEALERWPV ELVEKLLPRH LQIIYEINQK HLDKIAALFP
KDVDRLRRMS LIEEEGGKRI NMAHLCIVGS HAVNGVAKIH SDIVKTQVFK DFSELEPDKF
QNKTNGITPR RWLLLCNPGL AELIAEKIGE DYVKDLSQLT KLNSFLGDDI FLREISNVKQ
ENKLKFSQFL EKEYKVKINP SSMFDVQVKR IHEYKRQLLN CLHVVTMYNR IKKDPKKLFV
PRTVIIGGKA APGYYMAKLI IKLITSVAEV VNNDPVVGSK LKLIFLENYR VSLAEKVIPA
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRIEDVA
ALDKKGYEAK EYYEALPELK LAIDQIDKGF FSPKQPDLFK DLVNMLFYHD RFKVFADYEA
YVKCQEKVSQ LYMNPKAWNI MVLKNIAASG KFSSDRTIKE YARDIWNMEP SDIKISLSSD
PSGGANKANG K
