PYGB_RAT
ID PYGB_RAT Reviewed; 838 AA.
AC P53534;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Glycogen phosphorylase, brain form;
DE EC=2.4.1.1;
DE Flags: Fragment;
GN Name=Pygb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7916624; DOI=10.1016/0167-4838(93)90248-p;
RA Hudson J.W., Hefferon K.L., Crerar M.M.;
RT "Comparative analysis of species-independent, isozyme-specific amino-acid
RT substitutions in mammalian muscle, brain and liver glycogen
RT phosphorylases.";
RL Biochim. Biophys. Acta 1164:197-208(1993).
RN [2]
RP PROTEIN SEQUENCE OF 50-60, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (DEC-2006) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 570-729.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=3209063; DOI=10.1139/g88-098;
RA Crerar M.M., Hudson J.W., Matthews K.E., David E.S., Golding G.B.;
RT "Studies on the expression and evolution of the glycogen phosphorylase gene
RT family in the rat.";
RL Genome 30:582-590(1988).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-524, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Glycogen phosphorylase that regulates glycogen mobilization
CC (By similarity). Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism. Enzymes from different sources differ in their
CC regulatory mechanisms and in their natural substrates. However, all
CC known phosphorylases share catalytic and structural properties.
CC {ECO:0000250|UniProtKB:P11216, ECO:0000305|PubMed:7916624}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: Activity of phosphorylase is controlled both by
CC allosteric means (through the non-covalent binding of metabolites) and
CC by covalent modification. Thus AMP allosterically activates, whereas
CC ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase
CC B.
CC -!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
CC enzymatically active phosphorylase A.
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; L10668; AAA41252.1; -; mRNA.
DR EMBL; M27726; AAA40815.1; -; mRNA.
DR PIR; S37300; S37300.
DR RefSeq; NP_037320.1; NM_013188.1.
DR AlphaFoldDB; P53534; -.
DR SMR; P53534; -.
DR BioGRID; 247767; 8.
DR IntAct; P53534; 4.
DR MINT; P53534; -.
DR STRING; 10116.ENSRNOP00000010158; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; P53534; -.
DR World-2DPAGE; 0004:P53534; -.
DR jPOST; P53534; -.
DR PaxDb; P53534; -.
DR PeptideAtlas; P53534; -.
DR PRIDE; P53534; -.
DR GeneID; 25739; -.
DR KEGG; rno:25739; -.
DR UCSC; RGD:3460; rat.
DR CTD; 5834; -.
DR RGD; 3460; Pygb.
DR eggNOG; KOG2099; Eukaryota.
DR InParanoid; P53534; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0097159; F:organic cyclic compound binding; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0005977; P:glycogen metabolic process; IDA:RGD.
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 Direct protein sequencing; Glycogen metabolism; Glycosyltransferase;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P11216"
FT CHAIN 2..>838
FT /note="Glycogen phosphorylase, brain form"
FT /id="PRO_0000188538"
FT REGION 677..678
FT /note="Pyridoxal 5'-phosphate"
FT /evidence="ECO:0000250|UniProtKB:P11216"
FT BINDING 43
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P11216"
FT BINDING 197
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P11216"
FT BINDING 310
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P11216"
FT BINDING 569
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P11216"
FT SITE 76
FT /note="Participates in a stacking interaction with the
FT adenine ring of AMP"
FT /evidence="ECO:0000250|UniProtKB:P11216"
FT SITE 109
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250"
FT SITE 143
FT /note="Involved in the association of subunits"
FT /evidence="ECO:0000250"
FT SITE 156
FT /note="May be involved in allosteric control"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P11216"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 197
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI94"
FT MOD_RES 473
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI94"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11216"
FT CONFLICT 589
FT /note="N -> K (in Ref. 3; AAA40815)"
FT /evidence="ECO:0000305"
FT NON_TER 838
SQ SEQUENCE 838 AA; 96174 MW; 281C4BBE1EE08240 CRC64;
MAKPLTDSER QKQISVRGIA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYFFALAHTV
RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQTACD EATYQLGLDL
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA
DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PNGVLWLDTQ VVLAMPYDTP VPGYKNNTVN
TMRLWSAKAP NDFKLKDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL MRILVDVEKV
DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LEIIYAINQR HLDHVAALFP
GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVKQSVFK DFYELEPEKF
QNKTNGITPR RWLLLCNPGL AEIIVERIGE GFLTDLSQLK KLLSLVDDEA FIRDVAKVKQ
ENKLKFSAQL EKEYKVKINP CSMFDVHVKR IHEYKRQLLN CLHIITLYNR IKKDPTKTFV
PRTVMIGGKA APGYHMAKMI IKLVTSIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA
ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVEDVE
ALDQKGYNAQ EFYERLPELR QAVDQISSGF FSPKDPDCFK DVVNMLMYHD RFKVFADYEA
YIQCQAQVDH LYRNPKDWTK KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPP
