PYGB_MOUSE
ID PYGB_MOUSE Reviewed; 843 AA.
AC Q8CI94; Q8K283;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Glycogen phosphorylase, brain form;
DE EC=2.4.1.1;
GN Name=Pygb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197 AND TYR-473, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Glycogen phosphorylase that regulates glycogen mobilization.
CC Phosphorylase is an important allosteric enzyme in carbohydrate
CC metabolism. Enzymes from different sources differ in their regulatory
CC mechanisms and in their natural substrates. However, all known
CC phosphorylases share catalytic and structural properties.
CC {ECO:0000250|UniProtKB:P11216}.
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 Evidence={ECO:0000250};
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 (By similarity). {ECO:0000250|UniProtKB:P11216}.
CC -!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
CC enzymatically active phosphorylase A (By similarity).
CC {ECO:0000250|UniProtKB:P11216}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32209.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC032209; AAH32209.1; ALT_INIT; mRNA.
DR EMBL; BC035283; AAH35283.1; -; mRNA.
DR CCDS; CCDS16862.1; -.
DR RefSeq; NP_722476.1; NM_153781.1.
DR AlphaFoldDB; Q8CI94; -.
DR SMR; Q8CI94; -.
DR BioGRID; 225278; 17.
DR IntAct; Q8CI94; 7.
DR STRING; 10090.ENSMUSP00000035743; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; Q8CI94; -.
DR PhosphoSitePlus; Q8CI94; -.
DR SwissPalm; Q8CI94; -.
DR EPD; Q8CI94; -.
DR jPOST; Q8CI94; -.
DR MaxQB; Q8CI94; -.
DR PaxDb; Q8CI94; -.
DR PRIDE; Q8CI94; -.
DR ProteomicsDB; 301853; -.
DR Antibodypedia; 10014; 633 antibodies from 35 providers.
DR Ensembl; ENSMUST00000045441; ENSMUSP00000035743; ENSMUSG00000033059.
DR GeneID; 110078; -.
DR KEGG; mmu:110078; -.
DR UCSC; uc008mul.1; mouse.
DR CTD; 5834; -.
DR MGI; MGI:97828; Pygb.
DR VEuPathDB; HostDB:ENSMUSG00000033059; -.
DR eggNOG; KOG2099; Eukaryota.
DR GeneTree; ENSGT00950000183148; -.
DR HOGENOM; CLU_010198_1_1_1; -.
DR InParanoid; Q8CI94; -.
DR OMA; HCACSVA; -.
DR OrthoDB; 240595at2759; -.
DR PhylomeDB; Q8CI94; -.
DR TreeFam; TF300309; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 110078; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pygb; mouse.
DR PRO; PR:Q8CI94; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CI94; protein.
DR Bgee; ENSMUSG00000033059; Expressed in urinary bladder urothelium and 251 other tissues.
DR Genevisible; Q8CI94; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0097159; F:organic cyclic compound binding; ISO:MGI.
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:MGI.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:MGI.
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 Glycogen metabolism; Glycosyltransferase; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P11216"
FT CHAIN 2..843
FT /note="Glycogen phosphorylase, brain form"
FT /id="PRO_0000188536"
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; by PHK; in form phosphorylase A"
FT /evidence="ECO:0000250|UniProtKB:P53534"
FT MOD_RES 197
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 473
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P11216"
SQ SEQUENCE 843 AA; 96730 MW; AF9F499FBB5B8B0C CRC64;
MAKPLTDSER QKQISVRGIA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYFFALAHTV
RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQTACD EATYQLGLDL
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA
DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PDGVLWLDTQ VVLAMPYDTP VPGYKNNTVN
TMRLWSAKAP NDFKLKDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSRFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL MRILVDVEKV
DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LEIIYAINQR HLDHVAALFP
GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVKQSVFK DFYELEPEKF
QNKTNGITPR RWLLLCNPGL AEIIVERIGE GFLTDLSQLK KLLSLVDDEA FIRDVAKVKQ
ENKLKFSAQL EKEYKVKINP ASMFDVHVKR IHEYKRQLLN CLHIITLYNR IKKDPAKAFV
PRTVMIGGKA APGYHMAKMI IKLVTSIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA
ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVEDVE
ALDQKGYNAR EFYERLPELR QAVDQISSGF FSPKDPDCFK DVVNMLMYHD RFKVFADYEA
YIQCQAQVDR LYRNSKEWTK KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNL
PKD
