PYG_DROME
ID PYG_DROME Reviewed; 844 AA.
AC Q9XTL9; Q9V467;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Glycogen phosphorylase;
DE EC=2.4.1.1;
GN Name=GlyP; Synonyms=Glp1; ORFNames=CG7254;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S;
RX PubMed=10092506; DOI=10.1006/bbrc.1999.0396;
RA Tick G., Cserpan I., Dombradi V., Mechler B.M., Toeroek I., Kiss I.;
RT "Structural and functional characterization of the Drosophila glycogen
RT phosphorylase gene.";
RL Biochem. Biophys. Res. Commun. 257:34-43(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [5]
RP FUNCTION.
RX PubMed=24265594; DOI=10.1371/journal.pbio.1001708;
RA Zirin J., Nieuwenhuis J., Perrimon N.;
RT "Role of autophagy in glycogen breakdown and its relevance to chloroquine
RT myopathy.";
RL PLoS Biol. 11:E1001708-E1001708(2013).
CC -!- FUNCTION: 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 (By
CC similarity). Required for glycogen breakdown in skeletal muscle.
CC {ECO:0000250, ECO:0000269|PubMed:24265594}.
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 -!- PTM: Phosphorylation of Ser-15 converts phosphorylase B
CC (unphosphorylated) to phosphorylase A. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; AF073177; AAD41649.1; -; Genomic_DNA.
DR EMBL; AF073178; AAD27759.1; -; mRNA.
DR EMBL; AF073179; AAD27760.1; -; mRNA.
DR EMBL; AE014134; AAF51303.1; -; Genomic_DNA.
DR EMBL; AF160947; AAD46887.1; -; mRNA.
DR RefSeq; NP_001027219.1; NM_001032048.2.
DR RefSeq; NP_722762.1; NM_164453.4.
DR AlphaFoldDB; Q9XTL9; -.
DR SMR; Q9XTL9; -.
DR BioGRID; 59616; 26.
DR DIP; DIP-22585N; -.
DR IntAct; Q9XTL9; 16.
DR STRING; 7227.FBpp0077501; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; Q9XTL9; -.
DR PaxDb; Q9XTL9; -.
DR PRIDE; Q9XTL9; -.
DR DNASU; 33386; -.
DR EnsemblMetazoa; FBtr0077828; FBpp0077501; FBgn0004507.
DR EnsemblMetazoa; FBtr0100485; FBpp0099923; FBgn0004507.
DR GeneID; 33386; -.
DR KEGG; dme:Dmel_CG7254; -.
DR CTD; 33386; -.
DR FlyBase; FBgn0004507; GlyP.
DR VEuPathDB; VectorBase:FBgn0004507; -.
DR eggNOG; KOG2099; Eukaryota.
DR GeneTree; ENSGT00950000183148; -.
DR HOGENOM; CLU_010198_1_1_1; -.
DR InParanoid; Q9XTL9; -.
DR OMA; KHKRTFT; -.
DR OrthoDB; 240595at2759; -.
DR PhylomeDB; Q9XTL9; -.
DR BioCyc; MetaCyc:MON-17099; -.
DR Reactome; R-DME-70221; Glycogen breakdown (glycogenolysis).
DR SignaLink; Q9XTL9; -.
DR BioGRID-ORCS; 33386; 0 hits in 3 CRISPR screens.
DR ChiTaRS; GlyP; fly.
DR GenomeRNAi; 33386; -.
DR PRO; PR:Q9XTL9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004507; Expressed in capitellum (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q9XTL9; baseline and differential.
DR Genevisible; Q9XTL9; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IDA:FlyBase.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:FlyBase.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:FlyBase.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0005980; P:glycogen catabolic process; IMP:FlyBase.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0045824; P:negative regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0045819; P:positive regulation of glycogen catabolic process; IMP:FlyBase.
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 Carbohydrate metabolism; Glycogen metabolism; Glycosyltransferase;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..844
FT /note="Glycogen phosphorylase"
FT /id="PRO_0000188540"
FT BINDING 76
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Phosphoserine; by PHK; in form phosphorylase A"
FT /evidence="ECO:0000250"
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VARIANT 642
FT /note="K -> N (in strain: Canton-S)"
SQ SEQUENCE 844 AA; 96997 MW; 0A65C5B9DCA060ED CRC64;
MSKPQSDADR RKQISVRGIA EVGNVTEVKK NFNRHLHYTL VKDRNVSTLR DYYFALANTV
KDNMVGRWIR TQQHYYEKDP KRVYYLSLEY YMGRSLTNTM INLGIQSECE EAMYQLGLDI
ENLEEMEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFAQK IKNGEQVEEP
DDWLRYGNPW EKARPEFMLP VNFYGRVIDT PEGKKWVDTQ RVFAMPYDNP IPGYNNNHVN
TLRLWSAKSP IDFNLKFFND GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFM
CAATLQDIIR RYKASKFGSR EAVRNTFDHF PDKVAIQLND THPSLAIPEL MRILVDEEHL
TWEKAWDITV RSCAYTNHTV LPEALERWPV SLLESILPRH LQIIYHINFL HMENVKKKFP
DDLDRMRRMS MVEEDGEKRI NMAHLSIVGS HAVNGVAAIH SQILKDSLFH DFYEMEPQKF
QNKTNGITPR RWLLLCNPGL SDLIAEKIGD EWPVHLDQLV ALKKWAKDPN FQRNVARVKQ
ENKLKLAAIL EKDYGVKINP SSMFDIQVKR IHEYKRQLLN CLHIITLYNR IKKDPTANFT
PRTIMIGGKA APGYYVAKQI IKLICAVGNV VNNDPIVGDK LKVIFLENYR VTLAEKIMPA
ADLSEQISTA GTEASGTGNM KFQLNGALTI GTLDGANVEM AEEMGLDNIF IFGMTVDEVE
ALKKKGYNAY DYYNANPEVK QVIDQIQGGF FSPGNPNEFK NIADILLKYD HYYLLADYDA
YIKAQDLVSK TYQNQAKWLE MSINNIASSG KFSSDRTIAE YAREIWGVEP TWEKLPAPED
QPQN
