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Glycogen phosphorylase, liver form (EC 2.4.1.1)

 PYGL_MOUSE              Reviewed;         850 AA.
Q9ET01; Q3UKJ0;
16-APR-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 4.
28-FEB-2018, entry version 151.
RecName: Full=Glycogen phosphorylase, liver form;
EC=2.4.1.1;
Name=Pygl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BTBR T+ tf/J; TISSUE=Liver;
McInerney M.M., Hurt C.B., Laipis P.J., Frost S.C.;
"Expression and regulation of glycogen phosphorylase in 3T3-L1
adipocytes.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
PROTEIN SEQUENCE OF 2-10; 162-170; 173-185; 279-290; 353-359; 388-395;
492-507 AND 643-650, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Liver;
Kanor S., Bienvenut W.V.;
Submitted (OCT-2005) to UniProtKB.
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524 AND SER-527, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-364, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Phosphorylase is an important allosteric enzyme in
carbohydrate metabolism. Enzymes from different sources differ in
their regulatory mechanisms and in their natural substrates.
However, all known phosphorylases share catalytic and structural
properties (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ((1->4)-alpha-D-glucosyl)(n) + phosphate =
((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activity of phosphorylase is controlled both by
allosteric means (through the noncovalent binding of metabolites)
and by covalent modification. Thus AMP allosterically activates,
whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit,
phosphorylase B (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
enzymatically active phosphorylase A. Interacts with PPP1R3B (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylation of Ser-15 converts phosphorylase B
(unphosphorylated) to phosphorylase A. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycogen phosphorylase family.
{ECO:0000305}.
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EMBL; AF288783; AAG00588.1; -; mRNA.
EMBL; AK140321; BAE24332.1; -; mRNA.
EMBL; AK145989; BAE26811.1; -; mRNA.
CCDS; CCDS25957.1; -.
RefSeq; NP_573461.2; NM_133198.2.
UniGene; Mm.256926; -.
UniGene; Mm.447796; -.
ProteinModelPortal; Q9ET01; -.
SMR; Q9ET01; -.
BioGrid; 225292; 1.
IntAct; Q9ET01; 5.
MINT; Q9ET01; -.
STRING; 10090.ENSMUSP00000071231; -.
BindingDB; Q9ET01; -.
ChEMBL; CHEMBL3008; -.
CAZy; GT35; Glycosyltransferase Family 35.
iPTMnet; Q9ET01; -.
PhosphoSitePlus; Q9ET01; -.
SwissPalm; Q9ET01; -.
EPD; Q9ET01; -.
MaxQB; Q9ET01; -.
PaxDb; Q9ET01; -.
PeptideAtlas; Q9ET01; -.
PRIDE; Q9ET01; -.
Ensembl; ENSMUST00000071250; ENSMUSP00000071231; ENSMUSG00000021069.
GeneID; 110095; -.
KEGG; mmu:110095; -.
UCSC; uc007ntm.2; mouse.
CTD; 5836; -.
MGI; MGI:97829; Pygl.
eggNOG; KOG2099; Eukaryota.
eggNOG; COG0058; LUCA.
GeneTree; ENSGT00390000016886; -.
HOGENOM; HOG000278444; -.
HOVERGEN; HBG006848; -.
InParanoid; Q9ET01; -.
KO; K00688; -.
OMA; ARDIWNM; -.
OrthoDB; EOG091G03RB; -.
TreeFam; TF300309; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
ChiTaRS; Pygl; mouse.
PRO; PR:Q9ET01; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000021069; -.
CleanEx; MM_PYGL; -.
ExpressionAtlas; Q9ET01; baseline and differential.
Genevisible; Q9ET01; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016208; F:AMP binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0032052; F:bile acid binding; ISO:MGI.
GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
GO; GO:0008144; F:drug binding; ISO:MGI.
GO; GO:0008184; F:glycogen phosphorylase activity; IDA:MGI.
GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0002060; F:purine nucleobase binding; ISO:MGI.
GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0019842; F:vitamin binding; ISO:MGI.
GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
GO; GO:0005977; P:glycogen metabolic process; IDA:MGI.
GO; GO:0070266; P:necroptotic process; IGI:MGI.
CDD; cd04300; GT1_Glycogen_Phosphorylase; 1.
InterPro; IPR011833; Glycg_phsphrylas.
InterPro; IPR000811; Glyco_trans_35.
InterPro; IPR035090; Pyridoxal_P_attach_site.
PANTHER; PTHR11468; PTHR11468; 1.
Pfam; PF00343; Phosphorylase; 1.
PIRSF; PIRSF000460; Pprylas_GlgP; 1.
TIGRFAMs; TIGR02093; P_ylase; 1.
PROSITE; PS00102; PHOSPHORYLASE; 1.
1: Evidence at protein level;
Acetylation; Allosteric enzyme; Carbohydrate metabolism;
Complete proteome; Direct protein sequencing; Glycogen metabolism;
Glycosyltransferase; Nucleotide-binding; Phosphoprotein;
Pyridoxal phosphate; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.3}.
CHAIN 2 850 Glycogen phosphorylase, liver form.
/FTId=PRO_0000188525.
BINDING 76 76 AMP. {ECO:0000250}.
SITE 109 109 Involved in the association of subunits.
{ECO:0000250}.
SITE 143 143 Involved in the association of subunits.
{ECO:0000250}.
SITE 156 156 May be involved in allosteric control.
{ECO:0000250}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.3}.
MOD_RES 15 15 Phosphoserine; by PHK; in form
phosphorylase A.
{ECO:0000250|UniProtKB:P06737}.
MOD_RES 364 364 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 561 561 Phosphoserine.
{ECO:0000250|UniProtKB:P09811}.
MOD_RES 639 639 Phosphoserine.
{ECO:0000250|UniProtKB:P06737}.
MOD_RES 681 681 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
CONFLICT 198 198 M -> V (in Ref. 1; AAG00588).
{ECO:0000305}.
SEQUENCE 850 AA; 97463 MW; C4BFF6A9AA4E181E CRC64;
MAKPLTDQEK RRQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR DYYFALAHTV
RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IREGWQVEEA
DDWLRHGNPW EKARPEFMLP VHFYGRVEHT QTGTKWVDTQ VVLALPYDTP VPGYMNNTVN
TMRLWSARAP NDFNLQDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDVIR RFKASKFGSK DGMGTVFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL
PWAKAWEITK KTFAYTNHTV LPEALERWPV ELVEKLLPRH LEIIYEINQK HLDRIVALFP
KDISRMRRMS LIEEEGGKRI NMAHLCIVGC HAVNGVAKIH SDIVKTQVFK DFSELEPDKF
QNKTNGITPR RWLLLCNPGL ADLIAEKIGE DYVKDLSQLT KLHSFVSDDI FLREIAKVKQ
ENKLKFSQFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVITMYNR IKKDPKKFFV
PRTVIIGGKA APGYHMAKMI IKLITSVAEV VNNDPMVGSK LKVIFLENYR VSLAEKVIPA
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVDDVA
ALDKKGYEAK EYYEALPELK LVIDQIDNGF FSPNQPDLFK DIINMLFYHD RFKVFADYEA
YVKCQEKVSQ LYMNQKAWNT MVLKNIAASG KFSSDRTIKE YAKDIWNMEP SDLKISLSNE
SSNGVSANGK


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