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Glycogen phosphorylase, muscle form (EC 2.4.1.1) (Myophosphorylase)

 PYGM_RAT                Reviewed;         842 AA.
P09812;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
25-OCT-2017, entry version 137.
RecName: Full=Glycogen phosphorylase, muscle form;
EC=2.4.1.1;
AltName: Full=Myophosphorylase;
Name=Pygm;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7916624; DOI=10.1016/0167-4838(93)90248-P;
Hudson J.W., Hefferon K.L., Crerar M.M.;
"Comparative analysis of species-independent, isozyme-specific amino-
acid substitutions in mammalian muscle, brain and liver glycogen
phosphorylases.";
Biochim. Biophys. Acta 1164:197-208(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 566-762.
PubMed=2424788; DOI=10.1016/0014-5793(86)80702-5;
Osawa S., Chiu R.H., McDonough A., Miller T.B. Jr., Johnson G.L.;
"Isolation of partial cDNAs for rat liver and muscle glycogen
phosphorylase isozymes.";
FEBS Lett. 202:282-288(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 763-842.
PubMed=3840433; DOI=10.1111/j.1432-1033.1985.tb09193.x;
Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J.,
Crerar M.M.;
"Comparative sequence analysis of rat, rabbit, and human muscle
glycogen phosphorylase cDNAs.";
Eur. J. Biochem. 152:267-274(1985).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; TYR-204; TYR-227;
TYR-473; SER-514; SER-747 AND SER-748, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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.
-!- 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;
-!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
enzymatically active phosphorylase A.
-!- PTM: Phosphorylation of Ser-15 converts phosphorylase B
(unphosphorylated) to phosphorylase A.
-!- SIMILARITY: Belongs to the glycogen phosphorylase family.
{ECO:0000305}.
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EMBL; L10669; AAA41253.1; -; mRNA.
EMBL; X03032; CAA26835.1; -; mRNA.
PIR; S34624; S34624.
UniGene; Rn.11238; -.
ProteinModelPortal; P09812; -.
SMR; P09812; -.
IntAct; P09812; 1.
STRING; 10116.ENSRNOP00000028636; -.
CAZy; GT35; Glycosyltransferase Family 35.
iPTMnet; P09812; -.
PhosphoSitePlus; P09812; -.
PaxDb; P09812; -.
PRIDE; P09812; -.
UCSC; RGD:3461; rat.
RGD; 3461; Pygm.
eggNOG; KOG2099; Eukaryota.
eggNOG; COG0058; LUCA.
HOGENOM; HOG000278444; -.
HOVERGEN; HBG006848; -.
InParanoid; P09812; -.
PhylomeDB; P09812; -.
PRO; PR:P09812; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
GO; GO:0016208; F:AMP binding; IDA:RGD.
GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0008184; F:glycogen phosphorylase activity; IDA:RGD.
GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; IC:RGD.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:RGD.
GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:RGD.
GO; GO:0005980; P:glycogen catabolic process; IDA:RGD.
GO; GO:0005977; P:glycogen metabolic process; IDA:RGD.
GO; GO:0051591; P:response to cAMP; IDA:RGD.
GO; GO:0001666; P:response to hypoxia; IDA:RGD.
GO; GO:0010033; P:response to organic substance; IDA:RGD.
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; Glycogen metabolism; Glycosyltransferase;
Nucleotide-binding; Phosphoprotein; Pyridoxal phosphate;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P00489}.
CHAIN 2 842 Glycogen phosphorylase, muscle form.
/FTId=PRO_0000188533.
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-acetylserine.
{ECO:0000250|UniProtKB:P00489}.
MOD_RES 15 15 Phosphoserine; by PHK; in form
phosphorylase A.
{ECO:0000250|UniProtKB:P11217}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 204 204 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 227 227 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 364 364 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9ET01}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WUB3}.
MOD_RES 473 473 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 514 514 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ET01}.
MOD_RES 681 681 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
MOD_RES 747 747 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 748 748 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CONFLICT 640 641 RF -> L (in Ref. 2). {ECO:0000305}.
CONFLICT 724 724 Q -> N (in Ref. 2). {ECO:0000305}.
CONFLICT 766 766 V -> L (in Ref. 3; CAA26835).
{ECO:0000305}.
SEQUENCE 842 AA; 97273 MW; EA30BBB63FE69700 CRC64;
MSRPLSDQDK RKQISVRGLA GVENVSDLKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV
RDHLVDRWIR TQQHYYAKDP KRIYYLSLEL YMGRTLQNTM VNLALENACD EATYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ICGGWQMEEA
DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN
TMRLWSAKAP PYFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDKFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL IRILVDLERL
DWDKAWDVTV KTCAYTNHTV LPEALERWPV HLMETLLPRH LQIIYEINQR FLNRVAAAFP
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF
QNKTNGITPR RWLVLCNPGL AEVIAERIGE EYISDLDQLR KLLSYLDDQA FIRDVAKVKQ
ENKLKFSAYL ETEYKVHINP NSLFDVQVKR IHEYKRQLLN CLHIITLYNR IKREPNRFMV
PRTIMIGGKA APGYHMAKMI IKLITAIGDV VNHDPAVGDR FRVIFLENYR VSLAEKVIPA
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEDNFF IFGMRVEDVE
RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF FSPKQPDLFK DIVNMVMHHD RFKVFADYEE
YIKCQDKVSE LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGLEP SRQRLPAPDE
KI


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