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Glycogen phosphorylase, brain form (EC 2.4.1.1) (Fragment)

 PYGB_RAT                Reviewed;         838 AA.
P53534;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 134.
RecName: Full=Glycogen phosphorylase, brain form;
EC=2.4.1.1;
Flags: Fragment;
Name=Pygb;
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]
PROTEIN SEQUENCE OF 50-60, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (DEC-2006) to UniProtKB.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 570-729.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=3209063;
Crerar M.M., Hudson J.W., Matthews K.E., David E.S., Golding G.B.;
"Studies on the expression and evolution of the glycogen phosphorylase
gene family in the rat.";
Genome 30:582-590(1988).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-524, 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: Glycogen phosphorylase that regulates glycogen
mobilization (By similarity). 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.
{ECO:0000250|UniProtKB:P11216, ECO:0000305|PubMed:7916624}.
-!- CATALYTIC ACTIVITY:
Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-
D-glucosyl](n-1) + alpha-D-glucose 1-phosphate;
Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586,
ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601;
EC=2.4.1.1;
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- ACTIVITY REGULATION: Activity of phosphorylase is controlled both
by allosteric means (through the non-covalent binding of
metabolites) and by covalent modification. Thus AMP allosterically
activates, whereas ATP, ADP, and glucose-6-phosphate
allosterically inhibit, phosphorylase B.
-!- 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.
{ECO:0000250|UniProtKB:P11217}.
-!- SIMILARITY: Belongs to the glycogen phosphorylase family.
{ECO:0000305}.
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EMBL; L10668; AAA41252.1; -; mRNA.
EMBL; M27726; AAA40815.1; -; mRNA.
PIR; S37300; S37300.
RefSeq; NP_037320.1; NM_013188.1.
UniGene; Rn.1518; -.
ProteinModelPortal; P53534; -.
SMR; P53534; -.
BioGrid; 247767; 5.
IntAct; P53534; 2.
STRING; 10116.ENSRNOP00000010158; -.
CAZy; GT35; Glycosyltransferase Family 35.
iPTMnet; P53534; -.
World-2DPAGE; 0004:P53534; -.
PaxDb; P53534; -.
PeptideAtlas; P53534; -.
PRIDE; P53534; -.
GeneID; 25739; -.
KEGG; rno:25739; -.
UCSC; RGD:3460; rat.
CTD; 5834; -.
RGD; 3460; Pygb.
eggNOG; KOG2099; Eukaryota.
eggNOG; COG0058; LUCA.
HOGENOM; HOG000278444; -.
HOVERGEN; HBG006848; -.
InParanoid; P53534; -.
KO; K00688; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IDA:RGD.
GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0005980; P:glycogen catabolic process; IDA:RGD.
GO; GO:0005977; P:glycogen metabolic process; 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; Direct protein sequencing; Glycogen metabolism;
Glycosyltransferase; Phosphoprotein; Pyridoxal phosphate;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P11216}.
CHAIN 2 >838 Glycogen phosphorylase, brain form.
/FTId=PRO_0000188538.
REGION 677 678 Pyridoxal 5'-phosphate.
{ECO:0000250|UniProtKB:P11216}.
BINDING 43 43 AMP; shared with dimeric partner.
{ECO:0000250|UniProtKB:P11216}.
BINDING 197 197 AMP. {ECO:0000250|UniProtKB:P11216}.
BINDING 310 310 AMP. {ECO:0000250|UniProtKB:P11216}.
BINDING 569 569 Pyridoxal 5'-phosphate.
{ECO:0000250|UniProtKB:P11216}.
SITE 76 76 Participates in a stacking interaction
with the adenine ring of AMP.
{ECO:0000250|UniProtKB:P11216}.
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:0000250|UniProtKB:P11216}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 197 197 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8CI94}.
MOD_RES 473 473 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8CI94}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 681 681 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:P11216}.
CONFLICT 589 589 N -> K (in Ref. 3; AAA40815).
{ECO:0000305}.
NON_TER 838 838
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


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Catalog number Product name Quantity
LF-PA40977 anti-Glycogen Phosphorylase, Brain Form, Rabbit polyclonal to Glycogen Phosphorylase, Brain Form, Isotype IgG, Host Rabbit 50 ug
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GTX22075 Glycogen phosphorylase brain form 250 µg
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4GP31-6G5 Glycogen phosphorylase brain form 1 mg
4GP31-7B9 Glycogen phosphorylase brain form 1 mg
4GP31-8G7 Glycogen phosphorylase brain form 1 mg
AP06887PU-N Glycogen phosphorylase brain form 50 µg
AP06856PU-N Glycogen phosphorylase brain form 50 µg
8G67XC Glycogen phosphorylase brain form 1 mg
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NB120-885 Glycogen phosphorylase brain form 0.2 mg
GTX114952 Glycogen phosphorylase brain form 0.1 ml


 

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