Reviewed, UniProtKB/Swiss-Prot P09811 (PYGL_RAT)

Names and origin

Protein names

Recommended name:
    Glycogen phosphorylase, liver form
    EC=2.4.1.1

Gene names

Name:	Pygl
Synonyms:	Lgp

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	850 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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	Pyridoxal phosphate.
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.
Subunit structure	Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A. Interacts with PPP1R3B. Ref.7 Ref.8 Ref.9
Post-translational modification	Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A.
Sequence similarities	Belongs to the glycogen phosphorylase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Ligand	Nucleotide-binding Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from mutant phenotype. Source: RGD glycogen catabolic process Inferred from direct assay. Source: RGD
Cellular component	cytoplasm Inferred from direct assay. Source: RGD soluble fraction Inferred from direct assay. Source: RGD
Molecular function	drug binding Inferred from direct assay. Source: RGD glycogen phosphorylase activity Inferred from direct assay. Source: RGD nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from direct assay. Source: RGD pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro sugar binding Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 850	849	Glycogen phosphorylase, liver form		PRO_0000188526
Sites
	Binding site	76	1	AMP By similarity
	Site	109	1	Involved in the association of subunits By similarity
	Site	143	1	Involved in the association of subunits By similarity
	Site	156	1	May be involved in allosteric control By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	15	1	Phosphoserine; by PHK; in form phosphorylase A By similarity
	Modified residue	75	1	Phosphotyrosine By similarity
	Modified residue	76	1	Phosphotyrosine By similarity
	Modified residue	681	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	667	1	I → V in CAA27704. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P09811-1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 0BE9A641DFFF3E0D	FASTA	850	97,483
	10 20 30 40 50 60 MAKPLTDQEK RRQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR DYYFALAHTV 70 80 90 100 110 120 RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDM 130 140 150 160 170 180 EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IREGWQVEEA 190 200 210 220 230 240 DDWLRHGNPW EKARPEFMLP VHFYGRVEHT QAGTKWVDTQ VVLALPYDTP VPGYMNNTVN 250 260 270 280 290 300 TMRLWSARAP NDFNLQDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 310 320 330 340 350 360 VAATLQDVIR RFKASKFGSK DGVGTVFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL 370 380 390 400 410 420 PWSKAWEITK KTFAYTNHTV LPEALERWPV DLVEKLLPRH LQIIYEINQK HLDRIVALFP 430 440 450 460 470 480 KDIDRMRRMS LIEEEGGKRI NMAHLCIVGC HAVNGVAKIH SDIVKTQVFK DFSELEPDKF 490 500 510 520 530 540 QNKTNGITPR RWLLLCNPGL ADLIAEKIGE DYVKDLSQLT KLHSFVGDDI FLREIAKVKQ 550 560 570 580 590 600 ENKLKFSQFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVITMYNR IKKDPKKFFV 610 620 630 640 650 660 PRTVIIGGKA APGYHMAKMI IKLVTSVAEV VNNDPMVGSK LKVIFLENYR VSLAEKVIPA 670 680 690 700 710 720 TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVDDVA 730 740 750 760 770 780 ALDKKGYEAK EYYEALPELK LVIDQIDNGF FSPNQPDLFK DIINMLFYHD RFKVFADYEA 790 800 810 820 830 840 YVKCQEKVSQ LYMNQKAWNT MVLRNIAASG KFSSDRTIRE YAKDIWNMEP SDLKISLSKE 850 SSNGVNANGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of rat liver glycogen phosphorylase cDNA." Schiebel K., Pekel E., Mayer D. Biochim. Biophys. Acta 1130:349-351(1992) [PubMed: 1339293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[3]	"Characterization of the 5' flanking region of the gene encoding rat liver glycogen phosphorylase." Herrick K.R., Gorin F.A., Park E.A., Tait R.C. Gene 126:203-211(1993) [PubMed: 8482535] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81. Strain: Sprague-Dawley. Tissue: Liver.
[4]	"Localization of the muscle, liver, and brain glycogen phosphorylase genes on linkage maps of mouse chromosomes 19, 12, and 2, respectively." Glaser T., Matthews K.E., Hudson J.W., Seth P., Houseman D.E., Crerar M.M. Genomics 5:510-521(1989) [PubMed: 2575583] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 333-430.
[5]	"Isolation of partial cDNAs for rat liver and muscle glycogen phosphorylase isozymes." Osawa S., Chiu R.H., McDonough A., Miller T.B. Jr., Johnson G.L. FEBS Lett. 202:282-288(1986) [PubMed: 2424788] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 441-850. Tissue: Liver.
[6]	"The gene encoding rat liver glycogen phosphorylase contains multiple polyadenylation signal sequences." Froman B.E., Tait R.C., Gorin F.A., Horwitz B.A., Stern J.S. Gene 109:269-274(1991) [PubMed: 1765272] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 835-850. Strain: Zucker.
[7]	"Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography." Moorhead G., MacKintosh C., Morrice N., Cohen P. FEBS Lett. 362:101-105(1995) [PubMed: 7720853] [Abstract] Cited for: INTERACTION WITH PPP1R3B.
[8]	"Amino acid sequence and expression of the hepatic glycogen-binding (GL)-subunit of protein phosphatase-1." Doherty M.J., Moorhead G., Morrice N., Cohen P., Cohen P.T.W. FEBS Lett. 375:294-298(1995) [PubMed: 7498521] [Abstract] Cited for: INTERACTION WITH PPP1R3B.
[9]	"Identification of the separate domains in the hepatic glycogen-targeting subunit of protein phosphatase 1 that interact with phosphorylase a, glycogen and protein phosphatase 1." Armstrong C.G., Doherty M.J., Cohen P.T.W. Biochem. J. 336:699-704(1998) [PubMed: 9841883] [Abstract] Cited for: INTERACTION WITH PPP1R3B.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X63515 mRNA. Translation: CAA45083.1. BC070901 mRNA. Translation: AAH70901.1. M85280 Genomic DNA. Translation: AAA41254.1. J03080 mRNA. Translation: AAA41986.1. X04069 mRNA. Translation: CAA27704.1. M59460 mRNA. Translation: AAA41987.1.
IPI	IPI00190179.
PIR	S22338.
RefSeq	NP_071604.1.
UniGene	Rn.21399
3D structure databases
HSSP	HSSP built from PDB template 1PYG based on UniProtKB P00489.
SMR	P09811. Positions 13-839.
ModBase	Search...
Protein-protein interaction databases
STRING	P09811.
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
Proteomic databases
PRIDE	P09811.
Genome annotation databases
Ensembl	ENSRNOT00000009183; ENSRNOP00000009183; ENSRNOG00000006388; Rattus norvegicus. [Genome view]
GeneID	64035.
KEGG	rno:64035.
NMPDR	fig|10116.3.peg.25219.
UCSC	NM_022268. rat.
Organism-specific databases
CTD	64035.
RGD	620687. Pygl.
Phylogenomic databases
HOVERGEN	P09811.
OMA	VIPATDL.
Enzyme and pathway databases
BRENDA	2.4.1.1. 248.
Gene expression databases
ArrayExpress	P09811.
Genevestigator	P09811.
GermOnline	ENSRNOG00000006388. Rattus norvegicus.
Family and domain databases
InterPro	IPR011833. Glycg_phsphrylas. IPR000811. Glyco_trans_35. [Graphical view]
PANTHER	PTHR11468. Glyco_trans_35. 1 hit.
Pfam	PF00343. Phosphorylase. 1 hit. [Graphical view]
PIRSF	PIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMs	TIGR02093. P_ylase. 1 hit.
PROSITE	PS00102. PHOSPHORYLASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	612666.

Entry information

Entry name

PYGL_RAT

Accession

Primary (citable) accession number: P09811

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 97 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)