P53534 (PYGB_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycogen phosphorylase, brain form
EC=2.4.1.1

Gene names

Name:

Pygb

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	838 AA.
Sequence status	Fragment.
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.
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	Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	glycogen catabolic process Inferred from direct assay. Source: RGD
Cellular component	axon 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 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 – ›838	›837	Glycogen phosphorylase, brain form		PRO_0000188538
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
	Modified residue	76	1	Phosphotyrosine By similarity
	Modified residue	197	1	Phosphotyrosine By similarity
	Modified residue	473	1	Phosphotyrosine By similarity
	Modified residue	681	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	589	1	N → K in AAA40815. Ref.3
	Non-terminal residue	838	1

Sequences

	Sequence		Length	Mass (Da)
	P53534 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 281C4BBE1EE08240	FASTA	838	96,174
	10 20 30 40 50 60 MAKPLTDSER QKQISVRGIA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYFFALAHTV 70 80 90 100 110 120 RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQTACD EATYQLGLDL 130 140 150 160 170 180 EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA 190 200 210 220 230 240 DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PNGVLWLDTQ VVLAMPYDTP VPGYKNNTVN 250 260 270 280 290 300 TMRLWSAKAP NDFKLKDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 310 320 330 340 350 360 VAATLQDIIR RFKSSKFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL MRILVDVEKV 370 380 390 400 410 420 DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LEIIYAINQR HLDHVAALFP 430 440 450 460 470 480 GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVKQSVFK DFYELEPEKF 490 500 510 520 530 540 QNKTNGITPR RWLLLCNPGL AEIIVERIGE GFLTDLSQLK KLLSLVDDEA FIRDVAKVKQ 550 560 570 580 590 600 ENKLKFSAQL EKEYKVKINP CSMFDVHVKR IHEYKRQLLN CLHIITLYNR IKKDPTKTFV 610 620 630 640 650 660 PRTVMIGGKA APGYHMAKMI IKLVTSIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA 670 680 690 700 710 720 ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVEDVE 730 740 750 760 770 780 ALDQKGYNAQ EFYERLPELR QAVDQISSGF FSPKDPDCFK DVVNMLMYHD RFKVFADYEA 790 800 810 820 830 YIQCQAQVDH LYRNPKDWTK KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPP

References

[1]	"Comparative analysis of species-independent, isozyme-specific amino-acid substitutions in mammalian muscle, brain and liver glycogen phosphorylases." Hudson J.W., Hefferon K.L., Crerar M.M. Biochim. Biophys. Acta 1164:197-208(1993) [PubMed: 7916624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Lubec G., Afjehi-Sadat L. Submitted (DEC-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 50-60, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
[3]	"Studies on the expression and evolution of the glycogen phosphorylase gene family in the rat." Crerar M.M., Hudson J.W., Matthews K.E., David E.S., Golding G.B. Genome 30:582-590(1988) [PubMed: 3209063] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 570-729. Strain: Sprague-Dawley. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L10668 mRNA. Translation: AAA41252.1. M27726 mRNA. Translation: AAA40815.1.
IPI	IPI00948869.
PIR	S37300.
RefSeq	NP_037320.1. NM_013188.1.
UniGene	Rn.1518.
3D structure databases
ProteinModelPortal	P53534.
SMR	P53534. Positions 14-838.
ModBase	Search...
Protein-protein interaction databases
IntAct	P53534. 1 interaction.
STRING	P53534.
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
PTM databases
PhosphoSite	P53534.
2D gel databases
World-2DPAGE	0004:P53534.
Proteomic databases
PRIDE	P53534.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	25739.
KEGG	rno:25739.
Organism-specific databases
CTD	5834.
RGD	3460. Pygb.
Phylogenomic databases
eggNOG	roNOG12045.
GeneTree	ENSGT00390000016886.
HOVERGEN	HBG006848.
InParanoid	P53534.
PhylomeDB	P53534.
Gene expression databases
ArrayExpress	P53534.
Genevestigator	P53534.
GermOnline	ENSRNOG00000007583. Rattus norvegicus.
Family and domain databases
InterPro	IPR011833. Glycg_phsphrylas. IPR000811. Glyco_trans_35. [Graphical view]
KO	K00688.
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
NextBio	607887.

Entry information

Entry name

PYGB_RAT

Accession

Primary (citable) accession number: P53534

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program