Reviewed, UniProtKB/Swiss-Prot P09812 (PYGM_RAT)

Names and origin

Protein names

Recommended name:
    Glycogen phosphorylase, muscle form
    EC=2.4.1.1
Alternative name(s):
    Myophosphorylase

Gene names

Name:

Pygm

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	842 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
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	Nucleotide-binding Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	cellular calcium ion homeostasis Inferred from direct assay. Source: RGD glycogen catabolic process Inferred from direct assay. Source: RGD response to cAMP Inferred from direct assay. Source: RGD response to hypoxia Inferred from direct assay. Source: RGD
Cellular component	sarcoplasmic reticulum Inferred from direct assay. Source: RGD soluble fraction Inferred from direct assay. Source: RGD
Molecular function	AMP binding Inferred from direct assay. Source: RGD drug binding Inferred from direct assay. Source: RGD glycogen phosphorylase activity Inferred from direct assay. Source: RGD protein homodimerization activity Inferred by curator. Source: RGD pyridoxal phosphate binding Inferred from direct assay. Source: RGD 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 – 842	841	Glycogen phosphorylase, muscle form		PRO_0000188533
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-acetylserine By similarity
	Modified residue	15	1	Phosphoserine; by PHK; in form phosphorylase A By similarity
	Modified residue	316	1	N6-acetyllysine By similarity
	Modified residue	473	1	Phosphotyrosine By similarity
	Modified residue	681	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	640 – 641	2	RF → L Ref.2
	Sequence conflict	724	1	Q → N Ref.2
	Sequence conflict	766	1	V → L in CAA26835. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P09812-1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: EA30BBB63FE69700	FASTA	842	97,273
	10 20 30 40 50 60 MSRPLSDQDK RKQISVRGLA GVENVSDLKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV 70 80 90 100 110 120 RDHLVDRWIR TQQHYYAKDP KRIYYLSLEL YMGRTLQNTM VNLALENACD EATYQLGLDM 130 140 150 160 170 180 EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ICGGWQMEEA 190 200 210 220 230 240 DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN 250 260 270 280 290 300 TMRLWSAKAP PYFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDKFFEGK ELRLKQEYFV 310 320 330 340 350 360 VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL IRILVDLERL 370 380 390 400 410 420 DWDKAWDVTV KTCAYTNHTV LPEALERWPV HLMETLLPRH LQIIYEINQR FLNRVAAAFP 430 440 450 460 470 480 GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF 490 500 510 520 530 540 QNKTNGITPR RWLVLCNPGL AEVIAERIGE EYISDLDQLR KLLSYLDDQA FIRDVAKVKQ 550 560 570 580 590 600 ENKLKFSAYL ETEYKVHINP NSLFDVQVKR IHEYKRQLLN CLHIITLYNR IKREPNRFMV 610 620 630 640 650 660 PRTIMIGGKA APGYHMAKMI IKLITAIGDV VNHDPAVGDR FRVIFLENYR VSLAEKVIPA 670 680 690 700 710 720 ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEDNFF IFGMRVEDVE 730 740 750 760 770 780 RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF FSPKQPDLFK DIVNMVMHHD RFKVFADYEE 790 800 810 820 830 840 YIKCQDKVSE LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGLEP SRQRLPAPDE KI

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]	"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 [MRNA] OF 566-762.
[3]	"Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs." Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J., Crerar M.M. Eur. J. Biochem. 152:267-274(1985) [PubMed: 3840433] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 763-842.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L10669 mRNA. Translation: AAA41253.1. X03032 mRNA. Translation: CAA26835.1.
IPI	IPI00190181.
PIR	S34624.
UniGene	Rn.11238
3D structure databases
HSSP	HSSP built from PDB template 1PYG based on UniProtKB P00489.
SMR	P09812. Positions 13-836.
ModBase	Search...
Protein-protein interaction databases
STRING	P09812.
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
PTM databases
PhosphoSite	P09812.
Proteomic databases
PRIDE	P09812.
Genome annotation databases
Ensembl	ENSRNOT00000028636; ENSRNOP00000028636; ENSRNOG00000021090; Rattus norvegicus. [Genome view]
Organism-specific databases
RGD	3461. Pygm.
Phylogenomic databases
HOVERGEN	P09812.
Enzyme and pathway databases
BRENDA	2.4.1.1. 248.
Gene expression databases
ArrayExpress	P09812.
Genevestigator	P09812.
GermOnline	ENSRNOG00000021090. 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...

Entry information

Entry name

PYGM_RAT

Accession

Primary (citable) accession number: P09812

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 90 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)