P79334 (PYGM_BOVIN) Reviewed, UniProtKB/Swiss-Prot

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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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 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.
Subunit structure	Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A By similarity.
Post-translational modification	Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A By similarity.
Involvement in disease	Note=Defects in PYGM are the cause of glycogen storage disease V (GSD-V); also known as McArdle disease. Ref.1
Sequence similarities	Belongs to the glycogen phosphorylase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Disease	Disease mutation Glycogen storage disease
Ligand	Nucleotide-binding Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
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_0000188528
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
Natural variations
	Natural variant	490	1	R → W in GSD-V. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P79334 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DFCEF2D8ADBF878E	FASTA	842	97,293
	10 20 30 40 50 60 MSRPLTDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAYTV 70 80 90 100 110 120 RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YIGRTLQNTM VNLALENACD EATYQLGLDM 130 140 150 160 170 180 EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA 190 200 210 220 230 240 DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN 250 260 270 280 290 300 TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 310 320 330 340 350 360 VAATLQDIIR RFKSSKFGCL DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDQERL 370 380 390 400 410 420 EWEKAWEVTV KTCAYTNHTV LPEALERWPV HLIETLLPRH LQIIYEINQR FLNRVAAAFP 430 440 450 460 470 480 GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF 490 500 510 520 530 540 QNKTNGITPR RWLVMCNPGL AEIIAERIGE EYIADLDQLR KLLSYVDDES FIRDVAKVKQ 550 560 570 580 590 600 ENKLKFSAYL EKEYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKKEPNKFFV 610 620 630 640 650 660 PRTVMIGGKA APGYHMAKMI IKLITAIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA 670 680 690 700 710 720 ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVE 730 740 750 760 770 780 RLDQKGYNAQ EYYDRIPELR HVIDQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYEE 790 800 810 820 830 840 YIKCQERVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP TRQRMPAPDE KI

References

[1]

"Cloning of bovine muscle glycogen phosphorylase cDNA and identification of a mutation in cattle with myophosphorylase deficiency, an animal model for McArdle's disease." Tsujino S., Shanske S., Valberg S.J., Cardinet G.H. III, Smith B.P., DiMauro S. Neuromuscul. Disord. 6:19-26(1996) [PubMed: 8845714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GSD-V TRP-490. Tissue: Skeletal muscle.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S82859 mRNA. Translation: AAB46846.1.
IPI	IPI00700882.
RefSeq	NP_786980.1. NM_175786.2.
UniGene	Bt.16003.
3D structure databases
ProteinModelPortal	P79334.
SMR	P79334. Positions 14-842.
ModBase	Search...
Protein-protein interaction databases
STRING	P79334.
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
Proteomic databases
PRIDE	P79334.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	327664.
KEGG	bta:327664.
Organism-specific databases
CTD	5837.
Phylogenomic databases
eggNOG	maNOG12882.
GeneTree	ENSGT00390000016886.
HOVERGEN	HBG006848.
InParanoid	P79334.
OrthoDB	EOG4S1T6F.
PhylomeDB	P79334.
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...

Entry information

Entry name

PYGM_BOVIN

Accession

Primary (citable) accession number: P79334

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2001
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