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Q0VCM4 (PYGL_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glycogen phosphorylase, liver form

EC=2.4.1.1
Gene names
Name:PYGL
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length851 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 By similarity.

Catalytic activity

(1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.

Cofactor

Pyridoxal phosphate By similarity.

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 By similarity.

Subunit structure

Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A. Interacts with PPP1R3B By similarity.

Post-translational modification

Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A By similarity.

Sequence similarities

Belongs to the glycogen phosphorylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 851850Glycogen phosphorylase, liver form
PRO_0000272607

Sites

Binding site761AMP By similarity
Site1091Involved in the association of subunits By similarity
Site1431Involved in the association of subunits By similarity
Site1561May be involved in allosteric control By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue151Phosphoserine; by PHK; in form phosphorylase A By similarity
Modified residue751Phosphotyrosine By similarity
Modified residue761Phosphotyrosine By similarity
Modified residue6811N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VCM4 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: A81FBC5224A71350

FASTA85197,456
        10         20         30         40         50         60 
MAKPLTDQEK RRQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR DYFFALAHTV 

        70         80         90        100        110        120 
RDHLVGRWIR TQQYYYEKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDM 

       130        140        150        160        170        180 
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IRDGWQIEEA 

       190        200        210        220        230        240 
DDWLRHGNPW EKARPEFMLP VHFYGRVEHT EAGTKWTDTQ VVLALPYDTP VPGYLNNTVN 

       250        260        270        280        290        300 
TMRLWSARAP NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 

       310        320        330        340        350        360 
VAATLQDVIR RFKASKFDSS NSTKTAFDAF PDQVAIQLND THPSLAIPEL MRIFVDIEKL 

       370        380        390        400        410        420 
PWSKAWEITQ KTFAYTNHTV LPEALERWPV ELVEKLLPRH LQIIYEINQK HLDKIAALFP 

       430        440        450        460        470        480 
KDVDRLRRMS LIEEEGGKRI NMAHLCIVGS HAVNGVAKIH SDIVKTQVFK DFSELEPDKF 

       490        500        510        520        530        540 
QNKTNGITPR RWLLLCNPGL AELIAEKIGE DYVKDLSQLT KLNSFLGDDI FLREISNVKQ 

       550        560        570        580        590        600 
ENKLKFSQFL EKEYKVKINP SSMFDVQVKR IHEYKRQLLN CLHVVTMYNR IKKDPKKLFV 

       610        620        630        640        650        660 
PRTVIIGGKA APGYYMAKLI IKLITSVAEV VNNDPVVGSK LKLIFLENYR VSLAEKVIPA 

       670        680        690        700        710        720 
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRIEDVA 

       730        740        750        760        770        780 
ALDKKGYEAK EYYEALPELK LAIDQIDKGF FSPKQPDLFK DLVNMLFYHD RFKVFADYEA 

       790        800        810        820        830        840 
YVKCQEKVSQ LYMNPKAWNI MVLKNIAASG KFSSDRTIKE YARDIWNMEP SDIKISLSSD 

       850 
PSGGANKANG K 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC120097 mRNA. Translation: AAI20098.1.
IPIIPI00685482.
RefSeqNP_001068671.1. NM_001075203.1.
UniGeneBt.39311.

3D structure databases

ProteinModelPortalQ0VCM4.
SMRQ0VCM4. Positions 6-839.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0VCM4.

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

Proteomic databases

PRIDEQ0VCM4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000015277; ENSBTAP00000015277; ENSBTAG00000011494.
GeneID505472.
KEGGbta:505472.

Organism-specific databases

CTD5836.

Phylogenomic databases

eggNOGmaNOG11381.
GeneTreeENSGT00390000016886.
HOVERGENHBG006848.
InParanoidQ0VCM4.
OMAMLFYHDR.
OrthoDBEOG4S1T6F.
PhylomeDBQ0VCM4.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
KOK00688.
PANTHERPTHR11468. Glyco_trans_35. 1 hit.
PfamPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsTIGR02093. P_ylase. 1 hit.
PROSITEPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYGL_BOVIN
AccessionPrimary (citable) accession number: Q0VCM4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: September 5, 2006
Last modified: November 16, 2011
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families