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Reviewed, UniProtKB/Swiss-Prot P12928 (KPYR_RAT)

Last modified November 3, 2009. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyruvate kinase isozymes R/L
    EC=2.7.1.40
Alternative name(s):
    L-PK
Gene names
Name: Pklr
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium.

Potassium.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.

Subunit structure

Homotetramer.

Miscellaneous

There are 4 isozymes of pyruvate kinase in mammals: L, R, M1 and M2. L type is major isozyme in the liver, R is found in red cells, M1 is the main form in muscle, heart and brain, and M2 is found in early fetal tissues.

Sequence similarities

Belongs to the pyruvate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Pyruvate
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Biological processATP biosynthetic process

Inferred from direct assay. Source: RGD

cellular response to insulin stimulus

Inferred from direct assay. Source: RGD

glycolysis

Inferred from direct assay. Source: RGD

pyruvate biosynthetic process

Inferred from direct assay. Source: RGD

response to ATP

Inferred from direct assay. Source: RGD

response to cAMP

Inferred from direct assay. Source: RGD

response to glucose stimulus

Inferred from expression pattern. Source: RGD

response to heat

Inferred from direct assay. Source: RGD

response to hypoxia

Inferred from expression pattern. Source: RGD

response to lithium ion

Inferred from direct assay. Source: RGD

response to nutrient

Inferred from expression pattern. Source: RGD

response to organic cyclic substance

Inferred from expression pattern. Source: RGD

   Cellular componentcytosol

Inferred from direct assay. Source: RGD

soluble fraction

Inferred from direct assay. Source: RGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

potassium ion binding

Inferred from electronic annotation. Source: InterPro

pyruvate kinase activity

Inferred from direct assay. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform R-type (identifier: P12928-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform L-type (identifier: P12928-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MSVQENTLPQQLWPWIFRSQKDLAKSALSGAPG → ME

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574Pyruvate kinase isozymes R/L
PRO_0000112096

Sites

Active site3131 By similarity
Metal binding3151Magnesium Potential
Metal binding3361Magnesium Potential
Metal binding3371Magnesium Potential

Amino acid modifications

Modified residue431Phosphoserine By similarity
Modified residue3481N6-acetyllysine By similarity
Modified residue5561Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 3333MSVQE…SGAPG → ME in isoform L-type.
VSP_002884

Experimental info

Sequence conflict1301S → Y in AAA41882. Ref.1
Sequence conflict1301S → Y in AAA41883. Ref.1
Sequence conflict3221K → R in AAA41882. Ref.1
Sequence conflict3221K → R in AAA41883. Ref.1
Sequence conflict4981R → G in AAA41880. Ref.3
Sequence conflict5011Q → K in AAA41880. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform R-type [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 6BBC544653C51380

FASTA57462,200
        10         20         30         40         50         60 
MSVQENTLPQ QLWPWIFRSQ KDLAKSALSG APGGPAGYLR RASVAQLTQE LGTAFFQQQQ 

        70         80         90        100        110        120 
LPAAMADTFL EHLCLLDIDS QPVAARSTSI IATIGPASRS VDRLKEMIKA GMNIARLNFS 

       130        140        150        160        170        180 
HGSHEYHAES IANIREATES FATSPLSYRP VAIALDTKGP EIRTGVLQGG PESEVEIVKG 

       190        200        210        220        230        240 
SQVLVTVDPK FQTRGDAKTV WVDYHNITRV VAVGGRIYID DGLISLVVQK IGPEGLVTEV 

       250        260        270        280        290        300 
EHGGILGSRK GVNLPNTEVD LPGLSEQDLL DLRFGVQHNV DIIFASFVRK ASDVLAVRDA 

       310        320        330        340        350        360 
LGPEGQNIKI ISKIENHEGV KKFDEILEVS DGIMVARGDL GIEIPAEKVF LAQKMMIGRC 

       370        380        390        400        410        420 
NLAGKPVVCA TQMLESMITK ARPTRAETSD VANAVLDGAD CIMLSGETAK GSFPVEAVMM 

       430        440        450        460        470        480 
QHAIAREAEA AVYHRQLFEE LRRAAPLSRD PTEVTAIGAV EASFKCCAAA IIVLTKTGRS 

       490        500        510        520        530        540 
AQLLSQYRPR AAVIAVTRSA QAARQVHLSR GVFPLLYREP PEAIWADDVD RRVQFGIESG 

       550        560        570 
KLRGFLRVGD LVIVVTGWRP GSGYTNIMRV LSVS 

« Hide

Isoform L-type.

Checksum: E5472B97649E2A47
Show »

FASTA54358,794

References

[1]"The L- and R-type isozymes of rat pyruvate kinase are produced from a single gene by use of different promoters."
Noguchi T., Yamada K., Inoue H., Matsuda T., Tanaka T.
J. Biol. Chem. 262:14366-14371(1987) [PubMed: 3654663] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete amino acid sequence of rat L-type pyruvate kinase deduced from the cDNA sequence."
Inoue H., Noguchi T., Tanaka T.
Eur. J. Biochem. 154:465-469(1986) [PubMed: 3002799] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Complete nucleotide and deduced amino acid sequences of rat L-type pyruvate kinase."
Lone Y.-C., Simon M.-P., Kahn A., Marie J.
FEBS Lett. 195:97-100(1986) [PubMed: 3080337] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Structure of the rat L-type pyruvate kinase gene."
Cognet M., Lone Y.C., Vaulont S., Kahn A., Marie J.
J. Mol. Biol. 196:11-25(1987) [PubMed: 3309348] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

M17091 expand/collapse EMBL AC list , M17088, M17089, M17090 Genomic DNA. Translation: AAA41882.1.
M17091 expand/collapse EMBL AC list , M17088, M17089, M17090 Genomic DNA. Translation: AAA41883.1.
M17685 mRNA. Translation: AAA41881.1.
X05684 Genomic DNA. Translation: CAA29169.1.
M11709 mRNA. Translation: AAA41880.1.
IPIIPI00202549.
IPI00231683.
PIRKIRTPR. A27427.
KIRTPL. A92940.
RefSeqNP_036756.3.
UniGeneRn.48821

3D structure databases

HSSPHSSP built from PDB template 1LIU based on UniProtKB P30613.
ModBaseSearch...

Protein-protein interaction databases

STRINGP12928.

PTM databases

PhosphoSiteP12928.

Proteomic databases

PRIDEP12928.

Genome annotation databases

EnsemblENSRNOT00000027700; ENSRNOP00000027700; ENSRNOG00000020420; Rattus norvegicus. [Genome view]
GeneID24651.
KEGGrno:24651.
NMPDRfig|10116.3.peg.16404.
UCSCNM_012624. rat.

Organism-specific databases

RGD3336. Pklr.

Phylogenomic databases

HOVERGENP12928.
OMAWVSKSQR.

Enzyme and pathway databases

BRENDA2.7.1.40. 248.

Gene expression databases

ArrayExpressP12928.
GenevestigatorP12928.
GermOnlineENSRNOG00000020420. Rattus norvegicus.

Family and domain databases

InterProIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
[Graphical view]
Gene3DG3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
G3DSA:3.40.1380.20. Pyrv_Knase_a/b. 1 hit.
PANTHERPTHR11817. Pyruvate_kinase. 1 hit.
PfamPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
ProDomPD001009. Pyruvate_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKPYR_RAT
AccessionPrimary (citable) accession number: P12928
Secondary accession number(s): P04763, Q64618
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1995
Last modified: November 3, 2009
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents