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Protein

Pyruvate kinase PKLR

Gene

Pklr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a key role in glycolysis.By similarity

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Allosterically activated by fructose 1,6-bisphosphate.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161SubstrateBy similarity
Metal bindingi118 – 1181PotassiumBy similarity
Metal bindingi120 – 1201PotassiumBy similarity
Metal bindingi156 – 1561PotassiumBy similarity
Metal bindingi157 – 1571Potassium; via carbonyl oxygenBy similarity
Sitei313 – 3131Transition state stabilizerBy similarity
Metal bindingi315 – 3151MagnesiumBy similarity
Binding sitei338 – 3381Substrate; via amide nitrogenBy similarity
Metal bindingi339 – 3391MagnesiumBy similarity
Binding sitei339 – 3391Substrate; via amide nitrogenBy similarity
Binding sitei371 – 3711SubstrateBy similarity
Binding sitei525 – 5251Allosteric activatorBy similarity
Binding sitei532 – 5321Allosteric activatorBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: RGD

GO - Biological processi

  1. ATP biosynthetic process Source: RGD
  2. carbohydrate metabolic process Source: RGD
  3. cellular response to insulin stimulus Source: RGD
  4. glycolytic process Source: RGD
  5. pyruvate biosynthetic process Source: RGD
  6. response to ATP Source: RGD
  7. response to cAMP Source: RGD
  8. response to glucose Source: RGD
  9. response to heat Source: RGD
  10. response to hypoxia Source: RGD
  11. response to lithium ion Source: RGD
  12. response to metal ion Source: RGD
  13. response to nutrient Source: RGD
  14. response to organic cyclic compound Source: RGD
  15. response to other organism Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

ReactomeiREACT_225694. Glycolysis.
REACT_230812. Regulation of gene expression in beta cells.
REACT_260003. ChREBP activates metabolic gene expression.
SABIO-RKP12928.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase PKLR (EC:2.7.1.40)
Alternative name(s):
L-PK
Pyruvate kinase isozymes L/R
Gene namesi
Name:Pklr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi3336. Pklr.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 574574Pyruvate kinase PKLRPRO_0000112096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphoserineBy similarity
Modified residuei105 – 1051N6-acetyllysineBy similarity
Modified residuei109 – 1091N6-succinyllysineBy similarity
Modified residuei148 – 1481PhosphotyrosineBy similarity
Modified residuei292 – 2921PhosphoserineBy similarity
Modified residuei313 – 3131N6-acetyllysineBy similarity
Modified residuei365 – 3651N6-acetyllysine; alternateBy similarity
Modified residuei365 – 3651N6-succinyllysine; alternateBy similarity
Modified residuei541 – 5411N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP12928.
PRIDEiP12928.

PTM databases

PhosphoSiteiP12928.

Expressioni

Gene expression databases

ExpressionAtlasiP12928. baseline.
GenevestigatoriP12928.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP12928. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP12928.
SMRiP12928. Positions 57-573.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni475 – 4806Allosteric activator bindingBy similarity
Regioni559 – 5646Allosteric activator bindingBy similarity

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0469.
GeneTreeiENSGT00390000008859.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiP12928.
KOiK12406.
OMAiPEAVWAD.
OrthoDBiEOG78M01Q.
PhylomeDBiP12928.
TreeFamiTF300390.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform R-type (identifier: P12928-1) [UniParc]FASTAAdd to basket

Also known as: PKR

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.

« Hide

        10         20         30         40         50
MSVQENTLPQ QLWPWIFRSQ KDLAKSALSG APGGPAGYLR RASVAQLTQE
60 70 80 90 100
LGTAFFQQQQ LPAAMADTFL EHLCLLDIDS QPVAARSTSI IATIGPASRS
110 120 130 140 150
VDRLKEMIKA GMNIARLNFS HGSHEYHAES IANIREATES FATSPLSYRP
160 170 180 190 200
VAIALDTKGP EIRTGVLQGG PESEVEIVKG SQVLVTVDPK FQTRGDAKTV
210 220 230 240 250
WVDYHNITRV VAVGGRIYID DGLISLVVQK IGPEGLVTEV EHGGILGSRK
260 270 280 290 300
GVNLPNTEVD LPGLSEQDLL DLRFGVQHNV DIIFASFVRK ASDVLAVRDA
310 320 330 340 350
LGPEGQNIKI ISKIENHEGV KKFDEILEVS DGIMVARGDL GIEIPAEKVF
360 370 380 390 400
LAQKMMIGRC NLAGKPVVCA TQMLESMITK ARPTRAETSD VANAVLDGAD
410 420 430 440 450
CIMLSGETAK GSFPVEAVMM QHAIAREAEA AVYHRQLFEE LRRAAPLSRD
460 470 480 490 500
PTEVTAIGAV EASFKCCAAA IIVLTKTGRS AQLLSQYRPR AAVIAVTRSA
510 520 530 540 550
QAARQVHLSR GVFPLLYREP PEAIWADDVD RRVQFGIESG KLRGFLRVGD
560 570
LVIVVTGWRP GSGYTNIMRV LSVS
Length:574
Mass (Da):62,200
Last modified:February 1, 1995 - v2
Checksum:i6BBC544653C51380
GO
Isoform L-type (identifier: P12928-2) [UniParc]FASTAAdd to basket

Also known as: PKL

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

Show »
Length:543
Mass (Da):58,794
Checksum:iE5472B97649E2A47
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301S → Y in AAA41882 (PubMed:3654663).Curated
Sequence conflicti130 – 1301S → Y in AAA41883 (PubMed:3654663).Curated
Sequence conflicti322 – 3221K → R in AAA41882 (PubMed:3654663).Curated
Sequence conflicti322 – 3221K → R in AAA41883 (PubMed:3654663).Curated
Sequence conflicti498 – 4981R → G in AAA41880 (PubMed:3080337).Curated
Sequence conflicti501 – 5011Q → K in AAA41880 (PubMed:3080337).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333MSVQE…SGAPG → ME in isoform L-type. CuratedVSP_002884Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17091
, M17088, M17089, M17090 Genomic DNA. Translation: AAA41882.1.
M17091
, M17088, M17089, M17090 Genomic DNA. Translation: AAA41883.1.
M17685 mRNA. Translation: AAA41881.1.
X05684 Genomic DNA. Translation: CAA29169.1.
M11709 mRNA. Translation: AAA41880.1.
PIRiA27427. KIRTPR.
A92940. KIRTPL.
RefSeqiNP_036756.3. NM_012624.3. [P12928-2]
XP_006232655.1. XM_006232593.2. [P12928-1]
UniGeneiRn.48821.

Genome annotation databases

EnsembliENSRNOT00000027700; ENSRNOP00000027700; ENSRNOG00000020420. [P12928-1]
ENSRNOT00000065791; ENSRNOP00000058886; ENSRNOG00000020420. [P12928-2]
GeneIDi24651.
KEGGirno:24651.
UCSCiRGD:3336. rat. [P12928-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17091
, M17088, M17089, M17090 Genomic DNA. Translation: AAA41882.1.
M17091
, M17088, M17089, M17090 Genomic DNA. Translation: AAA41883.1.
M17685 mRNA. Translation: AAA41881.1.
X05684 Genomic DNA. Translation: CAA29169.1.
M11709 mRNA. Translation: AAA41880.1.
PIRiA27427. KIRTPR.
A92940. KIRTPL.
RefSeqiNP_036756.3. NM_012624.3. [P12928-2]
XP_006232655.1. XM_006232593.2. [P12928-1]
UniGeneiRn.48821.

3D structure databases

ProteinModelPortaliP12928.
SMRiP12928. Positions 57-573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP12928. 1 interaction.

Chemistry

BindingDBiP12928.
ChEMBLiCHEMBL3089.

PTM databases

PhosphoSiteiP12928.

Proteomic databases

PaxDbiP12928.
PRIDEiP12928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027700; ENSRNOP00000027700; ENSRNOG00000020420. [P12928-1]
ENSRNOT00000065791; ENSRNOP00000058886; ENSRNOG00000020420. [P12928-2]
GeneIDi24651.
KEGGirno:24651.
UCSCiRGD:3336. rat. [P12928-1]

Organism-specific databases

CTDi5313.
RGDi3336. Pklr.

Phylogenomic databases

eggNOGiCOG0469.
GeneTreeiENSGT00390000008859.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiP12928.
KOiK12406.
OMAiPEAVWAD.
OrthoDBiEOG78M01Q.
PhylomeDBiP12928.
TreeFamiTF300390.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
ReactomeiREACT_225694. Glycolysis.
REACT_230812. Regulation of gene expression in beta cells.
REACT_260003. ChREBP activates metabolic gene expression.
SABIO-RKP12928.

Miscellaneous databases

NextBioi603974.
PROiP12928.

Gene expression databases

ExpressionAtlasiP12928. baseline.
GenevestigatoriP12928.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiKPYR_RAT
AccessioniPrimary (citable) accession number: P12928
Secondary accession number(s): P04763, Q64618
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1995
Last modified: March 4, 2015
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.