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UniProtKB - P12928 (KPYR_RAT)
Protein
Pyruvate kinase PKLR
Gene
Pklr
Organism
Rattus norvegicus (Rat)
Status
Functioni
Plays a key role in glycolysis.
By similarityMiscellaneous
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.
Catalytic activityi
- EC:2.7.1.40
Cofactori
Protein has several cofactor binding sites:Activity regulationi
Allosterically activated by fructose 1,6-bisphosphate.By similarity
: glycolysis Pathwayi
This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate. This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 116 | SubstrateBy similarity | 1 | |
Metal bindingi | 118 | PotassiumBy similarity | 1 | |
Metal bindingi | 120 | PotassiumBy similarity | 1 | |
Metal bindingi | 156 | PotassiumBy similarity | 1 | |
Metal bindingi | 157 | Potassium; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 163 | ATPBy similarity | 1 | |
Binding sitei | 250 | ATPBy similarity | 1 | |
Sitei | 313 | Transition state stabilizerBy similarity | 1 | |
Metal bindingi | 315 | MagnesiumBy similarity | 1 | |
Binding sitei | 338 | Substrate; via amide nitrogenBy similarity | 1 | |
Metal bindingi | 339 | MagnesiumBy similarity | 1 | |
Binding sitei | 339 | Substrate; via amide nitrogenBy similarity | 1 | |
Binding sitei | 371 | SubstrateBy similarity | 1 | |
Binding sitei | 525 | Fructose-1,6-bisphosphate; allosteric activatorBy similarity | 1 | |
Binding sitei | 532 | Fructose-1,6-bisphosphate; allosteric activatorBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 118 – 121 | ATPBy similarity | 4 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- kinase activity Source: UniProtKB-KW
- magnesium ion binding Source: InterPro
- potassium ion binding Source: InterPro
- pyruvate kinase activity Source: RGD
GO - Biological processi
- ATP biosynthetic process Source: RGD
- carbohydrate metabolic process Source: RGD
- cellular response to epinephrine stimulus Source: RGD
- cellular response to insulin stimulus Source: RGD
- glycolytic process Source: RGD
- pyruvate biosynthetic process Source: RGD
- response to ATP Source: RGD
- response to cAMP Source: RGD
- response to glucose Source: RGD
- response to heat Source: RGD
- response to hypoxia Source: RGD
- response to lithium ion Source: RGD
- response to metal ion Source: RGD
- response to nutrient Source: RGD
- response to other organism Source: RGD
Keywordsi
Molecular function | Allosteric enzyme, Kinase, Transferase |
Biological process | Glycolysis |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate |
Enzyme and pathway databases
Reactomei | R-RNO-70171, Glycolysis |
SABIO-RKi | P12928 |
UniPathwayi | UPA00109;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 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3336, Pklr |
Subcellular locationi
Cytosol
- cytosol Source: RGD
Plasma Membrane
- plasma membrane Source: RGD
Other locations
- cytoplasm Source: RGD
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000112096 | 1 – 574 | Pyruvate kinase PKLRAdd BLAST | 574 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | PhosphoserineBy similarity | 1 | |
Modified residuei | 19 | PhosphoserineBy similarity | 1 | |
Modified residuei | 26 | PhosphoserineBy similarity | 1 | |
Modified residuei | 43 | PhosphoserineBy similarity | 1 | |
Modified residuei | 292 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
jPOSTi | P12928 |
PaxDbi | P12928 |
PRIDEi | P12928 |
PTM databases
iPTMneti | P12928 |
PhosphoSitePlusi | P12928 |
Expressioni
Gene expression databases
Bgeei | ENSRNOG00000020420, Expressed in liver and 18 other tissues |
ExpressionAtlasi | P12928, baseline and differential |
Genevisiblei | P12928, RN |
Interactioni
Subunit structurei
Homotetramer.
Protein-protein interaction databases
IntActi | P12928, 1 interactor |
MINTi | P12928 |
STRINGi | 10116.ENSRNOP00000027700 |
Chemistry databases
BindingDBi | P12928 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P12928 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 475 – 480 | Fructose-1,6-bisphosphate binding; allosteric activatorBy similarity | 6 | |
Regioni | 559 – 564 | Fructose-1,6-bisphosphate binding; allosteric activatorBy similarity | 6 |
Sequence similaritiesi
Belongs to the pyruvate kinase family.Curated
Phylogenomic databases
eggNOGi | KOG2323, Eukaryota |
GeneTreei | ENSGT00390000008859 |
HOGENOMi | CLU_015439_0_1_1 |
InParanoidi | P12928 |
OMAi | MVRVHHL |
OrthoDBi | 933620at2759 |
PhylomeDBi | P12928 |
TreeFami | TF300390 |
Family and domain databases
CDDi | cd00288, Pyruvate_Kinase, 1 hit |
Gene3Di | 2.40.33.10, 1 hit 3.20.20.60, 1 hit 3.40.1380.20, 1 hit |
InterProi | View protein in InterPro IPR001697, Pyr_Knase IPR015813, Pyrv/PenolPyrv_Kinase-like_dom IPR040442, Pyrv_Kinase-like_dom_sf IPR011037, Pyrv_Knase-like_insert_dom_sf IPR018209, Pyrv_Knase_AS IPR015793, Pyrv_Knase_brl IPR015795, Pyrv_Knase_C IPR036918, Pyrv_Knase_C_sf IPR015806, Pyrv_Knase_insert_dom_sf |
PANTHERi | PTHR11817, PTHR11817, 1 hit |
Pfami | View protein in Pfam PF00224, PK, 1 hit PF02887, PK_C, 1 hit |
PRINTSi | PR01050, PYRUVTKNASE |
SUPFAMi | SSF50800, SSF50800, 1 hit SSF51621, SSF51621, 1 hit SSF52935, SSF52935, 1 hit |
TIGRFAMsi | TIGR01064, pyruv_kin, 1 hit |
PROSITEi | View protein in PROSITE PS00110, PYRUVATE_KINASE, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
Isoform R-type (identifier: P12928-1) [UniParc]FASTAAdd to basket
Also known as: PKR
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A0H2UI07 | A0A0H2UI07_RAT | Pyruvate kinase | Pklr | 558 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 130 | S → Y in AAA41882 (PubMed:3654663).Curated | 1 | |
Sequence conflicti | 130 | S → Y in AAA41883 (PubMed:3654663).Curated | 1 | |
Sequence conflicti | 322 | K → R in AAA41882 (PubMed:3654663).Curated | 1 | |
Sequence conflicti | 322 | K → R in AAA41883 (PubMed:3654663).Curated | 1 | |
Sequence conflicti | 498 | R → G in AAA41880 (PubMed:3080337).Curated | 1 | |
Sequence conflicti | 501 | Q → K in AAA41880 (PubMed:3080337).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_002884 | 1 – 33 | MSVQE…SGAPG → ME in isoform L-type. CuratedAdd BLAST | 33 |
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 |
PIRi | A27427, KIRTPR A92940, KIRTPL |
RefSeqi | NP_036756.3, NM_012624.3 [P12928-2] XP_006232655.1, XM_006232593.3 [P12928-1] |
Genome annotation databases
Ensembli | ENSRNOT00000027700; ENSRNOP00000027700; ENSRNOG00000020420 [P12928-1] |
GeneIDi | 24651 |
KEGGi | rno:24651 |
UCSCi | RGD:3336, rat [P12928-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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 |
PIRi | A27427, KIRTPR A92940, KIRTPL |
RefSeqi | NP_036756.3, NM_012624.3 [P12928-2] XP_006232655.1, XM_006232593.3 [P12928-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6ECH | X-ray | 2.19 | A/B/C/D | 34-574 | [»] | |
6ECK | X-ray | 2.36 | A/B | 34-574 | [»] | |
SMRi | P12928 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P12928, 1 interactor |
MINTi | P12928 |
STRINGi | 10116.ENSRNOP00000027700 |
Chemistry databases
BindingDBi | P12928 |
ChEMBLi | CHEMBL3089 |
PTM databases
iPTMneti | P12928 |
PhosphoSitePlusi | P12928 |
Proteomic databases
jPOSTi | P12928 |
PaxDbi | P12928 |
PRIDEi | P12928 |
Genome annotation databases
Ensembli | ENSRNOT00000027700; ENSRNOP00000027700; ENSRNOG00000020420 [P12928-1] |
GeneIDi | 24651 |
KEGGi | rno:24651 |
UCSCi | RGD:3336, rat [P12928-1] |
Organism-specific databases
CTDi | 5313 |
RGDi | 3336, Pklr |
Phylogenomic databases
eggNOGi | KOG2323, Eukaryota |
GeneTreei | ENSGT00390000008859 |
HOGENOMi | CLU_015439_0_1_1 |
InParanoidi | P12928 |
OMAi | MVRVHHL |
OrthoDBi | 933620at2759 |
PhylomeDBi | P12928 |
TreeFami | TF300390 |
Enzyme and pathway databases
UniPathwayi | UPA00109;UER00188 |
Reactomei | R-RNO-70171, Glycolysis |
SABIO-RKi | P12928 |
Miscellaneous databases
PROi | PR:P12928 |
Gene expression databases
Bgeei | ENSRNOG00000020420, Expressed in liver and 18 other tissues |
ExpressionAtlasi | P12928, baseline and differential |
Genevisiblei | P12928, RN |
Family and domain databases
CDDi | cd00288, Pyruvate_Kinase, 1 hit |
Gene3Di | 2.40.33.10, 1 hit 3.20.20.60, 1 hit 3.40.1380.20, 1 hit |
InterProi | View protein in InterPro IPR001697, Pyr_Knase IPR015813, Pyrv/PenolPyrv_Kinase-like_dom IPR040442, Pyrv_Kinase-like_dom_sf IPR011037, Pyrv_Knase-like_insert_dom_sf IPR018209, Pyrv_Knase_AS IPR015793, Pyrv_Knase_brl IPR015795, Pyrv_Knase_C IPR036918, Pyrv_Knase_C_sf IPR015806, Pyrv_Knase_insert_dom_sf |
PANTHERi | PTHR11817, PTHR11817, 1 hit |
Pfami | View protein in Pfam PF00224, PK, 1 hit PF02887, PK_C, 1 hit |
PRINTSi | PR01050, PYRUVTKNASE |
SUPFAMi | SSF50800, SSF50800, 1 hit SSF51621, SSF51621, 1 hit SSF52935, SSF52935, 1 hit |
TIGRFAMsi | TIGR01064, pyruv_kin, 1 hit |
PROSITEi | View protein in PROSITE PS00110, PYRUVATE_KINASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | KPYR_RAT | |
Accessioni | P12928Primary (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: | February 23, 2022 | |
This is version 189 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families