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P12928

- KPYR_RAT

UniProt

P12928 - KPYR_RAT

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Protein
Pyruvate kinase PKLR
Gene
Pklr
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

Magnesium.
Potassium.

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161Substrate By similarity
Metal bindingi118 – 1181Potassium By similarity
Metal bindingi120 – 1201Potassium By similarity
Metal bindingi156 – 1561Potassium By similarity
Metal bindingi157 – 1571Potassium; via carbonyl oxygen By similarity
Sitei313 – 3131Transition state stabilizer By similarity
Metal bindingi315 – 3151Magnesium By similarity
Binding sitei338 – 3381Substrate; via amide nitrogen By similarity
Metal bindingi339 – 3391Magnesium By similarity
Binding sitei339 – 3391Substrate; via amide nitrogen By similarity
Binding sitei371 – 3711Substrate By similarity
Binding sitei525 – 5251Allosteric activator By similarity
Binding sitei532 – 5321Allosteric activator By 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
Complete GO annotation...

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.
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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 574574Pyruvate kinase PKLR
PRO_0000112096Add
BLAST

Proteomic databases

PaxDbiP12928.
PRIDEiP12928.

PTM databases

PhosphoSiteiP12928.

Expressioni

Gene expression databases

GenevestigatoriP12928.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP12928. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP12928.
SMRiP12928. Positions 57-573.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the pyruvate kinase family.

Phylogenomic databases

eggNOGiCOG0469.
GeneTreeiENSGT00390000008859.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiP12928.
KOiK12406.
OMAiCVTRNEQ.
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. Align

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

MSVQENTLPQ QLWPWIFRSQ KDLAKSALSG APGGPAGYLR RASVAQLTQE    50
LGTAFFQQQQ LPAAMADTFL EHLCLLDIDS QPVAARSTSI IATIGPASRS 100
VDRLKEMIKA GMNIARLNFS HGSHEYHAES IANIREATES FATSPLSYRP 150
VAIALDTKGP EIRTGVLQGG PESEVEIVKG SQVLVTVDPK FQTRGDAKTV 200
WVDYHNITRV VAVGGRIYID DGLISLVVQK IGPEGLVTEV EHGGILGSRK 250
GVNLPNTEVD LPGLSEQDLL DLRFGVQHNV DIIFASFVRK ASDVLAVRDA 300
LGPEGQNIKI ISKIENHEGV KKFDEILEVS DGIMVARGDL GIEIPAEKVF 350
LAQKMMIGRC NLAGKPVVCA TQMLESMITK ARPTRAETSD VANAVLDGAD 400
CIMLSGETAK GSFPVEAVMM QHAIAREAEA AVYHRQLFEE LRRAAPLSRD 450
PTEVTAIGAV EASFKCCAAA IIVLTKTGRS AQLLSQYRPR AAVIAVTRSA 500
QAARQVHLSR GVFPLLYREP PEAIWADDVD RRVQFGIESG KLRGFLRVGD 550
LVIVVTGWRP GSGYTNIMRV LSVS 574
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333MSVQE…SGAPG → ME in isoform L-type.
VSP_002884Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301S → Y in AAA41882. 1 Publication
Sequence conflicti130 – 1301S → Y in AAA41883. 1 Publication
Sequence conflicti322 – 3221K → R in AAA41882. 1 Publication
Sequence conflicti322 – 3221K → R in AAA41883. 1 Publication
Sequence conflicti498 – 4981R → G in AAA41880. 1 Publication
Sequence conflicti501 – 5011Q → K in AAA41880. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006232593.1. [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:
EMBL
GenBank
DDBJ
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_006232593.1. [P12928-1 ]
UniGenei Rn.48821.

3D structure databases

ProteinModelPortali P12928.
SMRi P12928. Positions 57-573.
ModBasei Search...

Protein-protein interaction databases

IntActi P12928. 1 interaction.

Chemistry

BindingDBi P12928.
ChEMBLi CHEMBL3089.

PTM databases

PhosphoSitei P12928.

Proteomic databases

PaxDbi P12928.
PRIDEi P12928.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000027700 ; ENSRNOP00000027700 ; ENSRNOG00000020420 . [P12928-1 ]
ENSRNOT00000065791 ; ENSRNOP00000058886 ; ENSRNOG00000020420 . [P12928-2 ]
GeneIDi 24651.
KEGGi rno:24651.
UCSCi RGD:3336. rat. [P12928-1 ]

Organism-specific databases

CTDi 5313.
RGDi 3336. Pklr.

Phylogenomic databases

eggNOGi COG0469.
GeneTreei ENSGT00390000008859.
HOGENOMi HOG000021559.
HOVERGENi HBG000941.
InParanoidi P12928.
KOi K12406.
OMAi CVTRNEQ.
OrthoDBi EOG78M01Q.
PhylomeDBi P12928.
TreeFami TF300390.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .
Reactomei REACT_225694. Glycolysis.
SABIO-RK P12928.

Miscellaneous databases

NextBioi 603974.
PROi P12928.

Gene expression databases

Genevestigatori P12928.

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProi IPR001697. 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 ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 140 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

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