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P12928

- KPYR_RAT

UniProt

P12928 - KPYR_RAT

Protein

Pyruvate kinase PKLR

Gene

Pklr

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    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 – 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

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 574574Pyruvate kinase PKLRPRO_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.
    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.
    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

    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:
    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...
    MobiDBi 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: October 1, 2014
    This is version 141 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