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Q29536

- KPYR_CANFA

UniProt

Q29536 - KPYR_CANFA

Protein

Pyruvate kinase PKLR

Gene

PKLR

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (21 Mar 2012)
      Previous versions | rss
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    Functioni

    Plays a key role in glycolysis.By similarity

    Catalytic activityi

    ATP + pyruvate = ADP + phosphoenolpyruvate.

    Cofactori

    Magnesium.By similarity
    Potassium.By similarity

    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: UniProtKB-EC

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-UniPathway
    2. 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

    UniPathwayiUPA00109; UER00188.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate kinase PKLR (EC:2.7.1.40)
    Alternative name(s):
    Pyruvate kinase isozymes L/R
    Gene namesi
    Name:PKLR
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    Pathology & Biotechi

    Involvement in diseasei

    Defects in PKLR are a cause of inherited hemolytic anemia, an autosomal recessive disease of the Basenji dog that closely resembles human pyruvate kinase deficiency.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 574574Pyruvate kinase PKLRPRO_0000112093Add
    BLAST

    Proteomic databases

    PaxDbiQ29536.
    PRIDEiQ29536.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000030741.

    Structurei

    3D structure databases

    ProteinModelPortaliQ29536.
    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.
    HOGENOMiHOG000021559.
    HOVERGENiHBG000941.
    InParanoidiQ29536.
    KOiK12406.

    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: Q29536-1) [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

    MSSQENIQPQ ELWSRISKSQ RDLAKSILIG APGGPAGYLR RASVAQLTLE    50
    LGTAFFQQQQ LSAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASHS 100
    VERLKEMIKA GMNIARLNFS HGSHEYHAQS IANIREAVES FATSPLGYRP 150
    VAIALDTKGP EIRTGVLKGG PETEVELVKG SWVLVTVDPA FRTLGDAHTV 200
    WVDYPNIVKV VPVGGRIFID DGLISLQVKK IDRKGLETQV ENGGLLGSRK 250
    GVNLPGAEVD LPGLSEQDAQ DLRFGVEHNV DIVFASFVRK ASDVAAIRAA 300
    LGPEGRTIKI ISKIENHEGV KKFDEILEVS DGIMVARGDL GIEIPAEKVF 350
    LAQKMMIGRC NLAGKPVVCA TQMLESMITK PRPTRAETSD VANAVLDGAD 400
    CIMLSGETAK GKFPVEAVKM QHAIAREAEA AVYHRQLFEE LRRAAPLSRD 450
    PTEVTAIGAV EAAFKCCAAA IIVLTKTGRS AQLLSRYRPR AAVIAVTRSA 500
    QAARQAHLCR GVFPLLYSEP PEAIWADDVD RRVQFGIESG KLRGFLRVGD 550
    LVIVVTGWRP GSGYTNIMRV LSIS 574
    Length:574
    Mass (Da):62,048
    Last modified:March 21, 2012 - v2
    Checksum:iF18E28450B1C7F30
    GO
    Isoform L-type (identifier: Q29536-2) [UniParc]FASTAAdd to Basket

    Also known as: PKL

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

    Show »
    Length:543
    Mass (Da):58,657
    Checksum:iC4976F7282F91798
    GO

    Sequence cautioni

    The sequence DN338485 differs from that shown. Reason: Derived from EST data.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti423 – 4231A → R in AAB31627. (PubMed:7520391)Curated
    Sequence conflicti458 – 4592GA → AT in AAB31627. (PubMed:7520391)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3333MSSQE…IGAPG → ME in isoform L-type. 1 PublicationVSP_042444Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAEX03005338 Genomic DNA. No translation available.
    AH004600 mRNA. Translation: AAB31627.2.
    DN338485 mRNA. No translation available.
    RefSeqiNP_001242947.1. NM_001256018.1.
    NP_001243191.1. NM_001256262.1. [Q29536-1]
    UniGeneiCfa.8012.

    Genome annotation databases

    GeneIDi490425.
    KEGGicfa:490425.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAEX03005338 Genomic DNA. No translation available.
    AH004600 mRNA. Translation: AAB31627.2 .
    DN338485 mRNA. No translation available.
    RefSeqi NP_001242947.1. NM_001256018.1.
    NP_001243191.1. NM_001256262.1. [Q29536-1 ]
    UniGenei Cfa.8012.

    3D structure databases

    ProteinModelPortali Q29536.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000030741.

    Proteomic databases

    PaxDbi Q29536.
    PRIDEi Q29536.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 490425.
    KEGGi cfa:490425.

    Organism-specific databases

    CTDi 5313.

    Phylogenomic databases

    eggNOGi COG0469.
    HOGENOMi HOG000021559.
    HOVERGENi HBG000941.
    InParanoidi Q29536.
    KOi K12406.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00188 .

    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. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
      Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R.
      , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
      Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Boxer.
    2. "The molecular basis of canine pyruvate kinase deficiency."
      Whitney K.M., Goodman S.A., Bailey E.M., Lothrop C.D. Jr.
      Exp. Hematol. 22:866-874(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 56-574.
      Tissue: Reticulocyte.
    3. Staten N.R.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-134 (ISOFORM L-TYPE).
      Tissue: Liver.

    Entry informationi

    Entry nameiKPYR_CANFA
    AccessioniPrimary (citable) accession number: Q29536
    Secondary accession number(s): F1P923, F1PXP8, F1PY57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: March 21, 2012
    Last modified: October 1, 2014
    This is version 102 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