Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyruvate kinase PKLR

Gene

PKLR

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
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

Pathway: glycolysis

This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (LOC100688969), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (LOC100683724), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (GAPDHS), Glyceraldehyde-3-phosphate dehydrogenase (LOC477441)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase PKLR (PKLR), Pyruvate kinase (PKLR), Pyruvate kinase (PKLR), Pyruvate kinase (pklr)
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 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

GO - Biological processi

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_294017. Regulation of gene expression in beta cells.
REACT_303596. ChREBP activates metabolic gene expression.
REACT_313542. Glycolysis.
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 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

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 residuei209 – 2091N6-acetyllysine; alternateBy similarity
Modified residuei209 – 2091N6-succinyllysine; alternateBy 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

PaxDbiQ29536.
PRIDEiQ29536.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000024956.

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. AlignAdd to basket

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

        10         20         30         40         50
MSSQENIQPQ ELWSRISKSQ RDLAKSILIG APGGPAGYLR RASVAQLTLE
60 70 80 90 100
LGTAFFQQQQ LSAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASHS
110 120 130 140 150
VERLKEMIKA GMNIARLNFS HGSHEYHAQS IANIREAVES FATSPLGYRP
160 170 180 190 200
VAIALDTKGP EIRTGVLKGG PETEVELVKG SWVLVTVDPA FRTLGDAHTV
210 220 230 240 250
WVDYPNIVKV VPVGGRIFID DGLISLQVKK IDRKGLETQV ENGGLLGSRK
260 270 280 290 300
GVNLPGAEVD LPGLSEQDAQ DLRFGVEHNV DIVFASFVRK ASDVAAIRAA
310 320 330 340 350
LGPEGRTIKI ISKIENHEGV KKFDEILEVS DGIMVARGDL GIEIPAEKVF
360 370 380 390 400
LAQKMMIGRC NLAGKPVVCA TQMLESMITK PRPTRAETSD VANAVLDGAD
410 420 430 440 450
CIMLSGETAK GKFPVEAVKM QHAIAREAEA AVYHRQLFEE LRRAAPLSRD
460 470 480 490 500
PTEVTAIGAV EAAFKCCAAA IIVLTKTGRS AQLLSRYRPR AAVIAVTRSA
510 520 530 540 550
QAARQAHLCR GVFPLLYSEP PEAIWADDVD RRVQFGIESG KLRGFLRVGD
560 570
LVIVVTGWRP GSGYTNIMRV LSIS
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.Derived from EST data.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ29536.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000024956.

Proteomic databases

PaxDbiQ29536.
PRIDEiQ29536.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi490425.
KEGGicfa:490425.

Organism-specific databases

CTDi5313.

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiQ29536.
KOiK12406.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
ReactomeiREACT_294017. Regulation of gene expression in beta cells.
REACT_303596. ChREBP activates metabolic gene expression.
REACT_313542. Glycolysis.

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

« Hide 'large scale' publications
  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: June 24, 2015
This is version 109 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.