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Q29536

- KPYR_CANFA

UniProt

Q29536 - KPYR_CANFA

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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

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 – 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: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
  2. 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

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 PKLR
PRO_0000112093Add
BLAST

Proteomic databases

PaxDbiQ29536.
PRIDEiQ29536.

Interactioni

Subunit structurei

Homotetramer By similarity.

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000030741.

Structurei

3D structure databases

ProteinModelPortaliQ29536.

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.
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333MSSQE…IGAPG → ME in isoform L-type.
VSP_042444Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti423 – 4231A → R in AAB31627. 1 Publication
Sequence conflicti458 – 4592GA → AT in AAB31627. 1 Publication

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

« 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 11, 2014
This is version 101 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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