KPYR_CANLF
ID KPYR_CANLF Reviewed; 574 AA.
AC Q29536; F1P923; F1PXP8; F1PY57;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Pyruvate kinase PKLR;
DE EC=2.7.1.40 {ECO:0000250|UniProtKB:P30613};
DE AltName: Full=Pyruvate kinase isozymes L/R;
GN Name=PKLR;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 56-574.
RC TISSUE=Reticulocyte;
RX PubMed=7520391;
RA Whitney K.M., Goodman S.A., Bailey E.M., Lothrop C.D. Jr.;
RT "The molecular basis of canine pyruvate kinase deficiency.";
RL Exp. Hematol. 22:866-874(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-134 (ISOFORM L-TYPE).
RC TISSUE=Liver;
RA Staten N.R.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pyruvate kinase that catalyzes the conversion of
CC phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which
CC plays a key role in glycolysis. {ECO:0000250|UniProtKB:P30613}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000250|UniProtKB:P30613};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18159;
CC Evidence={ECO:0000250|UniProtKB:P30613};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P30613};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P30613};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:P30613};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC bisphosphate. {ECO:0000250|UniProtKB:P30613}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000250|UniProtKB:P30613}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P30613}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=R-type; Synonyms=PKR;
CC IsoId=Q29536-1; Sequence=Displayed;
CC Name=L-type; Synonyms=PKL;
CC IsoId=Q29536-2; Sequence=VSP_042444;
CC -!- DISEASE: Note=Defects in PKLR are a cause of inherited hemolytic
CC anemia, an autosomal recessive disease of the Basenji dog that closely
CC resembles human pyruvate kinase deficiency.
CC {ECO:0000269|PubMed:7520391}.
CC -!- MISCELLANEOUS: There are 4 isozymes of pyruvate kinase in mammals: L,
CC R, M1 and M2. L type is major isozyme in the liver, R is found in red
CC cells, M1 is the main form in muscle, heart and brain, and M2 is found
CC in early fetal tissues. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=DN338485; Type=Miscellaneous discrepancy; Note=Derived from EST data.; Evidence={ECO:0000305};
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DR EMBL; AAEX03005338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AH004600; AAB31627.2; -; mRNA.
DR EMBL; DN338485; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001242947.1; NM_001256018.1.
DR RefSeq; NP_001243191.1; NM_001256262.1. [Q29536-1]
DR AlphaFoldDB; Q29536; -.
DR SMR; Q29536; -.
DR STRING; 9615.ENSCAFP00000061352; -.
DR PaxDb; Q29536; -.
DR PRIDE; Q29536; -.
DR Ensembl; ENSCAFT00030047792; ENSCAFP00030041802; ENSCAFG00030025851. [Q29536-1]
DR Ensembl; ENSCAFT00030047805; ENSCAFP00030041815; ENSCAFG00030025851. [Q29536-2]
DR Ensembl; ENSCAFT00040001436; ENSCAFP00040001228; ENSCAFG00040000772. [Q29536-1]
DR Ensembl; ENSCAFT00040001457; ENSCAFP00040001246; ENSCAFG00040000772. [Q29536-2]
DR Ensembl; ENSCAFT00845021649; ENSCAFP00845017017; ENSCAFG00845012059. [Q29536-1]
DR Ensembl; ENSCAFT00845021714; ENSCAFP00845017074; ENSCAFG00845012059. [Q29536-2]
DR GeneID; 490425; -.
DR KEGG; cfa:490425; -.
DR CTD; 5313; -.
DR VEuPathDB; HostDB:ENSCAFG00845012059; -.
DR eggNOG; KOG2323; Eukaryota.
DR GeneTree; ENSGT00390000008859; -.
DR InParanoid; Q29536; -.
DR OrthoDB; 933620at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000002254; Chromosome 7.
DR Bgee; ENSCAFG00000016959; Expressed in liver and 31 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; Alternative splicing; ATP-binding; Glycolysis; Kinase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Potassium; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..574
FT /note="Pyruvate kinase PKLR"
FT /id="PRO_0000112093"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 118..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 118
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 120
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 156
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 157
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 315
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 339
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 475..480
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 525
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 532
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 559..564
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT SITE 313
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00549"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT VAR_SEQ 1..33
FT /note="MSSQENIQPQELWSRISKSQRDLAKSILIGAPG -> ME (in isoform
FT L-type)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_042444"
FT CONFLICT 423
FT /note="A -> R (in Ref. 2; AAB31627)"
FT /evidence="ECO:0000305"
FT CONFLICT 458..459
FT /note="GA -> AT (in Ref. 2; AAB31627)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 62048 MW; F18E28450B1C7F30 CRC64;
MSSQENIQPQ ELWSRISKSQ RDLAKSILIG APGGPAGYLR RASVAQLTLE LGTAFFQQQQ
LSAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASHS VERLKEMIKA GMNIARLNFS
HGSHEYHAQS IANIREAVES FATSPLGYRP VAIALDTKGP EIRTGVLKGG PETEVELVKG
SWVLVTVDPA FRTLGDAHTV WVDYPNIVKV VPVGGRIFID DGLISLQVKK IDRKGLETQV
ENGGLLGSRK GVNLPGAEVD LPGLSEQDAQ DLRFGVEHNV DIVFASFVRK ASDVAAIRAA
LGPEGRTIKI ISKIENHEGV KKFDEILEVS DGIMVARGDL GIEIPAEKVF LAQKMMIGRC
NLAGKPVVCA TQMLESMITK PRPTRAETSD VANAVLDGAD CIMLSGETAK GKFPVEAVKM
QHAIAREAEA AVYHRQLFEE LRRAAPLSRD PTEVTAIGAV EAAFKCCAAA IIVLTKTGRS
AQLLSRYRPR AAVIAVTRSA QAARQAHLCR GVFPLLYSEP PEAIWADDVD RRVQFGIESG
KLRGFLRVGD LVIVVTGWRP GSGYTNIMRV LSIS
