ID KPYR_MOUSE Reviewed; 574 AA. AC P53657; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 24-JAN-2024, entry version 172. DE RecName: Full=Pyruvate kinase PKLR; DE EC=2.7.1.40 {ECO:0000250|UniProtKB:P30613}; DE AltName: Full=L-PK; DE AltName: Full=Pyruvate kinase isozymes L/R; GN Name=Pklr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CBA/N; TISSUE=Bone marrow; RX PubMed=7579416; RA Kanno H., Morimoto M., Fujii H., Tsujimura T., Asai H., Noguchi T., RA Kitamura Y., Miwa S.; RT "Primary structure of murine red blood cell-type pyruvate kinase (PK) and RT molecular characterization of PK deficiency identified in the CBA strain."; RL Blood 86:3205-3210(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and RC Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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=P53657-1; Sequence=Displayed; CC Name=L-type; Synonyms=PKL; CC IsoId=P53657-2; Sequence=Not described; 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S79731; AAB35435.1; -; mRNA. DR EMBL; D63764; BAA23642.1; -; mRNA. DR CCDS; CCDS17489.1; -. [P53657-1] DR AlphaFoldDB; P53657; -. DR SMR; P53657; -. DR ComplexPortal; CPX-3097; PKL pyruvate kinase complex. [P53657-2] DR ComplexPortal; CPX-3098; PKR pyruvate kinase complex. [P53657-1] DR STRING; 10090.ENSMUSP00000035417; -. DR iPTMnet; P53657; -. DR PhosphoSitePlus; P53657; -. DR SwissPalm; P53657; -. DR jPOST; P53657; -. DR MaxQB; P53657; -. DR PaxDb; 10090-ENSMUSP00000035417; -. DR PeptideAtlas; P53657; -. DR ProteomicsDB; 263562; -. [P53657-1] DR AGR; MGI:97604; -. DR MGI; MGI:97604; Pklr. DR eggNOG; KOG2323; Eukaryota. DR InParanoid; P53657; -. DR PhylomeDB; P53657; -. DR Reactome; R-MMU-70171; Glycolysis. [P53657-1] DR SABIO-RK; P53657; -. DR UniPathway; UPA00109; UER00188. DR ChiTaRS; Pklr; mouse. DR PRO; PR:P53657; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P53657; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:1902912; C:pyruvate kinase complex; ISO:ComplexPortal. 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:0048029; F:monosaccharide binding; ISO:MGI. DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro. DR GO; GO:0004743; F:pyruvate kinase activity; IDA:MGI. DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI. DR GO; GO:0006096; P:glycolytic process; IDA:MGI. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0042866; P:pyruvate biosynthetic process; ISO:MGI. DR GO; GO:0033198; P:response to ATP; ISO:MGI. DR GO; GO:0051591; P:response to cAMP; ISO:MGI. DR GO; GO:0051707; P:response to other organism; IMP:MGI. DR CDD; cd00288; Pyruvate_Kinase; 1. DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1. DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1. DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 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 NCBIfam; TIGR01064; pyruv_kin; 1. DR PANTHER; PTHR11817; PYRUVATE KINASE; 1. DR PANTHER; PTHR11817:SF31; PYRUVATE KINASE PKLR; 1. DR Pfam; PF00224; PK; 1. DR Pfam; PF02887; PK_C; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1. DR SUPFAM; SSF52935; PK C-terminal domain-like; 1. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. PE 1: Evidence at protein 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_0000112095" 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; by PKA" FT /evidence="ECO:0000250|UniProtKB:P30613" FT MOD_RES 292 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P30613" SQ SEQUENCE 574 AA; 62309 MW; 6C4689DE954E6166 CRC64; MSVQENELPQ QLWPWIFKSQ KDLAKSALSG APGGPAGYLR RASVAQLTQE LGTAFFQQQQ LPAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASRS VDRLKEMIKA GMNIARLNFS HGSHEYHAES IANIREAAES FATSPLSYRP VAIALDTKGP EIRTGVLQGG PESEVEIVKG SQVLVTVDPK FRTRGDAKTV WVDYHNITQV VAVGGRIYID DGLISLVVRK IGPEGLVTEV EHGGFLGNRK GVNLPNAEVD LPGLSEQDLL DLRFGVEHYV DIIFASFVRK ASDVVAVRDA LGPEGRGIKI ISKIENHEGV KKFDEILEVS DGIMMARGDL GIEIPAEKVF LAQKMMIGRC NLAGKPVVCA TQMLESMITK ARPTRAETSD VANAVLDGAD CIMLSGETAK GSFPVEAVKM QHAIAREAEA AVYHRQLFEE LRRAAPLSRD PTEVTAIGAV EASFKCCAAA IIVLTKTGRS AQLLSRYRPR AAVIAVTRSA QAARQVHLSR GVFPLLYREP PEAVWADDVD RRVQFGIESG KLRGFLRVGD LVIVVTGWRP GSGYTNIMRV LTIS //