KPYR_MOUSE
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 03-AUG-2022, entry version 165.
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 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}.
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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 jPOST; P53657; -.
DR MaxQB; P53657; -.
DR PaxDb; P53657; -.
DR PeptideAtlas; P53657; -.
DR PRIDE; P53657; -.
DR ProteomicsDB; 263562; -. [P53657-1]
DR MGI; MGI:97604; Pklr.
DR eggNOG; KOG2323; Eukaryota.
DR InParanoid; P53657; -.
DR PhylomeDB; P53657; -.
DR Reactome; R-MMU-70171; Glycolysis.
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; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0006754; P:ATP biosynthetic process; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0006096; P:glycolytic process; ISO:MGI.
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:0009408; P:response to heat; ISO:MGI.
DR GO; GO:0010226; P:response to lithium ion; ISO:MGI.
DR GO; GO:0051707; P:response to other organism; IMP:MGI.
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 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
