GLPK_RAT
ID GLPK_RAT Reviewed; 524 AA.
AC Q63060;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glycerol kinase;
DE Short=GK;
DE Short=Glycerokinase;
DE EC=2.7.1.30;
DE AltName: Full=ATP-stimulated glucocorticoid-receptor translocation promoter;
DE Short=ASTP;
DE AltName: Full=ATP:glycerol 3-phosphotransferase;
GN Name=Gk; Synonyms=Gyk;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8323560; DOI=10.1006/bbrc.1993.1703;
RA Okamoto K., Hirano H., Isohashi F.;
RT "Molecular cloning of rat liver glucocorticoid-receptor translocation
RT promoter.";
RL Biochem. Biophys. Res. Commun. 193:848-854(1993).
CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC metabolism (By similarity). Increases the binding of activated
CC glucocorticoid-receptor to nuclei in the presence of ATP. {ECO:0000250,
CC ECO:0000269|PubMed:8323560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC EC=2.7.1.30;
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Bound to the mitochondrial
CC surface or cytoplasmic. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR EMBL; D16102; BAA03677.1; -; mRNA.
DR PIR; JN0606; JN0606.
DR RefSeq; NP_077357.2; NM_024381.2.
DR AlphaFoldDB; Q63060; -.
DR SMR; Q63060; -.
DR BioGRID; 249431; 1.
DR STRING; 10116.ENSRNOP00000059825; -.
DR iPTMnet; Q63060; -.
DR PhosphoSitePlus; Q63060; -.
DR PaxDb; Q63060; -.
DR PRIDE; Q63060; -.
DR GeneID; 79223; -.
DR KEGG; rno:79223; -.
DR CTD; 2710; -.
DR RGD; 70893; Gk.
DR eggNOG; KOG2517; Eukaryota.
DR InParanoid; Q63060; -.
DR OrthoDB; 519426at2759; -.
DR Reactome; R-RNO-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00618; UER00672.
DR PRO; PR:Q63060; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004370; F:glycerol kinase activity; ISO:RGD.
DR GO; GO:0042393; F:histone binding; IDA:RGD.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006071; P:glycerol metabolic process; ISO:RGD.
DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; ISO:RGD.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; ISO:RGD.
DR GO; GO:0009409; P:response to cold; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IDA:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR CDD; cd07792; FGGY_GK1-3_metazoa; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR042018; GK1-3_metazoa.
DR InterPro; IPR005999; Glycerol_kin.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Glycerol metabolism; Kinase; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..524
FT /note="Glycerol kinase"
FT /id="PRO_0000059539"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 427..431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 524 AA; 57477 MW; A620C296D32B6B84 CRC64;
MAAAKKAVLG PLVGAVDQGT SSTRFLVFNS KTAELLSHHQ VEIKQEFPRE GWVEQDPKEI
LQSVYECIEK TCEKLGQLNI DISNIKAIGV SNQRETTVVW DKLTGEPLYN AVVWLDLRTQ
STVEKLSKRI PGNNNFVKSK TGLPLSTYFS AVKLRWLLDN VKKVQEAVEE NRALFGTIDS
WLIWSLTGGI NGGVHCTDVT NASRTMLFNI HSLEWDKELC EFFGIPMEIL PNVRSSSEIY
GLMKAGALEG VPISGCLGDQ SAALVGQMCF QDGQAKNTYG TGCFLLCNTG HKCVFSEHGL
LTTVAYKLGR DKPVYYALEG SVAIAGAVIR WLRDNLGIIK SSEEIEKLAK EVGTSYGCYF
VPAFSALYAP YWEPSARGII CGLTQFTNKC HIAFAALEAV CFQTREILDA MNRDCGIPLS
HLQVDGGMTS NKILMQLQAD ILYIPVVKPS MPETTALGAA MAAGAAEGVG VWSLEPEDLS
AVTMERFEPQ INAEESEIRY STWKKAVMKS IGWVTTQSPE SGIP
