GLPK_MOUSE
ID GLPK_MOUSE Reviewed; 559 AA.
AC Q64516; B1ASZ1; Q8C2M1; Q8C8X0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Glycerol kinase;
DE Short=GK;
DE Short=Glycerokinase;
DE EC=2.7.1.30 {ECO:0000269|PubMed:8884278};
DE AltName: Full=ATP:glycerol 3-phosphotransferase;
GN Name=Gk; Synonyms=Gyk {ECO:0000303|PubMed:8884278};
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] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=8884278; DOI=10.1006/geno.1996.0500;
RA Huq A.H., Lovell R.S., Sampson M.J., Decker W.K., Dinulos M.B.,
RA Disteche C.M., Craigen W.J.;
RT "Isolation, mapping, and functional expression of the mouse X chromosome
RT glycerol kinase gene.";
RL Genomics 36:530-534(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Retina, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Liver;
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: Key enzyme in the regulation of glycerol uptake and
CC metabolism. {ECO:0000250}.
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; Evidence={ECO:0000269|PubMed:8884278};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21645;
CC Evidence={ECO:0000269|PubMed:8884278};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC {ECO:0000269|PubMed:8884278}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q64516-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64516-2; Sequence=VSP_034650;
CC Name=1;
CC IsoId=Q64516-1; Sequence=VSP_034650, VSP_034651;
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR EMBL; U48403; AAC52824.1; -; mRNA.
DR EMBL; AK044308; BAC31861.1; -; mRNA.
DR EMBL; AK088373; BAC40312.1; -; mRNA.
DR EMBL; AL645567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003767; AAH03767.1; -; mRNA.
DR CCDS; CCDS41050.1; -. [Q64516-2]
DR CCDS; CCDS53126.1; -. [Q64516-1]
DR CCDS; CCDS81149.1; -. [Q64516-3]
DR RefSeq; NP_001281069.1; NM_001294140.1. [Q64516-3]
DR RefSeq; NP_032220.1; NM_008194.3. [Q64516-1]
DR RefSeq; NP_997609.1; NM_212444.2. [Q64516-2]
DR AlphaFoldDB; Q64516; -.
DR SMR; Q64516; -.
DR BioGRID; 200130; 3.
DR IntAct; Q64516; 3.
DR MINT; Q64516; -.
DR STRING; 10090.ENSMUSP00000119564; -.
DR iPTMnet; Q64516; -.
DR PhosphoSitePlus; Q64516; -.
DR SwissPalm; Q64516; -.
DR jPOST; Q64516; -.
DR MaxQB; Q64516; -.
DR PaxDb; Q64516; -.
DR PeptideAtlas; Q64516; -.
DR PRIDE; Q64516; -.
DR ProteomicsDB; 267454; -. [Q64516-3]
DR ProteomicsDB; 267455; -. [Q64516-2]
DR ProteomicsDB; 267456; -. [Q64516-1]
DR DNASU; 14933; -.
DR Ensembl; ENSMUST00000026039; ENSMUSP00000026039; ENSMUSG00000025059. [Q64516-1]
DR Ensembl; ENSMUST00000113978; ENSMUSP00000109611; ENSMUSG00000025059. [Q64516-3]
DR Ensembl; ENSMUST00000156390; ENSMUSP00000119564; ENSMUSG00000025059. [Q64516-2]
DR GeneID; 14933; -.
DR KEGG; mmu:14933; -.
DR UCSC; uc009trv.1; mouse. [Q64516-2]
DR UCSC; uc009trw.1; mouse. [Q64516-1]
DR UCSC; uc009trx.1; mouse. [Q64516-3]
DR CTD; 2710; -.
DR MGI; MGI:106594; Gk.
DR VEuPathDB; HostDB:ENSMUSG00000025059; -.
DR eggNOG; KOG2517; Eukaryota.
DR GeneTree; ENSGT01000000214434; -.
DR HOGENOM; CLU_009281_2_2_1; -.
DR InParanoid; Q64516; -.
DR OMA; FMLMNIG; -.
DR OrthoDB; 519426at2759; -.
DR PhylomeDB; Q64516; -.
DR TreeFam; TF321504; -.
DR Reactome; R-MMU-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00618; UER00672.
DR BioGRID-ORCS; 14933; 5 hits in 41 CRISPR screens.
DR ChiTaRS; Gk; mouse.
DR PRO; PR:Q64516; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q64516; protein.
DR Bgee; ENSMUSG00000025059; Expressed in proximal tubule and 264 other tissues.
DR ExpressionAtlas; Q64516; baseline and differential.
DR Genevisible; Q64516; MM.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004370; F:glycerol kinase activity; IDA:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006071; P:glycerol metabolic process; IMP:MGI.
DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IMP:MGI.
DR GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Glycerol metabolism; Kinase;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..559
FT /note="Glycerol kinase"
FT /id="PRO_0000059538"
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 265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 433..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 245..250
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8884278"
FT /id="VSP_034650"
FT VAR_SEQ 528..556
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8884278"
FT /id="VSP_034651"
FT CONFLICT 55
FT /note="Q -> R (in Ref. 2; BAC31861)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 61227 MW; 09A58CB47AB5CD41 CRC64;
MAAAKKAVLG PLVGAVDQGT SSTRFLVFNS KTAELLSHHQ VEIKQEFPRE GWVEQDPKEI
LQSVYECIEK TCEKLGQLNI DISNIKAIGV SNQRETTVVW DKVTGEPLYN AVVWLDLRTQ
STVENLSKRI PGNNNFVKSK TGLPLSTYFS AVKLRWLLDN VKKVQEAVEE NRALFGTIDS
WLIWSLTGGI HGGVHCTDVT NASRTMLFNI HSLEWDKELC EFFGIPMEIL PNVRSSSEIY
GLMKISHSLK AGALEGVPIS GCLGDQSAAL VGQMCFQDGQ AKNTYGTGCF LLCNTGHKCV
FSEHGLLTTV AYKLGRDKPV YYALEGSVAI AGAVIRWLRD NLGIIKSSEE IEKLAKEVGT
SYGCYFVPAF SGLYAPYWEP SARGIICGLT QFTNKCHIAF AALEAVCFQT REILDAMNRD
CGIPLSHLQV DGGMTSNKIL MQLQADILYI PVVKPSMPET TALGAAMAAG AAEGVGVWSL
EPEDLSAVTM ERFEPQINAE ESEIRYSTWK KAVMKSIGWV TTQSPESGDP SIFCSLPLGF
FIVSSMVMLI GARYISGIP