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Glycerol kinase (GK) (Glycerokinase) (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase)

 GLPK_MOUSE              Reviewed;         559 AA.
Q64516; B1ASZ1; Q8C2M1; Q8C8X0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
20-JUN-2018, entry version 139.
RecName: Full=Glycerol kinase;
Short=GK;
Short=Glycerokinase;
EC=2.7.1.30;
AltName: Full=ATP:glycerol 3-phosphotransferase;
Name=Gk; Synonyms=Gyk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ;
PubMed=8884278; DOI=10.1006/geno.1996.0500;
Huq A.H., Lovell R.S., Sampson M.J., Decker W.K., Dinulos M.B.,
Disteche C.M., Craigen W.J.;
"Isolation, mapping, and functional expression of the mouse X
chromosome glycerol kinase gene.";
Genomics 36:530-534(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=C57BL/6J, and NOD; TISSUE=Retina, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
metabolism. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3-
phosphate.
-!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Bound to the
mitochondrial surface or cytoplasmic. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=3;
IsoId=Q64516-3; Sequence=Displayed;
Name=2;
IsoId=Q64516-2; Sequence=VSP_034650;
Name=1;
IsoId=Q64516-1; Sequence=VSP_034650, VSP_034651;
-!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U48403; AAC52824.1; -; mRNA.
EMBL; AK044308; BAC31861.1; -; mRNA.
EMBL; AK088373; BAC40312.1; -; mRNA.
EMBL; AL645567; CAM16667.1; -; Genomic_DNA.
EMBL; AL672056; CAM16667.1; JOINED; Genomic_DNA.
EMBL; AL645567; CAM16668.1; -; Genomic_DNA.
EMBL; AL672056; CAM16668.1; JOINED; Genomic_DNA.
EMBL; AL672056; CAM25261.1; -; Genomic_DNA.
EMBL; AL645567; CAM25261.1; JOINED; Genomic_DNA.
EMBL; AL672056; CAM25262.1; -; Genomic_DNA.
EMBL; AL645567; CAM25262.1; JOINED; Genomic_DNA.
EMBL; BC003767; AAH03767.1; -; mRNA.
CCDS; CCDS41050.1; -. [Q64516-2]
CCDS; CCDS53126.1; -. [Q64516-1]
CCDS; CCDS81149.1; -. [Q64516-3]
RefSeq; NP_001281069.1; NM_001294140.1. [Q64516-3]
RefSeq; NP_032220.1; NM_008194.3. [Q64516-1]
RefSeq; NP_997609.1; NM_212444.2. [Q64516-2]
UniGene; Mm.246682; -.
ProteinModelPortal; Q64516; -.
SMR; Q64516; -.
BioGrid; 200130; 1.
IntAct; Q64516; 4.
MINT; Q64516; -.
STRING; 10090.ENSMUSP00000119564; -.
iPTMnet; Q64516; -.
PhosphoSitePlus; Q64516; -.
SwissPalm; Q64516; -.
MaxQB; Q64516; -.
PaxDb; Q64516; -.
PeptideAtlas; Q64516; -.
PRIDE; Q64516; -.
Ensembl; ENSMUST00000026039; ENSMUSP00000026039; ENSMUSG00000025059. [Q64516-1]
Ensembl; ENSMUST00000113978; ENSMUSP00000109611; ENSMUSG00000025059. [Q64516-3]
Ensembl; ENSMUST00000156390; ENSMUSP00000119564; ENSMUSG00000025059. [Q64516-2]
GeneID; 14933; -.
KEGG; mmu:14933; -.
UCSC; uc009trv.1; mouse. [Q64516-2]
UCSC; uc009trw.1; mouse. [Q64516-1]
UCSC; uc009trx.1; mouse. [Q64516-3]
CTD; 2710; -.
MGI; MGI:106594; Gk.
eggNOG; KOG2517; Eukaryota.
eggNOG; COG0554; LUCA.
GeneTree; ENSGT00530000063143; -.
HOGENOM; HOG000222134; -.
HOVERGEN; HBG002451; -.
InParanoid; Q64516; -.
KO; K00864; -.
OMA; WQDTRTQ; -.
OrthoDB; EOG091G04EJ; -.
PhylomeDB; Q64516; -.
TreeFam; TF321504; -.
Reactome; R-MMU-75109; Triglyceride biosynthesis.
UniPathway; UPA00618; UER00672.
ChiTaRS; Galk1; mouse.
PRO; PR:Q64516; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000025059; -.
CleanEx; MM_GYK; -.
ExpressionAtlas; Q64516; baseline and differential.
Genevisible; Q64516; MM.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004370; F:glycerol kinase activity; IDA:MGI.
GO; GO:0042393; F:histone binding; ISO:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0006071; P:glycerol metabolic process; IMP:MGI.
GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IBA:GO_Central.
GO; GO:0019217; P:regulation of fatty acid metabolic process; IMP:MGI.
GO; GO:0045471; P:response to ethanol; ISO:MGI.
GO; GO:0006641; P:triglyceride metabolic process; IBA:GO_Central.
InterPro; IPR000577; Carb_kinase_FGGY.
InterPro; IPR018485; Carb_kinase_FGGY_C.
InterPro; IPR018483; Carb_kinase_FGGY_CS.
InterPro; IPR018484; Carb_kinase_FGGY_N.
InterPro; IPR005999; Glycerol_kin.
Pfam; PF02782; FGGY_C; 1.
Pfam; PF00370; FGGY_N; 1.
PIRSF; PIRSF000538; GlpK; 1.
TIGRFAMs; TIGR01311; glycerol_kin; 1.
PROSITE; PS00933; FGGY_KINASES_1; 1.
PROSITE; PS00445; FGGY_KINASES_2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Glycerol metabolism; Kinase; Membrane; Mitochondrion;
Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
Transferase.
CHAIN 1 559 Glycerol kinase.
/FTId=PRO_0000059538.
NP_BIND 433 437 ATP. {ECO:0000250}.
BINDING 20 20 Substrate. {ECO:0000250}.
BINDING 24 24 ATP. {ECO:0000250}.
BINDING 94 94 Substrate. {ECO:0000250}.
BINDING 148 148 Substrate. {ECO:0000250}.
BINDING 265 265 Substrate. {ECO:0000250}.
BINDING 287 287 ATP. {ECO:0000250}.
BINDING 332 332 ATP; via carbonyl oxygen. {ECO:0000250}.
VAR_SEQ 245 250 Missing (in isoform 1 and isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:8884278}.
/FTId=VSP_034650.
VAR_SEQ 528 556 Missing (in isoform 1).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8884278}.
/FTId=VSP_034651.
CONFLICT 55 55 Q -> R (in Ref. 2; BAC31861).
{ECO:0000305}.
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


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