ID KIME_MOUSE Reviewed; 395 AA. AC Q9R008; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 10-JUN-2008, entry version 60. DE Mevalonate kinase (EC 2.7.1.36) (MK). GN Name=Mvk; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=99330561; PubMed=10401001; DOI=10.1093/hmg/8.8.1523; RA Houten S.M., Romeijn G.J., Koster J., Gray R.G.F., Darbyshire P., RA Smit G.P.A., de Klerk J.B.C., Duran R., Gibson K.M., Wanders R.J.A., RA Waterham H.R.; RT "Identification and characterization of three novel missense mutations RT in mevalonate kinase cDNA causing mevalonic aciduria, a disorder of RT isoprene biosynthesis."; RL Hum. Mol. Genet. 8:1523-1528(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: May be a regulatory site in cholesterol biosynthetic CC pathway. CC -!- CATALYTIC ACTIVITY: ATP + (R)-mevalonate = ADP + (R)-5- CC phosphomevalonate. CC -!- ENZYME REGULATION: Farnesyl- and geranyl-pyrophosphates are CC competitive inhibitors (By similarity). CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via CC mevalonate pathway; isopentenyl-PP from (R)-mevalonate: step 1/3. CC -!- PATHWAY: Context: Cholesterol biosynthesis. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome. CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase CC subfamily. 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; AF137598; AAF00700.1; -; mRNA. DR EMBL; BC005606; AAH05606.1; -; mRNA. DR RefSeq; NP_076045.1; -. DR UniGene; Mm.28088; -. DR HSSP; P17256; 1KVK. DR SMR; Q9R008; 1-394. DR Ensembl; ENSMUSG00000041939; Mus musculus. DR GeneID; 17855; -. DR KEGG; mmu:17855; -. DR NMPDR; fig|10090.3.peg.12235; -. DR MGI; MGI:107624; Mvk. DR HOVERGEN; Q9R008; -. DR ArrayExpress; Q9R008; -. DR CleanEx; MM_MVK; -. DR GermOnline; ENSMUSG00000041939; Mus musculus. DR GO; GO:0004496; F:mevalonate kinase activity; IDA:MGI. DR InterPro; IPR006204; GHMP_kinase. DR InterPro; IPR013750; GHMP_kinase_C. DR InterPro; IPR006203; GHMP_knse_ATP_bd_CS. DR InterPro; IPR006205; Mev_gal_kin. DR InterPro; IPR006206; Mev_galkinase. DR InterPro; IPR014721; Ribosomal_S5_D2-type_fold. DR Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1. DR PANTHER; PTHR10457:SF4; Mev_gal_kin; 1. DR Pfam; PF08544; GHMP_kinases_C; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PRINTS; PR00959; MEVGALKINASE. DR TIGRFAMs; TIGR00549; mevalon_kin; 1. DR PROSITE; PS00627; GHMP_KINASES_ATP; 1. PE 2: Evidence at transcript level; KW ATP-binding; Cholesterol biosynthesis; Cytoplasm; Kinase; KW Lipid synthesis; Nucleotide-binding; Peroxisome; Steroid biosynthesis; KW Sterol biosynthesis; Transferase. FT CHAIN 1 395 Mevalonate kinase. FT /FTId=PRO_0000156658. FT NP_BIND 138 148 ATP (Potential). SQ SEQUENCE 395 AA; 41877 MW; 953DB1C89403A3F8 CRC64; MLSEALLVSA PGKVILHGEH AVVHGKVALA AALNLRTFLL LRPQSNGKVS VNLPNIGIKQ VWDVGMLQRL DTSFLEQGDV SVPTLEQLEK LKKMGDLPRD RAGNEGMALL AFLYLYLAIC RKQRTLPSLD MVVWSELPPG AGLGSSAAYS VCLAAALLTA CEEVSNPLKD GVSVSRWPEE DLKSINKWAF EGERVIHGNP SGVDNAVSTW GGALRFQQGT MSSLKSLPSL QILLTNTKVP RSTKALVAAV RSRLTKFPEI VAPLLTSIDA ISLECERVLG EMVAAPVPEQ YLVLEELIDM NQHHLNALGV GHNSLDQLCQ VTAAHGLHSK LTGAGGGGCG ITLLKPGLEQ ATVEAAKQAL TSCGFDCWET SIGAPGVSTH SAAAVGDPVR QALGL //