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.
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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
//