ID   Q8BV96_MOUSE            Unreviewed;       336 AA.
AC   Q8BV96;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=3-hydroxy-3-methylglutaryl coenzyme A reductase {ECO:0000256|RuleBase:RU361219};
DE            Short=HMG-CoA reductase {ECO:0000256|RuleBase:RU361219};
DE            EC=1.1.1.34 {ECO:0000256|RuleBase:RU361219};
DE   Flags: Fragment;
GN   Name=Hmgcr {ECO:0000313|MGI:MGI:96159};
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 {ECO:0000313|EMBL:BAC37602.1};
RN   [1] {ECO:0000313|EMBL:BAC37602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC37602.1};
RC   TISSUE=Urinary bladder {ECO:0000313|EMBL:BAC37602.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAC37602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC37602.1};
RC   TISSUE=Urinary bladder {ECO:0000313|EMBL:BAC37602.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAC37602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC37602.1};
RC   TISSUE=Urinary bladder {ECO:0000313|EMBL:BAC37602.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAC37602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC37602.1};
RC   TISSUE=Urinary bladder {ECO:0000313|EMBL:BAC37602.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAC37602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC37602.1};
RC   TISSUE=Urinary bladder {ECO:0000313|EMBL:BAC37602.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:BAC37602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC37602.1};
RC   TISSUE=Urinary bladder {ECO:0000313|EMBL:BAC37602.1};
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K.,
RA   Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y.,
RA   Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T.,
RA   Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R.,
RA   Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K.,
RA   Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S.,
RA   Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M.,
RA   Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:BAC37602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC37602.1};
RC   TISSUE=Urinary bladder {ECO:0000313|EMBL:BAC37602.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAC37602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC37602.1};
RC   TISSUE=Urinary bladder {ECO:0000313|EMBL:BAC37602.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-
CC         methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34;
CC         Evidence={ECO:0000256|RuleBase:RU361219};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC       biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00005084, ECO:0000256|RuleBase:RU361219}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU361219}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU361219}.
CC   -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
CC       {ECO:0000256|ARBA:ARBA00007661, ECO:0000256|RuleBase:RU361219}.
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DR   EMBL; AK079302; BAC37602.1; -; mRNA.
DR   RefSeq; NP_032281.2; NM_008255.2.
DR   AlphaFoldDB; Q8BV96; -.
DR   SMR; Q8BV96; -.
DR   PeptideAtlas; Q8BV96; -.
DR   DNASU; 15357; -.
DR   GeneID; 15357; -.
DR   KEGG; mmu:15357; -.
DR   AGR; MGI:96159; -.
DR   CTD; 3156; -.
DR   MGI; MGI:96159; Hmgcr.
DR   OrthoDB; 816560at2759; -.
DR   UniPathway; UPA00058; UER00103.
DR   BioGRID-ORCS; 15357; 17 hits in 83 CRISPR screens.
DR   ChiTaRS; Hmgcr; mouse.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   CDD; cd00643; HMG-CoA_reductase_classI; 1.
DR   Gene3D; 3.30.70.420; Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain; 1.
DR   InterPro; IPR002202; HMG_CoA_Rdtase.
DR   InterPro; IPR023074; HMG_CoA_Rdtase_cat_sf.
DR   InterPro; IPR023076; HMG_CoA_Rdtase_CS.
DR   InterPro; IPR004554; HMG_CoA_Rdtase_eu_arc.
DR   InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
DR   InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
DR   NCBIfam; TIGR00533; HMG_CoA_R_NADP; 1.
DR   PANTHER; PTHR10572; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE; 1.
DR   PANTHER; PTHR10572:SF24; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE; 1.
DR   Pfam; PF00368; HMG-CoA_red; 1.
DR   PRINTS; PR00071; HMGCOARDTASE.
DR   SUPFAM; SSF55035; NAD-binding domain of HMG-CoA reductase; 1.
DR   SUPFAM; SSF56542; Substrate-binding domain of HMG-CoA reductase; 1.
DR   PROSITE; PS00066; HMG_COA_REDUCTASE_1; 1.
DR   PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1.
DR   PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1.
DR   PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
DR   Genevisible; Q8BV96; MM.
PE   2: Evidence at transcript level;
KW   Cholesterol biosynthesis {ECO:0000256|ARBA:ARBA00022778};
KW   Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022778};
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU361219};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022955};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU361219};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361219};
KW   Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00022778};
KW   Sterol biosynthesis {ECO:0000256|ARBA:ARBA00022778};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00022778}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAC37602.1"
SQ   SEQUENCE   336 AA;  35497 MW;  B6C9DF1BDF08F9BC CRC64;
     VPMATTEGCL VASTNRGCRA ISLGGGASSR VLADGMTRGP VVRLPRACDS AEVKTWLETP
     EGFAVIKEAF DSTSRFARLQ KLHVTMAGRN LYIRFQSRTG DAMGMNMISK GTEKALLKLQ
     EFFPDMQILA VSGNYCTDKK PAAINWIEGR GKTVVCEAVI PAKVVREVLK TTTEAMVDVN
     INKNLVGSAM AGSIGGYNAH AANIVTAIYI ACGQDAAQNV GSSKCITLME ASGPTNEDLY
     ISCTMPSIEI GTVGGGTNLL PQQACLQMLG VQGACKDNPG ENARQLARIV CGTVMAGELS
     LMAALAAGHL VRSHMVHNRS KINLQDLQGT CTKKAA
//