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3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34)

 HMDH_MESAU              Reviewed;         887 AA.
P09610;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
12-SEP-2018, entry version 132.
RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase;
Short=HMG-CoA reductase;
EC=1.1.1.34;
Name=HMGCR;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
NCBI_TaxID=10036;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3841506; DOI=10.1089/dna.1985.4.439;
Skalnik D.G., Simoni R.D.;
"The nucleotide sequence of Syrian hamster HMG-CoA reductase cDNA.";
DNA 4:439-444(1985).
[2]
ACTIVE SITES, AND MUTAGENESIS OF HIS-474; HIS-487; HIS-751; HIS-860;
HIS-865 AND HIS-868.
PubMed=8473286;
Darnay B.G., Rodwell V.W.;
"His865 is the catalytically important histidyl residue of Syrian
hamster 3-hydroxy-3-methylglutaryl-coenzyme A reductase.";
J. Biol. Chem. 268:8429-8435(1993).
[3]
ACTIVE SITES, SUBUNIT, AND MUTAGENESIS OF GLU-558 AND ASP-766.
PubMed=8288583;
Frimpong K., Rodwell V.W.;
"The active site of hamster 3-hydroxy-3-methylglutaryl-CoA reductase
resides at the subunit interface and incorporates catalytically
essential acidic residues from separate polypeptides.";
J. Biol. Chem. 269:1217-1221(1994).
-!- FUNCTION: Transmembrane glycoprotein that is the rate-limiting
enzyme in cholesterol biosynthesis as well as in the biosynthesis
of nonsterol isoprenoids that are essential for normal cell
function including ubiquinone and geranylgeranyl proteins.
-!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3-
hydroxy-3-methylglutaryl-CoA + 2 NADPH. {ECO:0000255|PROSITE-
ProRule:PRU10003}.
-!- ACTIVITY REGULATION: Regulated by a negative feedback mechanism
through sterols and non-sterol metabolites derived from
mevalonate.
-!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
-!- SUBUNIT: Homodimer. Interacts with INSIG1 (via its SSD); the
interaction, accelerated by sterols, leads to the recruitment of
HMGCR to AMFR/gp78 for its ubiquitination by the sterol-mediated
ERAD pathway. Interacts with UBIAD1 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- PTM: Undergoes sterol-mediated ubiquitination and ER-associated
degradation (ERAD). Accumulation of sterols in the endoplasmic
reticulum (ER) membrane, triggers binding of the reductase to the
ER membrane protein INSIG1. This INSIG1 binding leads to the
recruitment of the ubiquitin ligase, AMFR/gp78 or RNF145,
initiating ubiquitination of the reductase. The ubiquitinated
reductase is then extracted from the ER membrane and delivered to
cytosolic 26S proteosomes by a mechanism probably mediated by the
ATPase Valosin-containing protein VCP/p97. Lys-248 is the main
site of ubiquitination. Ubiquitination is enhanced by the presence
of a geranylgeranylated protein. {ECO:0000250|UniProtKB:P00347,
ECO:0000250|UniProtKB:P04035}.
-!- PTM: N-glycosylated. Deglycosylated by NGLY1 on release from the
endoplasmic reticulum (ER) in a sterol-mediated manner.
{ECO:0000250|UniProtKB:P04035}.
-!- SIMILARITY: Belongs to the HMG-CoA reductase family.
{ECO:0000305}.
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EMBL; M12705; AAA37077.1; -; mRNA.
PIR; A23586; A23586.
RefSeq; NP_001268631.1; NM_001281702.1.
ProteinModelPortal; P09610; -.
SMR; P09610; -.
BindingDB; P09610; -.
ChEMBL; CHEMBL1075267; -.
iPTMnet; P09610; -.
PRIDE; P09610; -.
GeneID; 101843185; -.
CTD; 3156; -.
HOVERGEN; HBG000453; -.
OrthoDB; EOG091G0I1B; -.
SABIO-RK; P09610; -.
UniPathway; UPA00058; UER00103.
PRO; PR:P09610; -.
Proteomes; UP000189706; Genome assembly.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
CDD; cd00643; HMG-CoA_reductase_classI; 1.
Gene3D; 1.10.3270.10; -; 1.
Gene3D; 3.30.70.420; -; 1.
Gene3D; 3.90.770.10; -; 2.
InterPro; IPR002202; HMG_CoA_Rdtase.
InterPro; IPR023074; HMG_CoA_Rdtase_cat_sf.
InterPro; IPR023076; HMG_CoA_Rdtase_CS.
InterPro; IPR004554; HMG_CoA_Rdtase_eu_arc.
InterPro; IPR004816; HMG_CoA_Rdtase_metazoan.
InterPro; IPR023282; HMG_CoA_Rdtase_N.
InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
InterPro; IPR000731; SSD.
PANTHER; PTHR10572; PTHR10572; 1.
Pfam; PF00368; HMG-CoA_red; 1.
Pfam; PF12349; Sterol-sensing; 1.
PRINTS; PR00071; HMGCOARDTASE.
SUPFAM; SSF55035; SSF55035; 1.
SUPFAM; SSF56542; SSF56542; 2.
TIGRFAMs; TIGR00920; 2A060605; 1.
TIGRFAMs; TIGR00533; HMG_CoA_R_NADP; 1.
PROSITE; PS00066; HMG_COA_REDUCTASE_1; 1.
PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1.
PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1.
PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
PROSITE; PS50156; SSD; 1.
1: Evidence at protein level;
Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome;
Endoplasmic reticulum; Glycoprotein; Isopeptide bond;
Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
Phosphoprotein; Reference proteome; Steroid biosynthesis;
Steroid metabolism; Sterol biosynthesis; Sterol metabolism;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 887 3-hydroxy-3-methylglutaryl-coenzyme A
reductase.
/FTId=PRO_0000114420.
TRANSMEM 10 39 Helical. {ECO:0000255}.
TRANSMEM 57 78 Helical. {ECO:0000255}.
TRANSMEM 90 114 Helical. {ECO:0000255}.
TRANSMEM 124 149 Helical. {ECO:0000255}.
TRANSMEM 160 187 Helical. {ECO:0000255}.
TRANSMEM 192 220 Helical. {ECO:0000255}.
TRANSMEM 315 339 Helical. {ECO:0000255}.
DOMAIN 61 218 SSD. {ECO:0000255|PROSITE-
ProRule:PRU00199}.
REGION 340 449 Linker.
REGION 450 887 Catalytic.
MOTIF 75 78 INSIG-binding motif. {ECO:0000250}.
COMPBIAS 243 246 Poly-Glu.
ACT_SITE 558 558 Charge relay system. {ECO:0000250}.
ACT_SITE 690 690 Charge relay system. {ECO:0000250}.
ACT_SITE 766 766 Charge relay system. {ECO:0000250}.
ACT_SITE 865 865 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10003}.
MOD_RES 871 871 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:P51639}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 517 517 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 869 869 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 89 89 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00347}.
CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00347}.
MUTAGEN 474 474 H->Q: No loss of activity.
{ECO:0000269|PubMed:8473286}.
MUTAGEN 487 487 H->Q: No loss of activity.
{ECO:0000269|PubMed:8473286}.
MUTAGEN 558 558 E->D,Q: Loss of activity.
{ECO:0000269|PubMed:8288583}.
MUTAGEN 751 751 H->Q: No loss of activity.
{ECO:0000269|PubMed:8473286}.
MUTAGEN 766 766 D->N: Loss of activity.
{ECO:0000269|PubMed:8288583}.
MUTAGEN 860 860 H->Q: No loss of activity.
{ECO:0000269|PubMed:8473286}.
MUTAGEN 865 865 H->K,Q: Loss of activity.
{ECO:0000269|PubMed:8473286}.
MUTAGEN 868 868 H->Y: No loss of activity.
{ECO:0000269|PubMed:8473286}.
SEQUENCE 887 AA; 96955 MW; BC6F9D1F8CAD5EA5 CRC64;
MLSRLFRMHG LFVASHPWEV IVGTVTLTIC MMSMNMFTGN NKICGWNYEC PKFEEDVLSS
DIIILTITRC IAILYIYFQF QNLRQLGSKY ILGIAGLFTI FSSFVFSTVV IHFLDKELTG
LNEALPFFLL LIDLSRASAL AKFALSSNSQ DEVRENIARG MAILGPTFTL DALVECLVIG
VGTMSGVRQL EIMCCFGCMS VLANYFVFMT FFPACVSLVL ELSRESREGR PIWQLSHFAR
VLEEEENKPN PVTQRVKMIM SLGLVLVHAH SRWIADPSPQ NSTTEHSKVS LGLDEDVSKR
IEPSVSLWQF YLSKMISMDI EQVVTLSLAF LLAVKYIFFE QAETESTLSL KNPITSPVAT
PKKAPDNCCR REPVLSRRNE KLSSVEEEPG VNQDRKVEVI KPLVAETEST SRATFVLGAS
GGCSPVALGT QEPEIELPSE PRPNEECLQI LESAEKGAKF LSDAEIIQLV NAKHIPAYKL
ETLMETHERG VSIRRQLLST KLPEPSSLQY LPYRDYNYSL VMGACCENVI GYMPIPVGVA
GPLCLDGKEY QVPMATTEGC LVASTNRGCR AIGLGGGASS RVLADGMTRG PVVRLPRACD
SAEVKAWLET PEGFAVIKDA FDSTSRFARL QKLHVTMAGR NLYIRFQSKT GDAMGMNMIS
KGTEKALVKL QEFFPEMQIL AVSGNYCTDK KPAAVNWIEG RGKTVVCEAV IPARVVREVL
KTTTEAMIDV NINKNLVGSA MAGSIGGYNA HAANIVTAIY IACGQDAAQN VGSSNCITLM
EASGPTNEDL YISCTMPSIE IGTVGGGTNL LPQQACLQML GVQGACKDNP GENARQLARI
VCGTVMAGEL SLMAALAAGH LVRSHMVHNR SKINLQDLQG TCTKKAA


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