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

 HMDH_CRIGR              Reviewed;         887 AA.
P00347;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 134.
RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase;
Short=HMG-CoA reductase;
EC=1.1.1.34;
Name=HMGCR;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6546784; DOI=10.1038/308613a0;
Chin D.J., Gil G., Russell D.W., Liscum L., Luskey K.L., Basu S.K.,
Okayama H., Berg P., Goldstein J.L., Brown M.S.;
"Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A
reductase, a glycoprotein of endoplasmic reticulum.";
Nature 308:613-617(1984).
[2]
GLYCOSYLATION, AND STRUCTURE OF CARBOHYDRATES.
PubMed=6580634; DOI=10.1073/pnas.80.23.7165;
Liscum L., Cummings R.D., Anderson R.G., DeMartino G.N.,
Goldstein J.L., Brown M.S.;
"3-Hydroxy-3-methylglutaryl-CoA reductase: a transmembrane
glycoprotein of the endoplasmic reticulum with N-linked 'high-mannose'
oligosaccharides.";
Proc. Natl. Acad. Sci. U.S.A. 80:7165-7169(1983).
[3]
GENE STRUCTURE.
PubMed=6088070; DOI=10.1016/0092-8674(84)90549-X;
Reynolds G.A., Basu S.K., Osborne T.F., Chin D.J., Gil G., Brown M.S.,
Goldstein J.L., Luskey K.L.;
"HMG CoA reductase: a negatively regulated gene with unusual promoter
and 5' untranslated regions.";
Cell 38:275-285(1984).
[4]
DOMAINS.
PubMed=3965461;
Liscum L., Finer-Moore J., Stroud R.M., Luskey K.L., Brown M.S.,
Goldstein J.L.;
"Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase,
a glycoprotein of the endoplasmic reticulum.";
J. Biol. Chem. 260:522-530(1985).
[5]
UBIQUITINATION AT LYS-89 AND LYS-248, AND MUTAGENESIS OF TYR-75;
ILE-76; TYR-77; PHE-78; LYS-89 AND LYS-248.
PubMed=14563840; DOI=10.1074/jbc.M310053200;
Sever N., Song B.L., Yabe D., Goldstein J.L., Brown M.S.,
DeBose-Boyd R.A.;
"Insig-dependent ubiquitination and degradation of mammalian 3-
hydroxy-3-methylglutaryl-CoA reductase stimulated by sterols and
geranylgeraniol.";
J. Biol. Chem. 278:52479-52490(2003).
[6]
UBIQUITINATION AT LYS-89 AND LYS-248.
PubMed=15247208; DOI=10.1074/jbc.M405935200;
Doolman R., Leichner G.S., Avner R., Roitelman J.;
"Ubiquitin is conjugated by membrane ubiquitin ligase to three sites,
including the N terminus, in transmembrane region of mammalian 3-
hydroxy-3-methylglutaryl coenzyme A reductase: implications for
sterol-regulated enzyme degradation.";
J. Biol. Chem. 279:38184-38193(2004).
[7]
UBIQUITINATION, INTERACTION WITH INSIG1, AND MUTAGENESIS OF SER-60;
GLY-87 AND ALA-333.
PubMed=17090658; DOI=10.1194/jlr.M600476-JLR200;
Lee P.C., Nguyen A.D., Debose-Boyd R.A.;
"Mutations within the membrane domain of HMG-CoA reductase confer
resistance to sterol-accelerated degradation.";
J. Lipid Res. 48:318-327(2007).
-!- 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.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3-
hydroxy-3-methylglutaryl-CoA + 2 NADPH. {ECO:0000255|PROSITE-
ProRule:PRU10003}.
-!- ENZYME 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 UBIAD1 (By similarity).
Interacts (via its SSD) with INSIG1; the interaction, accelerated
by sterols, leads to the recruitment of HMGCR to AMFR/gp78 for its
ubiquitination by the sterol-mediated ERAD pathway. {ECO:0000250,
ECO:0000269|PubMed:17090658}.
-!- INTERACTION:
O94905:ERLIN2 (xeno); NbExp=2; IntAct=EBI-11426687, EBI-4400770;
O15503:INSIG1 (xeno); NbExp=2; IntAct=EBI-11426687, EBI-6252425;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein.
-!- PTM: N-glycosylated. Glycosylated with high mannose chains
including Man(6)(GlcNAc)(2), Man(7)(GlcNAc)(2) and
Man(8)(GlcNAc)(2). Deglycosylated by NGLY1 on release from the
endoplasmic reticulum (ER) in a sterol-mediated manner (By
similarity). {ECO:0000250}.
-!- PTM: Undergoes sterol-mediated ubiquitination and ER-association
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, 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:0000269|PubMed:14563840,
ECO:0000269|PubMed:15247208, ECO:0000269|PubMed:17090658}.
-!- SIMILARITY: Belongs to the HMG-CoA reductase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L00183; AAA36989.1; -; Genomic_DNA.
EMBL; L00166; AAA36989.1; JOINED; Genomic_DNA.
EMBL; L00169; AAA36989.1; JOINED; Genomic_DNA.
EMBL; L00170; AAA36989.1; JOINED; Genomic_DNA.
EMBL; L00171; AAA36989.1; JOINED; Genomic_DNA.
EMBL; L00173; AAA36989.1; JOINED; Genomic_DNA.
EMBL; L00176; AAA36989.1; JOINED; Genomic_DNA.
EMBL; L00177; AAA36989.1; JOINED; Genomic_DNA.
EMBL; L00178; AAA36989.1; JOINED; Genomic_DNA.
EMBL; L00179; AAA36989.1; JOINED; Genomic_DNA.
EMBL; L00180; AAA36989.1; JOINED; Genomic_DNA.
EMBL; L00181; AAA36989.1; JOINED; Genomic_DNA.
EMBL; L00182; AAA36989.1; JOINED; Genomic_DNA.
EMBL; X00494; CAA25189.1; -; Genomic_DNA.
PIR; A93328; RDHYE.
RefSeq; XP_003508040.1; XM_003507992.3.
RefSeq; XP_007634389.1; XM_007636199.2.
RefSeq; XP_007646809.1; XM_007648619.2.
ProteinModelPortal; P00347; -.
SMR; P00347; -.
IntAct; P00347; 3.
iPTMnet; P00347; -.
Ensembl; ENSCGRT00000004515; ENSCGRP00000004432; ENSCGRG00000003265.
Ensembl; ENSCGRT00001020833; ENSCGRP00001016589; ENSCGRG00001016870.
GeneID; 100756363; -.
KEGG; cge:100756363; -.
CTD; 3156; -.
HOVERGEN; HBG000453; -.
KO; K00021; -.
BRENDA; 1.1.1.34; 1309.
UniPathway; UPA00058; UER00103.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl.
GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
GO; GO:0042282; F:hydroxymethylglutaryl-CoA reductase activity; IDA:UniProtKB.
GO; GO:0070402; F:NADPH binding; IEA:Ensembl.
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.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0051262; P:protein tetramerization; IEA:Ensembl.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
CDD; cd00643; HMG-CoA_reductase_classI; 1.
Gene3D; 1.10.3270.10; -; 1.
Gene3D; 3.30.70.420; -; 1.
Gene3D; 3.90.770.10; -; 1.
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;
Endoplasmic reticulum; Glycoprotein; Isopeptide bond;
Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
Phosphoprotein; 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_0000114418.
TRANSMEM 10 39 Helical.
TRANSMEM 57 78 Helical.
TRANSMEM 90 114 Helical.
TRANSMEM 124 149 Helical.
TRANSMEM 160 187 Helical.
TRANSMEM 192 220 Helical.
TRANSMEM 315 339 Helical.
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:0000269|PubMed:14563840,
ECO:0000269|PubMed:15247208}.
CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:14563840,
ECO:0000269|PubMed:15247208}.
VARIANT 733 733 N -> C.
MUTAGEN 60 60 S->N: Abolishes sterol-mediated
interaction with INSIG1, and no
ubiquitination nor degradation.
{ECO:0000269|PubMed:17090658}.
MUTAGEN 75 75 Y->A: Very little effect on the sterol-
mediated ubiquitination and degradation
of HMGCR. Marked reduction in the sterol-
mediated ubiquitination and degradation
of HMGCR; when associated with A-77.
Completely abolishes the sterol effect on
ubiquitination and degradation of HMGCR;
when associated with A-76; A-77 and A-78.
{ECO:0000269|PubMed:14563840}.
MUTAGEN 76 76 I->A: Greatly reduced sterol-mediated
ubiquitination and degradation of HMGCR.
Completely abolishes the sterol effect on
ubiquitination and degradation of HMGCR;
when associated with A-75; A-77 and A-78.
{ECO:0000269|PubMed:14563840}.
MUTAGEN 77 77 Y->A: Greatly reduced sterol-mediated
ubiquitination and degradation of HMGCR.
Marked reduction in the sterol-mediated
ubiquitination and degradation of HMGCR;
when associated with A-75. Completely
abolishes the sterol effect on
ubiquitination and degradation of HMGCR;
when associated with A-75; A-76 and A-78.
{ECO:0000269|PubMed:14563840}.
MUTAGEN 78 78 F->A: Very little effect on the sterol-
mediated ubiquitination and degradation
of HMGCR. Completely abolishes the sterol
effect on ubiquitination and degradation
of HMGCR; when associated with A-75; A-76
and A-77. {ECO:0000269|PubMed:14563840}.
MUTAGEN 87 87 G->R: Abolishes sterol-mediated
interaction with INSIG1, and no
ubiquitination nor degradation.
{ECO:0000269|PubMed:17090658}.
MUTAGEN 89 89 K->R: Little effect on sterol plus
mevalonate-stimulated ubiquitination and
degradation of HMGCR in the presence of
INSIG1. No sterol plus mevalonate-
stimulated ubiquitination and degradation
of HMGCR in the presence of INSIG1; when
associated with R-248.
{ECO:0000269|PubMed:14563840}.
MUTAGEN 248 248 K->R: Some reduction in sterol plus
mevalonate-stimulated ubiquitination and
degradation of HMGCR in the presence of
INSIG1. No sterol plus mevalonate-
stimulated ubiquitination and degradation
of HMGCR in the presence of INSIG1; when
associated with R-89.
{ECO:0000269|PubMed:14563840}.
MUTAGEN 333 333 A->P: Abolishes sterol-mediated
interaction with INSIG1, and no
ubiquitination nor degradation.
{ECO:0000269|PubMed:17090658}.
SEQUENCE 887 AA; 97081 MW; 4331E53ADA250E6A 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 KNPITSPVVT
PKKAPDNCCR REPLLVRRSE KLSSVEEEPG VSQDRKVEVI KPLVVETESA SRATFVLGAS
GTSPPVAART QELEIELPSE PRPNEECLQI LESAEKGAKF LSDAEIIQLV NAKHIPAYKL
ETLMETHERG VSIRRQLLST KLPEPSSLQY LPYRDYNYSL VMGACCENVI GYMPIPVGVA
GPLCLDGKEY QVPMATTEGC LVASTNRGCR AIGLGGGASS RVLADGMTRG PVVRLPRACD
SAEVKAWLET PEGFAVIKDA FDSTSRFARL QKLHVTMAGR NLYIRFQSKT GDAMGMNMIS
KGTEKALLKL QEFFPEMQIL AVSGNYCTDK KPAAINWIEG RGKTVVCEAV IPAKVVREVL
KTTTEAMIDV NINKNLVGSA MAGSIGGYNA HAANIVTAIY IACGQDAAQN VGSSNCITLM
EASGPTNEDL YISCTMPSIE IGTVGGGTNL LPQQACLQML GVQGACKDNP GENARQLARI
VCGTVMAGEL SLMAALAAGH LVRSHMVHNR SKINLQDLQG TCTKKSA


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