ID HMDH_RABIT Reviewed; 888 AA. AC Q29512; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 62. DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase; DE Short=HMG-CoA reductase; DE EC=1.1.1.34; GN Name=HMGCR; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=New Zealand white; TISSUE=Liver; RA Yamada M., Yoshimatsu M., Kinowaki M., Kai M., Kondo K., Setoguchi T.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This transmembrane glycoprotein is involved in the CC control of cholesterol biosynthesis. It is the rate-limiting CC enzyme of sterol biosynthesis. CC -!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3- CC hydroxy-3-methylglutaryl-CoA + 2 NADPH. CC -!- PATHWAY: Metabolic intermediate biosynthesis; mevalonic acid CC biosynthesis; (R)-mevalonic acid from acetyl-CoA: step 3/3. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. Peroxisome membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR HSSP; P04035; 1HWJ. DR SMR; Q29512; 462-870. DR HOVERGEN; Q29512; -. DR BRENDA; 1.1.1.34; 255. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH)...; IEA:EC. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0006695; P:cholesterol biosynthetic 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 GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002202; HMG_CoA_Rdtase_cat. DR InterPro; IPR004554; HMG_CoA_Rdtase_I_cat. DR InterPro; IPR004816; HMG_CoA_Rdtase_I_metazoan. DR InterPro; IPR000731; SSD_5TM. DR Gene3D; G3DSA:3.90.770.10; HMG-CoA_red; 1. DR PANTHER; PTHR10572; HMG-CoA_red; 1. DR Pfam; PF00368; HMG-CoA_red; 1. DR PRINTS; PR00071; HMGCOARDTASE. DR TIGRFAMs; TIGR00920; 2A060605; 1. DR TIGRFAMs; TIGR00533; HMG_CoA_R_NADP; 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 PROSITE; PS50156; SSD; 1. PE 3: Inferred from homology; KW Cholesterol biosynthesis; Endoplasmic reticulum; Glycoprotein; KW Lipid synthesis; Membrane; NADP; Oxidoreductase; Peroxisome; KW Steroid biosynthesis; Sterol biosynthesis; Transmembrane. FT CHAIN 1 888 3-hydroxy-3-methylglutaryl-coenzyme A FT reductase. FT /FTId=PRO_0000114423. FT TRANSMEM 10 39 Potential. FT TRANSMEM 57 78 Potential. FT TRANSMEM 90 114 Potential. FT TRANSMEM 124 149 Potential. FT TRANSMEM 160 187 Potential. FT TRANSMEM 192 220 Potential. FT TRANSMEM 315 339 Potential. FT REGION 340 449 Linker. FT REGION 450 888 Catalytic. FT ACT_SITE 559 559 Charge relay system (By similarity). FT ACT_SITE 691 691 Charge relay system (By similarity). FT ACT_SITE 767 767 Charge relay system (By similarity). FT ACT_SITE 866 866 Proton donor (By similarity). FT CARBOHYD 281 281 N-linked (GlcNAc...) (Potential). FT CARBOHYD 296 296 N-linked (GlcNAc...) (Potential). FT CARBOHYD 518 518 N-linked (GlcNAc...) (Potential). FT CARBOHYD 870 870 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 888 AA; 97300 MW; 336CDEBF931110D9 CRC64; MLSRLFRMHG LFVASHPWEV IVGTVTLTIC MMSMNMFTGN DKICGWNYEC PKFEEDVLSS DIIILTITRC IAILYIYFQF QNLRQLGSKY ILGIAGLFTI FSSFVFSTVV IHFLDKELTG LNEALPFFLL LIDLSRASAL AKFALSSNSQ DEVRENIARG MAILGPTFTL DALVECLVIG VGTMSGVRQL EIMCCFGCMS VLANYFVFMT FFPACVSLVL ELSRESREGR PIWQLSHFAR VLEEEENKPN PVTQRVKMIM SLGLVLVHAH SRWIADPSPQ NSTADNSKVS LGLDENVSKR IEPSVSLWQF YLSKMISMDI EQVITLSLAL LLAVKYIFFE QAETESTLSL KNPITSPVVT QKKVPDSCCR REPVVVRNNQ KFCSVEEEAG MSQDRKVEVI KPLVAETDSP HRAAFVVGGS SFPDTSLVLE TKEPEIELPK EPRPNEECLQ ILGNAEKGAK FLSDAEIIQL VNAKHIPAYK LETLMETHER GVSIRRQLLS KKLPEPSSLQ YLPYRDYNYS LVLGACCENV IGYMPIPVGV VGPLCLDGKE FQVPMATTEG CLVASTNRGC RAICLGGGAS SRVLADGMTR GPVVRLPRAC DSAEVKAWLE TPEGFAVIKE AFDSTSRFAR LQKLHISMAG RNLYIRFQSR TGDAMGMNMI SKGTEKALSK LHEYFPEMQI LAVSGNYCTD KKPAAVNWIE GRGKTVVCEA VIPAKVVREV LKTTTEAMID VNINKNLVGS AMAGSIGGYN AHAANYVTAI YIACGQDAAQ NVGSSNCITL MEASGPPNED LYISCTMPSI EIGTVGGGTN LLPQQACLQM LGVQGACKDS PGENARQLAR IVCGTVMAGE LSLMAALAAG HLVKSHMIHN RSKINLQDLE GACTKKAA //