[1]	NUCLEOTIDE SEQUENCE. STRAIN=New Zealand white; TISSUE=Liver; Yamada M., Yoshimatsu M., Kinowaki M., Kai M., Kondo K., Setoguchi T.; Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: This transmembrane glycoprotein is involved in the control of cholesterol biosynthesis. It is the rate-limiting enzyme of sterol biosynthesis.
CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP⁺ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH.
PATHWAY: Metabolic intermediate biosynthesis; mevalonic acid biosynthesis; (R)-mevalonic acid from acetyl-CoA: step 3/3 .
PATHWAY: Context: Cholesterol biosynthesis .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Peroxisome membrane; Multi-pass membrane protein.
SIMILARITY: Belongs to the HMG-CoA reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

HSSP

P04035; 1HWJ. [HSSP ENTRY / PDB]

SMR

Q29512; 462-870.

ModBase

Q29512.

Ontologies

GO:0005778;	Cellular component: peroxisomal membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR002202; HMG_CoA_Rdtase_cat.
IPR004554; HMG_CoA_Rdtase_I_cat.
IPR004816; HMG_CoA_Rdtase_I_metazoan.
IPR000731; SSD_5TM.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.770.10; HMG-CoA_red; 1.

PANTHER

PTHR10572; HMG-CoA_red; 1.

Pfam

PF00368; HMG-CoA_red; 1.
Pfam graphical view of domain structure.

PRINTS

PR00071; HMGCOARDTASE.

TIGRFAMs

TIGR00920; 2A060605; 1.
TIGR00533; HMG_CoA_R_NADP; 1.

PROSITE

PS00066; HMG_COA_REDUCTASE_1; 1.
PS00318; HMG_COA_REDUCTASE_2; 1.
PS01192; HMG_COA_REDUCTASE_3; 1.
PS50065; HMG_COA_REDUCTASE_4; 1.
PS50156; SSD; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q29512.

Phylogenomic databases

HOVERGEN

Q29512; -.

Other

ProtoNet

Q29512.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cholesterol biosynthesis; Endoplasmic reticulum; Glycoprotein; Lipid synthesis; Membrane; NADP; Oxidoreductase; Peroxisome; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 888`	`888`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase.`	`PRO_0000114423`
`TRANSMEM`	`10 39`	`30`	`Potential.`
`TRANSMEM`	`57 78`	`22`	`Potential.`
`TRANSMEM`	`90 114`	`25`	`Potential.`
`TRANSMEM`	`124 149`	`26`	`Potential.`
`TRANSMEM`	`160 187`	`28`	`Potential.`
`TRANSMEM`	`192 220`	`29`	`Potential.`
`TRANSMEM`	`315 339`	`25`	`Potential.`
`REGION`	`340 449`	`110`	`Linker.`
`REGION`	`450 888`	`439`	`Catalytic.`
`ACT_SITE`	`559 559`		`Charge relay system (By similarity).`
`ACT_SITE`	`691 691`		`Charge relay system (By similarity).`
`ACT_SITE`	`767 767`		`Charge relay system (By similarity).`
`ACT_SITE`	`866 866`		`Proton donor (By similarity).`
`CARBOHYD`	`281 281`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`296 296`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`518 518`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`870 870`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 888 AA [This is the length of the unprocessed precursor]

Molecular weight: 97300 Da [This is the MW of the unprocessed precursor]

CRC64: 336CDEBF931110D9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSRLFRMHG LFVASHPWEV IVGTVTLTIC MMSMNMFTGN DKICGWNYEC PKFEEDVLSS 

        70         80         90        100        110        120 
DIIILTITRC IAILYIYFQF QNLRQLGSKY ILGIAGLFTI FSSFVFSTVV IHFLDKELTG 

       130        140        150        160        170        180 
LNEALPFFLL LIDLSRASAL AKFALSSNSQ DEVRENIARG MAILGPTFTL DALVECLVIG 

       190        200        210        220        230        240 
VGTMSGVRQL EIMCCFGCMS VLANYFVFMT FFPACVSLVL ELSRESREGR PIWQLSHFAR 

       250        260        270        280        290        300 
VLEEEENKPN PVTQRVKMIM SLGLVLVHAH SRWIADPSPQ NSTADNSKVS LGLDENVSKR 

       310        320        330        340        350        360 
IEPSVSLWQF YLSKMISMDI EQVITLSLAL LLAVKYIFFE QAETESTLSL KNPITSPVVT 

       370        380        390        400        410        420 
QKKVPDSCCR REPVVVRNNQ KFCSVEEEAG MSQDRKVEVI KPLVAETDSP HRAAFVVGGS 

       430        440        450        460        470        480 
SFPDTSLVLE TKEPEIELPK EPRPNEECLQ ILGNAEKGAK FLSDAEIIQL VNAKHIPAYK 

       490        500        510        520        530        540 
LETLMETHER GVSIRRQLLS KKLPEPSSLQ YLPYRDYNYS LVLGACCENV IGYMPIPVGV 

       550        560        570        580        590        600 
VGPLCLDGKE FQVPMATTEG CLVASTNRGC RAICLGGGAS SRVLADGMTR GPVVRLPRAC 

       610        620        630        640        650        660 
DSAEVKAWLE TPEGFAVIKE AFDSTSRFAR LQKLHISMAG RNLYIRFQSR TGDAMGMNMI 

       670        680        690        700        710        720 
SKGTEKALSK LHEYFPEMQI LAVSGNYCTD KKPAAVNWIE GRGKTVVCEA VIPAKVVREV 

       730        740        750        760        770        780 
LKTTTEAMID VNINKNLVGS AMAGSIGGYN AHAANYVTAI YIACGQDAAQ NVGSSNCITL 

       790        800        810        820        830        840 
MEASGPPNED LYISCTMPSI EIGTVGGGTN LLPQQACLQM LGVQGACKDS PGENARQLAR 

       850        860        870        880 
IVCGTVMAGE LSLMAALAAG HLVKSHMIHN RSKINLQDLE GACTKKAA

Q29512 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools