[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2813388 [NCBI, ExPASy, EBI, Israel, Japan] Rajkovic A., Simonsen J.N., Davis R.E., Rottman F.M.; "Molecular cloning and sequence analysis of 3-hydroxy-3-methylglutaryl-coenzyme A reductase from the human parasite Schistosoma mansoni."; Proc. Natl. Acad. Sci. U.S.A. 86:8217-8221(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-236. STRAIN=Puerto Rican; DOI=10.1074/jbc.270.37.21813; PubMed=7665603 [NCBI, ExPASy, EBI, Israel, Japan] Davis R.E., Hardwick C., Tavernier P., Hodgson S., Singh H.; "RNA trans-splicing in flatworms. Analysis of trans-spliced mRNAs and genes in the human parasite, Schistosoma mansoni."; J. Biol. Chem. 270:21813-21819(1995).

Comments

FUNCTION: This transmembrane glycoprotein is involved in the control of cholesterol and nonsterol isoprenoid compounds 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 .
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

Sequence databases

EMBL

M27294; AAA29896.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33178; AAC46885.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A34416; A34416.

3D structure databases

HSSP

P04035; 1HW8. [HSSP ENTRY / PDB]

ModBase

P16237.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
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.
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

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.
PROSITE graphical view of domain structure (profiles).

Other

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`	`1 948`	`948`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase.`	`PRO_0000114432`
`TRANSMEM`	`9 25`	`17`	`Potential.`
`TRANSMEM`	`55 71`	`17`	`Potential.`
`TRANSMEM`	`96 112`	`17`	`Potential.`
`TRANSMEM`	`124 140`	`17`	`Potential.`
`TRANSMEM`	`207 223`	`17`	`Potential.`
`TRANSMEM`	`286 302`	`17`	`Potential.`
`TRANSMEM`	`347 363`	`17`	`Potential.`
`REGION`	`364 466`	`103`	`Linker.`
`REGION`	`467 948`	`482`	`Catalytic.`
`ACT_SITE`	`567 567`		`Charge relay system (By similarity).`
`ACT_SITE`	`699 699`		`Charge relay system (By similarity).`
`ACT_SITE`	`777 777`		`Charge relay system (By similarity).`
`ACT_SITE`	`869 869`		`Proton donor (By similarity).`
`CARBOHYD`	`316 316`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`430 430`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`895 895`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 948 AA [This is the length of the unprocessed precursor]

Molecular weight: 107045 Da [This is the MW of the unprocessed precursor]

CRC64: CD5B9B84776371BF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLKILNTVLL FFDCFSTGTF FVLLIYLFTR LRTHLLHFSS SNCHLDVIIY QSRAVIIFLV 

        70         80         90        100        110        120 
VFVYFIGVLT CKINDKILVH TMLRNKRQLN TLFYTLILFT FALCSLSSVL FVPYTSFAIF 

       130        140        150        160        170        180 
LLSTSVFLLF SDLSVFFIVL EYYLLEIELV NYEHAKRHCL LSHLFSNQLF VDHMLGMFLK 

       190        200        210        220        230        240 
TSLFSISTTS KYAYLESIFK CTLMEQIIYI MIVFVFLPSF MRIFASYAKR MYGEQKKCLV 

       250        260        270        280        290        300 
SNKGVSSSTR KRRHSYSSGH SYVEYRRMSV HNLIGYVVNP NCHYKCWSTT FVIFVSLIIL 

       310        320        330        340        350        360 
HLNNRYSERI SSFKHNSSEN EVFPVLYHIT AYEVTSIFHF IYNIFHVINA NLVVYLFLGL 

       370        380        390        400        410        420 
FLFKRIRLNK PINSQLRNLN IPKIKETLIS DQVKQSPVLP KFSKKLNDIP LQSRKRIYCL 

       430        440        450        460        470        480 
HKDDDYIDRN DSSSVSTFSN TCKNSNERPS NVLDLDMLTE KIKQGLGHEL SDTEILQLLS 

       490        500        510        520        530        540 
HGRLKTRELE SVVRNPFRAV ELRRLDLSTF LNNPHIIERI PYKDYDYRLV YGQCCEEVIG 

       550        560        570        580        590        600 
YMPIPVGKIG PLLLDGRSHY IPLATTEGCL VASTNRGCRA IFLAGGIKSV VYRDQMTRAP 

       610        620        630        640        650        660 
VVWFPSIIDS VKCIAWIDSE EGFQTLKSAF DKTSAHVNLL SVFACPAGRY IHIRFAARTG 

       670        680        690        700        710        720 
DAMGMNMVSK ATDSALHCLK KYFSNMQVIS LSGNMCTDKK PATINTILGR GKSVIAEAHL 

       730        740        750        760        770        780 
SADVLAQVLH TNAQRLARLT HSKNWIGSAM AGCPGMMGCN AHAANIIAGM FAATGQDLAQ 

       790        800        810        820        830        840 
VVDSSSCLTQ LEVDLSDDSL VASVTMPCLE VGTVGGGTRL SGQRACLDLL DLSVDRPTEH 

       850        860        870        880        890        900 
LSRIIAGTVL AAELSLMAAL DTDDLVKAHM HFNRAKQSTN SHSCSHSTTT DNNDNISNIY 

       910        920        930        940 
DNHNVALSSK IPVTDNSDIR ESVHSLHVKP FPVKSDLSVN PEISHYTM

P16237 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