[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3192541 [NCBI, ExPASy, EBI, Israel, Japan] Woodward H.D., Allen J.M.C., Lennarz W.J.; "3-hydroxy-3-methylglutaryl-coenzyme A reductase of the sea urchin embryo. Deduced structure and regulatory properties."; J. Biol. Chem. 263:18411-18418(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 689-735. PubMed=3276692 [NCBI, ExPASy, EBI, Israel, Japan] Woodward H.D., Allen J.M.C., Lennarz W.J.; "3-hydroxy-3-methylglutaryl coenzyme A reductase in the sea urchin embryo is developmentally regulated."; J. Biol. Chem. 263:2513-2517(1988).

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 .
SUBCELLULAR LOCATION: Endoplasmic reticulum 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

J04200; AAA30060.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J03523; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

A31898; A31898.

NP_999724.1; -.

3D structure databases

HSSP

P04035; 1DQA. [HSSP ENTRY / PDB]

ModBase

P16393.

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

P16393.

Genome annotation databases

GeneID

373355; -.

KEGG

spu:373355; -.

Other

ProtoNet

P16393.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 932`	`932`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase.`	`PRO_0000114425`
`TRANSMEM`	`20 40`	`21`	`Potential.`
`TRANSMEM`	`59 79`	`21`	`Potential.`
`TRANSMEM`	`92 112`	`21`	`Potential.`
`TRANSMEM`	`113 133`	`21`	`Potential.`
`TRANSMEM`	`162 182`	`21`	`Potential.`
`TRANSMEM`	`193 213`	`21`	`Potential.`
`TRANSMEM`	`322 342`	`21`	`Potential.`
`REGION`	`343 467`	`125`	`Linker.`
`REGION`	`468 932`	`465`	`Catalytic.`
`ACT_SITE`	`575 575`		`Charge relay system (By similarity).`
`ACT_SITE`	`707 707`		`Charge relay system (By similarity).`
`ACT_SITE`	`783 783`		`Charge relay system (By similarity).`
`ACT_SITE`	`882 882`		`Proton donor (By similarity).`
`CARBOHYD`	`279 279`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`850 850`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`886 886`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 932 AA [This is the length of the unprocessed precursor]

Molecular weight: 100966 Da [This is the MW of the unprocessed precursor]

CRC64: A645677DE1142A7B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSRLFLAQG RFCSSHPWEV IVCTLTLTIC MLSMNYFTGL PRICGWNYEC APQVKESSLS 

        70         80         90        100        110        120 
SDVLVMCIMR TLAVAYLYLQ FTKLRTTGSK YILGIAGLFT IFSSFLFSSA VIHLFGLELT 

       130        140        150        160        170        180 
GLNEALPFFL LLIDLTKASA LTKFALSSTT QNEVVDNIAR GMAILGPTIT LDTVVTTLVI 

       190        200        210        220        230        240 
SIGTMSSIRK MEVFCCFGIL SLIANYFVFM TFFPACLSLV LELSNSNKYG RPVWHLGRFA 

       250        260        270        280        290        300 
EVLEEEEDRK PNPVVQRVKM IMRTGLVLVH AHSYWLASND TELMSRDMLY DGNLLTDKKI 

       310        320        330        340        350        360 
DPTMPLWEFY ATRLWPPTLD YILTAILATV LASHYIFFSD LATYPEKRVS IMEGHEVVNP 

       370        380        390        400        410        420 
GSDHEDASEV ETIGTLSSSP STSDVRVIES MTSRTQACQT DPVTASPRNS RSSSPVSSHS 

       430        440        450        460        470        480 
VKPARFTIGS SGSGSEDEEE EVIKEEEVEW VLETELKAPR PMPELLEILN VGKGPNALTD 

       490        500        510        520        530        540 
DEVQLLVGAK HIPAYKLENI LDNPERGVAV RRQIISKLLP ITDALEKLPY ASYDYSFVSG 

       550        560        570        580        590        600 
ACCENVIGYM PVPVGVAGPL LLDGQEFQVP MATTEGCLVA STNRGCRALR SAGGIHSVLI 

       610        620        630        640        650        660 
GDGMTRGPLV RLPSAQEAGA IKQWLEVPEN FAAIKERFES TSRFAKLKSI QTALAGRYMF 

       670        680        690        700        710        720 
LRFKALTGDA MGMNMISKGT EQALHALQTM FPNIEIMSLS GNYCTDKKVA AINWIEGRGK 

       730        740        750        760        770        780 
SVVCEATVPA HIVQQVLKTS ASALVDLNIH KNLVGSAMAG SIGGFNAHAA NIVTAIYIAT 

       790        800        810        820        830        840 
GQDAAQNIAS SNCMTLMETR GPKGGDLYLS CTMPSIELGT VGGGTVLPPQ SACLQMMDVK 

       850        860        870        880        890        900 
GSNIHGSGLN ASQLARIVCA TVMAGELSLM SALAAGHLVK SHMKHNRSAL NIASPLPSID 

       910        920        930 
EVATHRRSKS VDFSALKESS AAAPGTCTAN AS

P16393 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