[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3065625 [NCBI, ExPASy, EBI, Israel, Japan] Basson M.E., Thorsness M., Finer-Moore J., Stroud R.M., Rine J.; "Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzyme of sterol biosynthesis."; Mol. Cell. Biol. 8:3797-3808(1988).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan] Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; Nature 387:90-93(1997).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 776-965. PubMed=3526336 [NCBI, ExPASy, EBI, Israel, Japan] Basson M.E., Thorsness M., Rine J.; "Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase."; Proc. Natl. Acad. Sci. U.S.A. 83:5563-5567(1986).
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-552, AND MASS SPECTROMETRY. DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan] Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.; "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."; J. Proteome Res. 6:1190-1197(2007).
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580 AND SER-581, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan] Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-552 AND SER-609, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).

Comments

FUNCTION: This transmembrane glycoprotein is involved in the control of cholesterol biosynthesis. It is the rate-limiting enzyme of the 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 .
INTERACTION:
Q08503:-; NbExp=1; IntAct=EBI-8377, EBI-36428;
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

M22002; AAA34676.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46373; CAA86503.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A30239; A30239.

RefSeq

NP_013636.1; -.

3D structure databases

HSSP

P04035; 1HWI. [HSSP ENTRY / PDB]

ModBase

P12683.

Protein-protein interaction databases

DIP

DIP:4529N; -.

IntAct

P12683; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-649; -.

Organism-specific databases

YML075c; -.

S000004540; HMG1.

Gene expression databases

ArrayExpress

P12683; -.

GermOnline

YML075C; Saccharomyces cerevisiae.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from direct assay from SGD).
GO:0005635;	Cellular component: nuclear envelope (inferred from direct assay from SGD).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR002202; HMG_CoA_Rdtase_cat.
IPR004554; HMG_CoA_Rdtase_I_cat.
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

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

P12683.

Proteomic databases

PeptideAtlas

P12683; -.

Genome annotation databases

Ensembl

YML075C; Saccharomyces cerevisiae. [Contig view]

854900; -.

Z71257_GR; YML075C.

sce:YML075C; -.

fig|4932.3.peg.4673; -.

Phylogenomic databases

HOGENOM

P12683; -.

Other

P12683; -.

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1054`	`1054`	`3-hydroxy-3-methylglutaryl-coenzyme A reductase 1.`	`PRO_0000114456`
`TRANSMEM`	`27 53`	`27`	`Potential.`
`TRANSMEM`	`187 211`	`25`	`Potential.`
`TRANSMEM`	`242 266`	`25`	`Potential.`
`TRANSMEM`	`300 324`	`25`	`Potential.`
`TRANSMEM`	`332 357`	`26`	`Potential.`
`TRANSMEM`	`398 422`	`25`	`Potential.`
`TRANSMEM`	`499 524`	`26`	`Potential.`
`REGION`	`525 617`	`93`	`Linker.`
`REGION`	`618 1054`	`437`	`Catalytic.`
`ACT_SITE`	`714 714`		`Charge relay system (By similarity).`
`ACT_SITE`	`848 848`		`Charge relay system (By similarity).`
`ACT_SITE`	`924 924`		`Charge relay system (By similarity).`
`ACT_SITE`	`1020 1020`		`Proton donor (By similarity).`
`MOD_RES`	`552 552`		`Phosphothreonine.`
`MOD_RES`	`580 580`		`Phosphoserine.`
`MOD_RES`	`581 581`		`Phosphoserine.`
`MOD_RES`	`609 609`		`Phosphoserine.`
`CARBOHYD`	`115 115`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`181 181`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`452 452`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`490 490`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`557 557`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`778 778`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 1054 AA [This is the length of the unprocessed precursor]

Molecular weight: 115626 Da [This is the MW of the unprocessed precursor]

CRC64: 2B624944FB7B2DD0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPPLFKGLKQ MAKPIAYVSR FSAKRPIHII LFSLIISAFA YLSVIQYYFN GWQLDSNSVF 

        70         80         90        100        110        120 
ETAPNKDSNT LFQECSHYYR DSSLDGWVSI TAHEASELPA PHHYYLLNLN FNSPNETDSI 

       130        140        150        160        170        180 
PELANTVFEK DNTKYILQED LSVSKEISST DGTKWRLRSD RKSLFDVKTL AYSLYDVFSE 

       190        200        210        220        230        240 
NVTQADPFDV LIMVTAYLMM FYTIFGLFND MRKTGSNFWL SASTVVNSAS SLFLALYVTQ 

       250        260        270        280        290        300 
CILGKEVSAL TLFEGLPFIV VVVGFKHKIK IAQYALEKFE RVGLSKRITT DEIVFESVSE 

       310        320        330        340        350        360 
EGGRLIQDHL LCIFAFIGCS MYAHQLKTLT NFCILSAFIL IFELILTPTF YSAILALRLE 

       370        380        390        400        410        420 
MNVIHRSTII KQTLEEDGVV PSTARIISKA EKKSVSSFLN LSVVVIIMKL SVILLFVFIN 

       430        440        450        460        470        480 
FYNFGANWVN DAFNSLYFDK ERVSLPDFIT SNASENFKEQ AIVSVTPLLY YKPIKSYQRI 

       490        500        510        520        530        540 
EDMVLLLLRN VSVAIRDRFV SKLVLSALVC SAVINVYLLN AARIHTSYTA DQLVKTEVTK 

       550        560        570        580        590        600 
KSFTAPVQKA STPVLTNKTV ISGSKVKSLS SAQSSSSGPS SSSEEDDSRD IESLDKKIRP 

       610        620        630        640        650        660 
LEELEALLSS GNTKQLKNKE VAALVIHGKL PLYALEKKLG DTTRAVAVRR KALSILAEAP 

       670        680        690        700        710        720 
VLASDRLPYK NYDYDRVFGA CCENVIGYMP LPVGVIGPLV IDGTSYHIPM ATTEGCLVAS 

       730        740        750        760        770        780 
AMRGCKAINA GGGATTVLTK DGMTRGPVVR FPTLKRSGAC KIWLDSEEGQ NAIKKAFNST 

       790        800        810        820        830        840 
SRFARLQHIQ TCLAGDLLFM RFRTTTGDAM GMNMISKGVE YSLKQMVEEY GWEDMEVVSV 

       850        860        870        880        890        900 
SGNYCTDKKP AAINWIEGRG KSVVAEATIP GDVVRKVLKS DVSALVELNI AKNLVGSAMA 

       910        920        930        940        950        960 
GSVGGFNAHA ANLVTAVFLA LGQDPAQNVE SSNCITLMKE VDGDLRISVS MPSIEVGTIG 

       970        980        990       1000       1010       1020 
GGTVLEPQGA MLDLLGVRGP HATAPGTNAR QLARIVACAV LAGELSLCAA LAAGHLVQSH 

      1030       1040       1050 
MTHNRKPAEP TKPNNLDATD INRLKDGSVT CIKS

P12683 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