3-hydroxy-3-methylglutaryl-coenzyme A reductase

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Reviewed, UniProtKB/Swiss-Prot P51639 (HMDH_RAT)

Last modified June 16, 2009. Version 82. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    3-hydroxy-3-methylglutaryl-coenzyme A reductase
      Short name=HMG-CoA reductase
    EC=1.1.1.34

Gene names

Name:

Hmgcr

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	887 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (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.
Subunit structure	Homodimer.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the HMG-CoA reductase family.

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Ontologies

Keywords
Biological process	Cholesterol biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Glycoprotein Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from direct assay. Source: RGD coenzyme A metabolic process Inferred from electronic annotation. Source: InterPro farnesyl diphosphate biosynthetic process, mevalonate pathway Traceable author statement. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from direct assay. Source: RGD
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro hydroxymethylglutaryl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: EC hydroxymethylglutaryl-CoA reductase activity Inferred from direct assay. Source: RGD protein homodimerization activity Ref.5 Inferred from direct assay. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 887

887

3-hydroxy-3-methylglutaryl-coenzyme A reductase

PRO_0000114424

Regions

Transmembrane

10 – 39

Potential

Transmembrane

57 – 78

Potential

Transmembrane

90 – 114

Potential

Transmembrane

124 – 149

Potential

Transmembrane

160 – 187

Potential

Transmembrane

192 – 220

Potential

Transmembrane

315 – 339

Potential

Region

340 – 449

110

Linker

Region

450 – 887

438

Catalytic

Sites

Active site

558

Charge relay system By similarity

Active site

690

Charge relay system By similarity

Active site

766

Charge relay system By similarity

Active site

865

Proton donor By similarity

Amino acid modifications

Modified residue

871

Phosphoserine Ref.4

Glycosylation

281

N-linked (GlcNAc...) Potential

Glycosylation

517

N-linked (GlcNAc...) Potential

Glycosylation

869

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

423

S → T AA sequence Ref.4

Sequence conflict

428

L → V AA sequence Ref.4

Sequence conflict

443

P → N AA sequence Ref.4

Sequence conflict

644 – 653

IRLQSKTGDA → PIRSPKRGTS Ref.3

Sequence conflict

673 – 674

FF → GV in AAA40608. Ref.1

Sequence conflict

722

T → S in CAA39001. Ref.3

Sequence conflict

750

A → L in AAA40608. Ref.1

Sequence conflict

764

G → A in CAA39001. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P51639-1 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: 856D99A9D5FA965C
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FASTA

887

96,688

        10         20         30         40         50         60 
MLSRLFRMHG LFVASHPWEV IVGTVTLTIC MMSMNMFTGN NKICGWNYEC 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 NSTAEQSKVS LGLAEDVSKR 

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

       370        380        390        400        410        420 
PKKAQDNCCR REPLLVRRNQ KLSSVEEDPG VNQDRKVEVI KPLVAEAETS GRATFVLGAS 

       430        440        450        460        470        480 
AASPPLALGA QEPGIELPSE PRPNEECLQI LESAEKGAKF LSDAEIIQLV NAKHIPAYKL 

       490        500        510        520        530        540 
ETLMETHERG VSIRRQLLSA KLAEPSSLQY LPYRDYNYSL VMGACCENVI GYMPIPVGVA 

       550        560        570        580        590        600 
GPLCLDGKEY QVPMATTEGC LVASTNRGCR AISLGGGASS RVLADGMSRG PVVRLPRACD 

       610        620        630        640        650        660 
SAEVKSWLET PEGFAVVKEA FDSTSRFARL QKLHVTLAGR NLYIRLQSKT GDAMGMNMIS 

       670        680        690        700        710        720 
KGTEKALLKL QEFFPELQIL AVSGNYCTDK KPAAINWIEG RGKTVVCEAV IPAKVVREVL 

       730        740        750        760        770        780 
KTTTEAMVDV NINKNLVGSA MAGSIGGYNA HAANIVTAIY IACGQDAAQN VGSSNCITLM 

       790        800        810        820        830        840 
EASGPTNEDL YISCTMPSIE IGTVGGGTNL LPQQACLQML GVQGACKDNP GENARQLARI 

       850        860        870        880 
VCGTVMAGEL SLMAALAAGH LVRSHMVHNR SKINLQDLQG TCTKKAA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of rat 3-hydroxy-3-methylglutaryl coenzyme A reductase." Hangjiong C., Williams D., Shapiro D. Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[3]	"Rat HMG-CoA reductase cDNA sequence contains an unusual 36 bp insert bounded by inverted repeats." Khan S., Kabat S., Stambrook P. Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 644-887. Strain: Sprague-Dawley. Tissue: Liver.
[4]	"Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver." Clarke P.R., Hardie D.G. EMBO J. 9:2439-2446(1990) [PubMed: 2369897] [Abstract] Cited for: PROTEIN SEQUENCE OF 423-443 AND 867-878, PHOSPHORYLATION AT SER-871. Tissue: Liver.
[5]	"Functional size of rat hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase as determined by radiation inactivation." Edwards P.A., Kempner E.S., Lan S.-F., Erickson S.K. J. Biol. Chem. 260:10278-10282(1985) [PubMed: 4019513] [Abstract] Cited for: CHARACTERIZATION. Tissue: Liver.
[6]	"Phosphorylation and inactivation of HMG-CoA reductase at the AMP-activated protein kinase site in response to fructose treatment of isolated rat hepatocytes." Gillespie J.G., Hardie D.G. FEBS Lett. 306:59-62(1992) [PubMed: 1628744] [Abstract] Cited for: PHOSPHORYLATION. Tissue: Liver.

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Cross-references

Sequence databases
	M29249 Genomic DNA. Translation: AAA40608.1. BC064654 mRNA. Translation: AAH64654.1. X55286 mRNA. Translation: CAA39001.1.
IPI	IPI00204259.
PIR	S33175.
RefSeq	NP_037266.2.
UniGene	Rn.9437
3D structure databases
HSSP	HSSP built from PDB template 1HWJ based on UniProtKB P04035.
SMR	P51639. Positions 461-869.
ModBase	Search...
PTM databases
PhosphoSite	P51639.
Genome annotation databases
Ensembl	ENSRNOG00000016122. Rattus norvegicus. [Contig view]
GeneID	25675.
KEGG	rno:25675.
NMPDR	fig\|10116.3.peg.15387.
Organism-specific databases
RGD	2803. Hmgcr.
Phylogenomic databases
HOVERGEN	P51639.
OMA	P51639. GAKFLSD.
Enzyme and pathway databases
BRENDA	1.1.1.34. 248.
Gene expression databases
ArrayExpress	P51639.
GermOnline	ENSRNOG00000016122. Rattus norvegicus.
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]
Gene3D	G3DSA:3.90.770.10. HMG-CoA_red. 1 hit.
PANTHER	PTHR10572. HMG-CoA_red. 1 hit.
Pfam	PF00368. HMG-CoA_red. 1 hit. [Graphical view]
PRINTS	PR00071. HMGCOARDTASE.
TIGRFAMs	TIGR00920. 2A060605. 1 hit. TIGR00533. HMG_CoA_R_NADP. 1 hit.
PROSITE	PS00066. HMG_COA_REDUCTASE_1. 1 hit. PS00318. HMG_COA_REDUCTASE_2. 1 hit. PS01192. HMG_COA_REDUCTASE_3. 1 hit. PS50065. HMG_COA_REDUCTASE_4. 1 hit. PS50156. SSD. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	607623.

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Entry information

Entry name

HMDH_RAT

Accession

Primary (citable) accession number: P51639
Secondary accession number(s): Q64601, Q6P2A6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 31, 2006
Last modified:	June 16, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents