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Q29512 (HMDH_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-hydroxy-3-methylglutaryl-coenzyme A reductase
Short name=HMG-CoA reductase
EC=1.1.1.34
Gene names
Name:HMGCR
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length888 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.

Subunit structure

Homodimer By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Peroxisome membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the HMG-CoA reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8888883-hydroxy-3-methylglutaryl-coenzyme A reductase
PRO_0000114423

Regions

Transmembrane10 – 3930Helical; Potential
Transmembrane57 – 7822Helical; Potential
Transmembrane90 – 11425Helical; Potential
Transmembrane124 – 14926Helical; Potential
Transmembrane160 – 18728Helical; Potential
Transmembrane192 – 22029Helical; Potential
Transmembrane315 – 33925Helical; Potential
Region340 – 449110Linker
Region450 – 888439Catalytic

Sites

Active site5591Charge relay system By similarity
Active site6911Charge relay system By similarity
Active site7671Charge relay system By similarity
Active site8661Proton donor By similarity

Amino acid modifications

Modified residue8721Phosphoserine; by AMPK By similarity
Glycosylation2811N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation5181N-linked (GlcNAc...) Potential
Glycosylation8701N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q29512 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 336CDEBF931110D9

FASTA88897,300
        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

« Hide

References

[1]Yamada M., Yoshimatsu M., Kinowaki M., Kai M., Kondo K., Setoguchi T.
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: New Zealand white.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

3D structure databases

ProteinModelPortalQ29512.
SMRQ29512. Positions 441-865.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ29512.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGmaNOG11482.
HOVERGENHBG000453.

Family and domain databases

InterProIPR002202. HMG_CoA_Rdtase.
IPR023074. HMG_CoA_Rdtase_cat.
IPR023076. HMG_CoA_Rdtase_CS.
IPR004554. HMG_CoA_Rdtase_eu_arc.
IPR004816. HMG_CoA_Rdtase_metazoan.
IPR023282. HMG_CoA_Rdtase_N.
IPR009023. HMG_CoA_Rdtase_NAD(P)-bd.
IPR009029. HMG_CoA_Rdtase_sub-bd.
IPR000731. SSD.
[Graphical view]
Gene3DG3DSA:3.30.70.420. G3DSA:3.30.70.420. 1 hit.
G3DSA:3.90.770.10. HMG-CoA_red. 2 hits.
G3DSA:1.10.3270.10. HMG_CoA_Rdtase_N. 1 hit.
PANTHERPTHR10572. HMG-CoA_red. 1 hit.
PfamPF00368. HMG-CoA_red. 1 hit.
[Graphical view]
PRINTSPR00071. HMGCOARDTASE.
SUPFAMSSF55035. HMG_CoA_NAD_bind. 1 hit.
SSF56542. HMG_CoA_sub_bind. 1 hit.
TIGRFAMsTIGR00920. 2A060605. 1 hit.
TIGR00533. HMG_CoA_R_NADP. 1 hit.
PROSITEPS00066. 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]
ProtoNetSearch...

Entry information

Entry nameHMDH_RABIT
AccessionPrimary (citable) accession number: Q29512
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 19, 2011
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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