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UniProtKB/Swiss-Prot entry P00347


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HMDH_CRIGR
Primary accession number P00347
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 72)
Name and origin of the protein
Protein name 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Synonyms HMG-CoA reductase
EC 1.1.1.34
Gene name
Name: HMGCR
From
Cricetulus griseus (Chinese hamster) [TaxID: 10029] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Cricetidae; Cricetinae; Cricetulus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1038/308613a0; PubMed=6546784 [NCBI, ExPASy, EBI, Israel, Japan]
Chin D.J., Gil G., Russell D.W., Liscum L., Luskey K.L., Basu S.K., Okayama H., Berg P., Goldstein J.L., Brown M.S.;
"Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum.";
Nature 308:613-617(1984).
[2]
GENE STRUCTURE.
DOI=10.1016/0092-8674(84)90549-X; PubMed=6088070 [NCBI, ExPASy, EBI, Israel, Japan]
Reynolds G.A., Basu S.K., Osborne T.F., Chin D.J., Gil G., Brown M.S., Goldstein J.L., Luskey K.L.;
"HMG CoA reductase: a negatively regulated gene with unusual promoter and 5' untranslated regions.";
Cell 38:275-285(1984).
[3]
DOMAINS.
PubMed=3965461 [NCBI, ExPASy, EBI, Israel, Japan]
Liscum L., Finer-Moore J., Stroud R.M., Luskey K.L., Brown M.S., Goldstein J.L.;
"Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum.";
J. Biol. Chem. 260:522-530(1985).
Comments
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
L00183; AAA36989.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00166; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00169; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00170; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00171; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00173; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00176; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00177; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00178; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00179; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00180; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00181; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00182; AAA36989.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00494; CAA25189.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A93328; RDHYE.
3D structure databases
HSSP P04035; 1HWJ. [HSSP ENTRY / PDB]
SMR P00347; 461-869.
ModBase P00347.
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 P00347.
Phylogenomic databases
HOVERGEN P00347; -.
Other
ProtoNet P00347.
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
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   887  887     3-hydroxy-3-methylglutaryl-coenzyme A reductase. PRO_0000114418
TRANSMEM   10    39  30      
TRANSMEM   57    78  22      
TRANSMEM   90   114  25      
TRANSMEM   124   149  26      
TRANSMEM   160   187  28      
TRANSMEM   192   220  29      
TRANSMEM   315   339  25      
REGION   340   449  110     Linker. 
REGION   450   887  438     Catalytic. 
ACT_SITE   558   558        Charge relay system (By similarity). 
ACT_SITE   690   690        Charge relay system (By similarity). 
ACT_SITE   766   766        Charge relay system (By similarity). 
ACT_SITE   865   865        Proton donor (By similarity). 
CARBOHYD   281   281        N-linked (GlcNAc...) (Potential). 
CARBOHYD   517   517        N-linked (GlcNAc...) (Potential). 
CARBOHYD   869   869        N-linked (GlcNAc...) (Potential). 
VARIANT   733   733  1     N -> C. 
Sequence information
Length: 887 AA [This is the length of the unprocessed precursor] Molecular weight: 97081 Da [This is the MW of the unprocessed precursor] CRC64: 4331E53ADA250E6A [This is a checksum on the sequence]
        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 NSTTEHSKVS LGLDEDVSKR 

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

       370        380        390        400        410        420 
PKKAPDNCCR REPLLVRRSE KLSSVEEEPG VSQDRKVEVI KPLVVETESA SRATFVLGAS 

       430        440        450        460        470        480 
GTSPPVAART QELEIELPSE PRPNEECLQI LESAEKGAKF LSDAEIIQLV NAKHIPAYKL 

       490        500        510        520        530        540 
ETLMETHERG VSIRRQLLST KLPEPSSLQY LPYRDYNYSL VMGACCENVI GYMPIPVGVA 

       550        560        570        580        590        600 
GPLCLDGKEY QVPMATTEGC LVASTNRGCR AIGLGGGASS RVLADGMTRG PVVRLPRACD 

       610        620        630        640        650        660 
SAEVKAWLET PEGFAVIKDA FDSTSRFARL QKLHVTMAGR NLYIRFQSKT GDAMGMNMIS 

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

       730        740        750        760        770        780 
KTTTEAMIDV 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 TCTKKSA 

P00347 in FASTA format

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View entry in raw text format (no links)
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