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UniProtKB/Swiss-Prot entry P20715


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

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Entry information
Entry name HMDH_XENLA
Primary accession number P20715
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on February 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 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
Xenopus laevis (African clawed frog) [TaxID: 8355] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2307680 [NCBI, ExPASy, EBI, Israel, Japan]
Chen H., Shapiro D.J.;
"Nucleotide sequence and estrogen induction of Xenopus laevis 3-hydroxy-3-methylglutaryl-coenzyme A reductase.";
J. Biol. Chem. 265:4622-4629(1990).
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
M29258; AAA49740.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A35728; A35728.
RefSeq NP_001081280.1; -.
UniGene Xl.800
3D structure databases
HSSP P04035; 1HWI. [HSSP ENTRY / PDB]
SMR P20715; 457-865.
ModBase P20715.
Organism-specific databases
Xenbase XB-FEAT-5840592; hmgcr.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from InterPro).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0004420; Molecular function: hydroxymethylglutaryl-CoA reductase (NADPH) activity (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006695; Biological process: cholesterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0015936; Biological process: coenzyme A metabolic process (inferred from electronic annotation from InterPro).
GO:0008299; Biological process: isoprenoid biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
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).
ProtoNet P20715.
Genome annotation databases
GeneID 397750; -.
KEGG xla:397750; -.
Phylogenomic databases
HOVERGEN P20715; -.
Other
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   883  883     3-hydroxy-3-methylglutaryl-coenzyme A reductase. PRO_0000114426
TRANSMEM   10    39  30     Potential. 
TRANSMEM   57    78  22     Potential. 
TRANSMEM   90   114  25     Potential. 
TRANSMEM   124   149  26     Potential. 
TRANSMEM   160   187  28     Potential. 
TRANSMEM   192   220  29     Potential. 
TRANSMEM   315   339  25     Potential. 
REGION   340   444  105     Linker. 
REGION   445   883  439     Catalytic. 
ACT_SITE   554   554        Charge relay system (By similarity). 
ACT_SITE   686   686        Charge relay system (By similarity). 
ACT_SITE   762   762        Charge relay system (By similarity). 
ACT_SITE   861   861        Proton donor (By similarity). 
CARBOHYD   282   282        N-linked (GlcNAc...) (Potential). 
CARBOHYD   513   513        N-linked (GlcNAc...) (Potential). 
CARBOHYD   865   865        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 883 AA [This is the length of the unprocessed precursor] Molecular weight: 96720 Da [This is the MW of the unprocessed precursor] CRC64: 53D6D1D9294A9A1F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLSRLFRMHG QFVASHPWEV IVGTVTLTIC MMSMNMFTGN DKICGWNYAC PKFEEDVLSS 

        70         80         90        100        110        120 
DIIILTITRC IAILYIYFQF QNLRQLGSKY ILGIAGLFTI FSSFVFSTVV IHFLDKELTG 

       130        140        150        160        170        180 
LNEALPFFLL LIDLSKASAL AKFALSSNSQ DEVRDNIARG MAILGPTFTL EALVECLVIG 

       190        200        210        220        230        240 
VGTMSGVRQL EIMCCFGCMS VLANYFAFMT FFPACVSLVL ELSRESREGR PIWQLSQFAS 

       250        260        270        280        290        300 
VLEEEEDNKP NPVTQRVKMI MSLGLVLVHA HSRWISEPSS QNSTSISDHE VTTMLDDMMP 

       310        320        330        340        350        360 
KRVEPSMPLW QFYLSRMVTM DVEQIITLGL ALLLAVKYIF FEQTETESTF SMKNPIISPV 

       370        380        390        400        410        420 
AVQKKQIESC CRREPEQEKT VHVSTTEEAS SKEETEAVIK PLPLETSPKA KFIVGDSSPL 

       430        440        450        460        470        480 
ELSPEDKNTM FDLPEEPRPL DECVRILKNP DKGAQYLTDA EVISLVNAKH IPAYKLETMM 

       490        500        510        520        530        540 
ESPREGVAIR RQMLSDKLPQ RSALQSLPYK NYNYSLVMGA CCENVIGYMP IPVGVAGPLL 

       550        560        570        580        590        600 
LNNKEYQVPM ATTEGCLVAS TNRGCRAIML GGGAKSRVLA DGMTRGPVVR LPTACDAAEV 

       610        620        630        640        650        660 
KAWLDSAEGF KVIKDAFDST SRFARLGRLQ NCVAGRNLYI RFQSKTGDAM GMNMISKVTE 

       670        680        690        700        710        720 
QALARLQEEF PDLHVLAVSG NYCTDKKPAA INWIEGRGKS VVCEAIIPAK VVREVLKSST 

       730        740        750        760        770        780 
EALVEVNINK NFIGSAMAGS IGGYNAHAAN IVTAIYIACG QDAAQNVGSS NCITIMEATG 

       790        800        810        820        830        840 
PTYEDLYISC TMPSIEIGTV GGGTNLAPQQ ACLQMLGVQG ASTETPGKNA CQLAQIVCST 

       850        860        870        880 
VMAGELSLMA ALAAGHLVKS HMVHNRSKIN LQDLPGTCTK KAA 

P20715 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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