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UniProtKB/Swiss-Prot entry P43256


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

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Entry information
Entry name HMDH2_ARATH
Primary accession number P43256
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 73)
Name and origin of the protein
Protein name 3-hydroxy-3-methylglutaryl-coenzyme A reductase 2
Synonyms HMG-CoA reductase 2
HMGR2
EC 1.1.1.34
Gene name
Name: HMG2
OrderedLocusNames: At2g17370
ORFNames: F5J6.24
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=8302869 [NCBI, ExPASy, EBI, Israel, Japan]
Enjuto M., Balcells L., Campos N., Caelles C., Arro M., Boronat A.;
"Arabidopsis thaliana contains two differentially expressed 3-hydroxy-3-methylglutaryl-CoA reductase genes, which encode microsomal forms of the enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 91:927-931(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/45471; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan]
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
Nature 402:761-768(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
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
L19262; AAA67317.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC002329; AAB86514.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY057680; AAL15311.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY143930; AAN28869.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D84551; D84551.
RefSeq NP_179329.1; -.
UniGene At.432
3D structure databases
HSSP P04035; 1DQA. [HSSP ENTRY / PDB]
ModBase P43256.
Organism-specific databases
TAIR At2g17370; -.
Gene expression databases
ArrayExpress P43256; -.
GermOnline AT2G17370; Arabidopsis thaliana.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR002202; HMG_CoA_Rdtase_cat.
IPR004554; HMG_CoA_Rdtase_I_cat.
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.
PROSITE graphical view of domain structure (profiles).
BLOCKS P43256.
Genome annotation databases
GeneID 816244; -.
GenomeReviews CT485783_GR; AT2G17370.
KEGG ath:AT2G17370; -.
NMPDR fig|3702.1.peg.8729; -.
Other
ProtoNet P43256.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Endoplasmic reticulum; Glycoprotein; Isoprene biosynthesis; Membrane; NADP; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   562  562     3-hydroxy-3-methylglutaryl-coenzyme A reductase 2. PRO_0000114434
TRANSMEM   32    56  25     Potential. 
TRANSMEM   77   100  24     Potential. 
REGION   101   146  46     Linker (By similarity). 
REGION   147   562  416     Catalytic (By similarity). 
ACT_SITE   240   240        Charge relay system (By similarity). 
ACT_SITE   372   372        Charge relay system (By similarity). 
ACT_SITE   448   448        Charge relay system (By similarity). 
ACT_SITE   544   544        Proton donor (By similarity). 
CARBOHYD   118   118        N-linked (GlcNAc...) (Potential). 
CARBOHYD   304   304        N-linked (GlcNAc...) (Potential). 
CARBOHYD   548   548        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 562 AA [This is the length of the unprocessed precursor] Molecular weight: 60715 Da [This is the MW of the unprocessed precursor] CRC64: A4BF6BE6796C940A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEDLRRRFPT KKNGEEISNV AVDPPLRKAS DALPLPLYLT NTFFLSLFFA TVYFLLSRWR 

        70         80         90        100        110        120 
EKIRNSTPLH VVDLSEICAL IGFVASFIYL LGFCGIDLIF RSSSDDDVWV NDGMIPCNQS 

       130        140        150        160        170        180 
LDCREVLPIK PNSVDPPRES ELDSVEDEEI VKLVIDGTIP SYSLETKLGD CKRAAAIRRE 

       190        200        210        220        230        240 
AVQRITGKSL TGLPLEGFDY NSILGQCCEM PVGYVQIPVG IAGPLLLDGV EYSVPMATTE 

       250        260        270        280        290        300 
GCLVASTNRG FKAIHLSGGA FSVLVKDAMT RAPVVRFPSA RRAALVMFYL QDPSNFERLS 

       310        320        330        340        350        360 
LIFNKSSRFA RLQSITCTIA GRNLYPRFAC STGDAMGMNM VSKGVQNVLD FVKSEFPDMD 

       370        380        390        400        410        420 
VIGISGNYCS DKKASAVNWI EGRGKHVVCE AFIKAEIVEK VLKTSVEALV ELNTLKNLVG 

       430        440        450        460        470        480 
SAMAGSLGGF NAHSSNIVSA VFIATGQDPA QNVESSHCMT MILPDGDDLH ISVSMPCIEV 

       490        500        510        520        530        540 
GTVGGGTQLA SQAACLNLLG VKGSNNEKPG SNAQQLARIV AGSVLAGELS LMSAIAAGQL 

       550        560 
VKSHMKYNRS SRDIGPSSQV NR 

P43256 in FASTA format

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