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E2IUA6 (TARS_KALDA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length779 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxidosqualene cyclase that generates taraxerol, a triterpenoid product. Taraxerol is probably required to coat the leaf exterior as a defense compound against pathogens or herbivores. Ref.1

Catalytic activity

(3S)-2,3-epoxy-2,3-dihydrosqualene = taraxerol. Ref.1

Tissue specificity

Expressed only in the epidermal cells on both sides of the leaf and not in internal leaf tissues. Ref.1

Sequence similarities

Belongs to the terpene cyclase/mutase family.

Contains 2 PFTB repeats.

Ontologies

Keywords
   DomainRepeat
   Molecular functionIsomerase
Gene Ontology (GO)
   Biological_processtriterpenoid biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionintramolecular transferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 779779Taraxerol synthase
PRO_0000418480

Regions

Repeat167 – 20842PFTB 1
Repeat659 – 70042PFTB 2

Sequences

Sequence LengthMass (Da)Tools
E2IUA6 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 54BFFFCCDD7D7BD5

FASTA77989,734
        10         20         30         40         50         60 
MSFVWVEESK ECSEQRKGSM WKLKIAQGGK DPYLYSTNNY VGRQTWEFDP EAGTPEERAE 

        70         80         90        100        110        120 
VEAARLNFYN NRYRVKPSAD LLYRMQFLKE KNFKQTIPPV KVEDGEEITY ETATTALKRA 

       130        140        150        160        170        180 
VHFYSALQAS DGHWPAENSG PLFFLPPLVM CLYITGHLNT VFPAEHQREI LRYIYYHQNE 

       190        200        210        220        230        240 
DGGWGLHIEG HSTMFCTALS YICMRILGEG PDGGLDNAVA RGRKWILDHG TVTAMPSWGK 

       250        260        270        280        290        300 
TWLSIMGLFD WSGSNPMPPE FWLLPSFLPM YPAKMWCYCR MVYMPMSYLY GKRFVGPITP 

       310        320        330        340        350        360 
LILQLREELY DQPYEQVNWK QVRHECAKED IYYPHPKIQD LLWDTLYIAI EPLLTRWPFN 

       370        380        390        400        410        420 
KLVRERALQR TMKHIHYEDE NSRYITIGCV EKVLCMLACW VEDPNGDYFK KHLARVPDYI 

       430        440        450        460        470        480 
WVAEDGMKMQ SFGSQQWDTG FAIQALLASN MSDEIGETLA KGHDFVKKSQ VKDNPSGDFK 

       490        500        510        520        530        540 
SMHRHISKGS WTFSDQDHGW QVSDCTAEGL KCCLLFSLMP PELVGEKMEP ERLYDSVNIL 

       550        560        570        580        590        600 
LSLQSKNGGL AAWEPAGAPE WLELLNPTEF FADIVIEHEY VECTASAIQA LVLFKKLYPG 

       610        620        630        640        650        660 
HRKKDIETFI KGAAQYIEDR QMPDGSWYGS WGVCFTYGTW FALGGLAAAG KNYDNCAAIR 

       670        680        690        700        710        720 
KGTEFLLNTQ CENGGWGESY RSCPEKRYVP LEENKSNLVH TAWALMGLIH SRQAERDITP 

       730        740        750        760        770 
LHRAAKLLIN SQLENGDFPQ QEITGVFMKN CMQHYAAYRN IYPLWGIAEY RKQIPLPLR 

« Hide

References

[1]"Cloning and characterization of oxidosqualene cyclases from Kalanchoe daigremontiana: enzymes catalyzing up to 10 rearrangement steps yielding friedelin and other triterpenoids."
Wang Z., Yeats T., Han H., Jetter R.
J. Biol. Chem. 285:29703-29712(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HM623868 mRNA. Translation: ADK35123.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17976.

Family and domain databases

Gene3D1.50.10.20. 2 hits.
InterProIPR001330. Prenyltrans.
IPR018333. Squalene_cyclase.
IPR002365. Terpene_synthase_CS.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamPF00432. Prenyltrans. 1 hit.
[Graphical view]
SUPFAMSSF48239. SSF48239. 2 hits.
TIGRFAMsTIGR01787. squalene_cyclas. 1 hit.
PROSITEPS01074. TERPENE_SYNTHASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTARS_KALDA
AccessionPrimary (citable) accession number: E2IUA6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families