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E2IUB0 (CASS_KALDA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 12. 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 length764 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxidosqualene cyclase which catalyzes the conversion of oxidosqualene to cycloartenol. Ref.1

Catalytic activity

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

Subcellular location

Membrane; Single-pass membrane protein Potential.

Tissue specificity

Expressed in all leaf tissues. Ref.1

Sequence similarities

Belongs to the terpene cyclase/mutase family.

Contains 5 PFTB repeats.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Steroid biosynthesis
   Cellular componentMembrane
   DomainRepeat
Transmembrane
Transmembrane helix
   Molecular functionIsomerase
Gene Ontology (GO)
   Biological_processmetabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

steroid biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncycloartenol synthase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 764764Cycloartenol synthase
PRO_0000418479

Regions

Transmembrane609 – 62921Helical; Potential
Repeat148 – 18942PFTB 1
Repeat513 – 55846PFTB 2
Repeat590 – 63041PFTB 3
Repeat639 – 68042PFTB 4
Repeat701 – 74242PFTB 5

Sequences

Sequence LengthMass (Da)Tools
E2IUB0 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 9A59D94C1072CF6A

FASTA76486,531
        10         20         30         40         50         60 
MWKLKIADAG GSQWLRSVNN HIGRQIWDFD PALGSPEELA QIEDARDNFA RHRFDKKHSA 

        70         80         90        100        110        120 
DLLMRFQLTK ENPQSDLLPK VNIGKIEDIT EDAVTNTLRR AINFHSTTQA HDGHWPGDYG 

       130        140        150        160        170        180 
GPLFLMPGLV ITLSITGALN AVLSKEHKKE MCRYLYNHQN EDGGWGLHIE GPSTMFGSVL 

       190        200        210        220        230        240 
NYVTLRLLGE DVNGGDGEIE RARKWILDHG GATAITSWGK MWLSVLGVFE WCGNNPLPPE 

       250        260        270        280        290        300 
MWLFPYYLPV HPGRMWCHCR MVYLPMSYLY GKRFVGPITP TVLSLRKELF TVPYHEIDWN 

       310        320        330        340        350        360 
EARSLCAKED LYYPHPVVQD ILWATLHKVV EPVLLNWPGK KLREKALCSA IEHIHYEDEN 

       370        380        390        400        410        420 
TRYICIGPVN KVLNMLCCWV EDPNSEAFKL HIPRLYDYLW IAEDGMKMQG YNGSQLWDTA 

       430        440        450        460        470        480 
FSVQAIVATK LVEEFSSTIS KAHEFMKNSQ VLEDYPGDLS YWYRHISKGA WPFSTADHGW 

       490        500        510        520        530        540 
PISDCTAEGL KVVLKLSQFP AELVGAPLSA KLVYNAVNVI LSLQNIDGGF ATYELTRSYS 

       550        560        570        580        590        600 
WMELLNPAET FGDIVIDYPY VECTSAALQS LVLFKKLHPE HRKEEVELCI KKAAAFIEKI 

       610        620        630        640        650        660 
QESDGSWYGS WAVCFTYGTW FGVLGLVAAG RNYKNSPSIR KACDFLLSKQ LASGGWGESY 

       670        680        690        700        710        720 
LSCQNKVYTN IPGGRSHVVN TGWAMLALIG AGQAERDPVP LHRAAKFLIE SQLENGDFPQ 

       730        740        750        760 
QEIMGVFNKN CMISYAAYRN IFPIWALGEY RCKVLNASRG QMKT 

« 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
HM623872 mRNA. Translation: ADK35127.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. 3 hits.
[Graphical view]
SUPFAMSSF48239. SSF48239. 2 hits.
TIGRFAMsTIGR01787. squalene_cyclas. 1 hit.
PROSITEPS01074. TERPENE_SYNTHASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCASS_KALDA
AccessionPrimary (citable) accession number: E2IUB0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 12 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