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Reviewed, UniProtKB/Swiss-Prot O48962 (EBP_ARATH)

Last modified November 3, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
    EC=5.3.3.5
Alternative name(s):
    Cholestenol Delta-isomerase
    Delta(8)-Delta(7) sterol isomerase
      Short name=D8-D7 sterol isomerase
Gene names
Ordered Locus Names: At1g20050
ORF Names: T20H2.18
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers By similarity.

Catalytic activity

5-alpha-cholest-7-en-3-beta-ol = 5-alpha-cholest-8-en-3-beta-ol.

Pathway

Steroid biosynthesis; sterol biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the EBP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 223223Probable 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
PRO_0000174345

Regions

Transmembrane28 – 4821 Potential
Transmembrane58 – 7821 Potential
Transmembrane115 – 13521 Potential
Transmembrane175 – 19521 Potential

Experimental info

Sequence conflict1571L → V in AAD04752. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O48962-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 8060845768EEBACC

FASTA22325,146
        10         20         30         40         50         60 
MEELAHPYVP RDLNLPGYVP ISMSMSSIVS IYLGSSLLVV SLVWLLFGRK KAKLDKLLMC 

        70         80         90        100        110        120 
WWTFTGLTHV ILEGYFVFSP EFFKDNTSAY LAEVWKEYSK GDSRYVGRDS AVVSVEGITA 

       130        140        150        160        170        180 
VIVGPASLLA IYAIAKEKSY SYVLQLAISV CQLYGCLVYF ITAILEGDNF ATNSFYYYSY 

       190        200        210        220 
YIGANCWWVL IPSLISFRCW KKICAAAAIA NNNVETKTKK KTR 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of an Arabidopsis thaliana C-8,7 sterol isomerase: functional and structural similarities to mammalian C-8,7 sterol isomerase/emopamil-binding protein."
Grebenok R.J., Ohnmeiss T.E., Yamamoto A., Huntley E.D., Galbraith D.W., Della Penna D.
Plant Mol. Biol. 38:807-815(1998) [PubMed: 9862498] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Benveniste P.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[3]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF030357 mRNA. Translation: AAD03489.1.
U81498 mRNA. Translation: AAD04752.1.
AC022472 Genomic DNA. Translation: AAF79909.1.
AF334733 mRNA. Translation: AAG50111.1.
IPIIPI00543529.
PIRT51727.
RefSeqNP_173433.1.
UniGeneAt.10970
At.71675

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO48962.

Proteomic databases

PRIDEO48962.

Genome annotation databases

GeneID838593.
GenomeReviewsGene locus AT1G20050 in contig CT485782_GR.
KEGGath:AT1G20050.

Organism-specific databases

TAIRAt1g20050.

Phylogenomic databases

OMALEGYFVF.

Enzyme and pathway databases

BioCycMetaCyc:AT1G20050-MON.
BRENDA5.3.3.5. 302.

Gene expression databases

ArrayExpressO48962.
GenevestigatorO48962.
GermOnlineAT1G20050. Arabidopsis thaliana.

Family and domain databases

InterProIPR007905. EBP.
[Graphical view]
PANTHERPTHR14207. EBP. 1 hit.
PfamPF05241. EBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEBP_ARATH
AccessionPrimary (citable) accession number: O48962
Secondary accession number(s): Q9SAQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: June 1, 1998
Last modified: November 3, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents