Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9SI62 (POED2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyprenol reductase 2

EC=1.3.1.94
Gene names
Ordered Locus Names:At2g16530
ORF Names:F1P15.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism By similarity.

Catalytic activity

Ditrans,polycis-dolichol + NADP+ = ditrans,polycis-polyprenol + NADPH.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.5.

Sequence similarities

Belongs to the steroid 5-alpha reductase family. Polyprenol reductase subfamily.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9SI62-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9SI62-2)

The sequence of this isoform differs from the canonical sequence as follows:
     58-58: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Polyprenol reductase 2
PRO_0000398656

Regions

Transmembrane12 – 3221Helical; Potential
Transmembrane66 – 8621Helical; Potential
Transmembrane164 – 18421Helical; Potential
Transmembrane223 – 24321Helical; Potential
Transmembrane266 – 28621Helical; Potential
Transmembrane291 – 31121Helical; Potential

Natural variations

Alternative sequence581Missing in isoform 2.
VSP_039793

Experimental info

Sequence conflict661F → L in BX819600. Ref.4
Sequence conflict691F → L in AAK96489. Ref.3
Sequence conflict691F → L in AAO11632. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 2.
Checksum: 49AB19FF40A9FA06

FASTA34338,678
        10         20         30         40         50         60 
MVELEIVWLV RGAWITVWIV SILPLVIASI PTSKLNSFRE LVLSFAGRGK ILHPSSQKFT 

        70         80         90        100        110        120 
IPQKCFAHFY VIGVVWTTLL LAATWMYACK MAPLSSEEFQ LSDIASRLAG GSDVFSVHKS 

       130        140        150        160        170        180 
NMTPVEHRFK VWRAVFLLLL MEIHVLRRLI ESFYVFKYSP SARMHILGYF AGLFFYVTAP 

       190        200        210        220        230        240 
LSLCSNIAPE VAGFVGNQVA EFIANGKSHT SAPEFNLLSS ISPLMKLGSL QWIGGAIFLW 

       250        260        270        280        290        300 
GWIHQRRCHA ILGSLRENPS QAKEYIIPYG DWFGMVSSPH FLAEIVLYAG LLIASGGTDI 

       310        320        330        340 
TIWLLFGFVA ANLTYAAGET HRWYLRKFEN YPANRHAIFP YVY 

« Hide

Isoform 2 [UniParc].

Checksum: 3510ED8C0A5AA451
Show »

FASTA34238,550

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[4]"Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
[5]"Mapping the Arabidopsis organelle proteome."
Dunkley T.P.J., Hester S., Shadforth I.P., Runions J., Weimar T., Hanton S.L., Griffin J.L., Bessant C., Brandizzi F., Hawes C., Watson R.B., Dupree P., Lilley K.S.
Proc. Natl. Acad. Sci. U.S.A. 103:6518-6523(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: cv. Columbia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC007195 Genomic DNA. Translation: AAD26491.2.
CP002685 Genomic DNA. Translation: AEC06507.1.
CP002685 Genomic DNA. Translation: AEC06508.1.
AY052296 mRNA. Translation: AAK96489.1.
BT002716 mRNA. Translation: AAO11632.1.
BX819600 mRNA. No translation available.
PIRD84541.
RefSeqNP_565389.1. NM_127207.3.
NP_973474.1. NM_201745.1.
UniGeneAt.14490.
At.48730.

3D structure databases

ProteinModelPortalQ9SI62.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G16530.1-P.

Proteomic databases

PaxDbQ9SI62.
PRIDEQ9SI62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G16530.1; AT2G16530.1; AT2G16530.
GeneID816152.
KEGGath:AT2G16530.

Organism-specific databases

TAIRAT2G16530.

Phylogenomic databases

eggNOGNOG330066.
HOGENOMHOG000240963.
InParanoidQ9SI62.
OMANQVAEFI.
PhylomeDBQ9SI62.
ProtClustDBPLN03164.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ9SI62.

Family and domain databases

InterProIPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOED2_ARATH
AccessionPrimary (citable) accession number: Q9SI62
Secondary accession number(s): Q3EBZ6, Q941B4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 1, 2002
Last modified: March 19, 2014
This is version 71 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names