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Protein

Polyprenol reductase 1

Gene

OsI_17065

Organism
Oryza sativa subsp. indica (Rice)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Pathway:iprotein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyprenol reductase 1 (EC:1.3.1.94)
Gene namesi
ORF Names:OsI_17065
OrganismiOryza sativa subsp. indica (Rice)
Taxonomic identifieri39946 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
ProteomesiUP000007015 Componenti: Chromosome 4

Organism-specific databases

GrameneiA2XWN6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121HelicalSequence AnalysisAdd
BLAST
Transmembranei78 – 9821HelicalSequence AnalysisAdd
BLAST
Transmembranei141 – 15818HelicalSequence AnalysisAdd
BLAST
Transmembranei176 – 19621HelicalSequence AnalysisAdd
BLAST
Transmembranei235 – 25521HelicalSequence AnalysisAdd
BLAST
Transmembranei301 – 32121HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Polyprenol reductase 1PRO_0000398658Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi39946.BGIOSGA016966-PA.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi60 – 678Poly-Ser

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG330066.
HOGENOMiHOG000240963.
OMAiVLMQARW.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2XWN6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METEGWPALQ PLLCLAWIAT TLPIIVAALP IPAAAGGHLL RRLLSAFSSR
60 70 80 90 100
GKTVRPSPAS SSGSSSSKAK FTVPQKYFMH FYVVGVLATT ILLLAIWFYA
110 120 130 140 150
YMKMTPLLPE SSSYSTIASH LVGSNSFSFG RVHSRTMGHK YHVWRTVFVL
160 170 180 190 200
LLMEIQVLRR LYETEHVFHY SPSARMHIVG YLTGLFYYVA APLSLASSCI
210 220 230 240 250
PEAAEYLQGQ VAEFIVKGRA RMPDLVIDSS SLLQPLLKLG WTQWIGAVIF
260 270 280 290 300
IWGSLHQIRC HAILGTLREH KDSDEYVIPC GDWFNRVSCP HYLAELVIYF
310 320 330 340 350
GMLVASGGED IPVWFLFVFV ITNLSFAAVE THKWYLQKFE DYPRSRYAII

PFVC
Length:354
Mass (Da):39,867
Last modified:March 20, 2007 - v1
Checksum:iA307F4A8CA15DD38
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000129 Genomic DNA. Translation: EAY95246.1.

Genome annotation databases

EnsemblPlantsiBGIOSGA016966-TA; BGIOSGA016966-PA; BGIOSGA016966.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000129 Genomic DNA. Translation: EAY95246.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39946.BGIOSGA016966-PA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiBGIOSGA016966-TA; BGIOSGA016966-PA; BGIOSGA016966.

Organism-specific databases

GrameneiA2XWN6.

Phylogenomic databases

eggNOGiNOG330066.
HOGENOMiHOG000240963.
OMAiVLMQARW.

Enzyme and pathway databases

UniPathwayiUPA00378.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genomes of Oryza sativa: a history of duplications."
    Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.
    , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
    PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. 93-11.

Entry informationi

Entry nameiPOED1_ORYSI
AccessioniPrimary (citable) accession number: A2XWN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 20, 2007
Last modified: July 22, 2015
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.