Q9SI62 (POED2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polyprenol reductase 2
EC=1.3.1.94

Gene names

Ordered Locus Names:	At2g16530
ORF Names:	F1P15.9

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid metabolic process Inferred from electronic annotation. Source: InterPro protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 22430844. Source: TAIR endoplasmic reticulum Inferred from direct assay Ref.5PubMed 22923678. Source: TAIR endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	oxidoreductase activity, acting on the CH-CH group of donors Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 343	343	Polyprenol reductase 2		PRO_0000398656
Regions
	Transmembrane	12 – 32	21	Helical; Potential
	Transmembrane	66 – 86	21	Helical; Potential
	Transmembrane	164 – 184	21	Helical; Potential
	Transmembrane	223 – 243	21	Helical; Potential
	Transmembrane	266 – 286	21	Helical; Potential
	Transmembrane	291 – 311	21	Helical; Potential
Natural variations
	Alternative sequence	58	1	Missing in isoform 2.		VSP_039793
Experimental info
	Sequence conflict	66	1	F → L in BX819600. Ref.4
	Sequence conflict	69	1	F → L in AAK96489. Ref.3
	Sequence conflict	69	1	F → L in AAO11632. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2002. Version 2. Checksum: 49AB19FF40A9FA06	FASTA	343	38,678
	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
	Isoform 2 [UniParc]. Checksum: 3510ED8C0A5AA451	FASTA	342	38,550
	10 20 30 40 50 60 MVELEIVWLV RGAWITVWIV SILPLVIASI PTSKLNSFRE LVLSFAGRGK ILHPSSQFTI 70 80 90 100 110 120 PQKCFAHFYV IGVVWTTLLL AATWMYACKM APLSSEEFQL SDIASRLAGG SDVFSVHKSN 130 140 150 160 170 180 MTPVEHRFKV WRAVFLLLLM EIHVLRRLIE SFYVFKYSPS ARMHILGYFA GLFFYVTAPL 190 200 210 220 230 240 SLCSNIAPEV AGFVGNQVAE FIANGKSHTS APEFNLLSSI SPLMKLGSLQ WIGGAIFLWG 250 260 270 280 290 300 WIHQRRCHAI LGSLRENPSQ AKEYIIPYGD WFGMVSSPHF LAEIVLYAGL LIASGGTDIT 310 320 330 340 IWLLFGFVAA NLTYAAGETH RWYLRKFENY PANRHAIFPY VY

References

	« Hide 'large scale' referencesShow '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. , 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. , 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: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

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.
IPI	IPI00526644. IPI00530393.
PIR	D84541.
RefSeq	NP_565389.1. NM_127207.3. NP_973474.1. NM_201745.1.
UniGene	At.14490. At.48730.
3D structure databases
ProteinModelPortal	Q9SI62.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT2G16530.1-P.
Proteomic databases
PaxDb	Q9SI62.
PRIDE	Q9SI62.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G16530.1; AT2G16530.1; AT2G16530.
GeneID	816152.
KEGG	ath:AT2G16530.
Organism-specific databases
TAIR	At2g16530.
Phylogenomic databases
eggNOG	NOG330066.
HOGENOM	HOG000240963.
InParanoid	Q9SI62.
OMA	THKWYLQ.
PhylomeDB	Q9SI62.
ProtClustDB	PLN03164.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Genevestigator	Q9SI62.
Family and domain databases
InterPro	IPR001104. 3-oxo-5_a-steroid_4-DH_C. [Graphical view]
Pfam	PF02544. Steroid_dh. 1 hit. [Graphical view]
PROSITE	PS50244. S5A_REDUCTASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POED2_ARATH

Accession

Primary (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:	May 1, 2013
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program