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Q5RIU9 (PORED_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Polyprenol reductase

EC=1.3.1.94
Alternative name(s):
3-oxo-5-alpha-steroid 4-dehydrogenase 3
EC=1.3.1.22
Steroid 5-alpha-reductase 3
Short name=S5AR 3
Short name=SR type 3
Gene names
Name:srd5a3
ORF Names:si:ch211-278f21.3
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. Also able to convert testosterone (T) into 5-alpha-dihydrotestosterone (DHT) By similarity.

Catalytic activity

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

A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta(4)-steroid + NADPH.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Polyprenol reductase
PRO_0000398651

Regions

Topological domain1 – 33Cytoplasmic Potential
Transmembrane4 – 2421Helical; Potential
Topological domain25 – 6743Lumenal Potential
Transmembrane68 – 8821Helical; Potential
Topological domain89 – 11426Cytoplasmic Potential
Transmembrane115 – 13521Helical; Potential
Topological domain136 – 15015Lumenal Potential
Transmembrane151 – 17121Helical; Potential
Topological domain172 – 18514Cytoplasmic Potential
Transmembrane186 – 20621Helical; Potential
Topological domain207 – 25549Lumenal Potential
Transmembrane256 – 27621Helical; Potential
Topological domain277 – 30933Cytoplasmic Potential

Experimental info

Sequence conflict691F → S in AAI33965. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q5RIU9 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 89513C21F5D7FEB6

FASTA30935,708
        10         20         30         40         50         60 
MFHILSIVNI IWLLLALCFG AAFCLNKFSV KLPNRVEHVF QDFIRYGKTK ENIKRASWQL 

        70         80         90        100        110        120 
VFDLSKRYFY HFYVVSVMWN GLLLLFSIRS VVMSEAFPDW IIDVLGSLTG RSRGAWNEIH 

       130        140        150        160        170        180 
LSTLLLQVLL WVHTLRRLLE CLFVSVFSDG VINVVQYAFG LSYYIILGLT VLCTNDSLPQ 

       190        200        210        220        230        240 
SESVSFFNQL TWYHVVGTLL FFWASFLQHQ SLSLLAKMRT DSSGKVETLA HKMPCGGWFE 

       250        260        270        280        290        300 
LVSCPHYLAE LLIYAAMCVC CGCASLTWWM VVLYVLCNQA LAAQLCHEYY RSKFKTYPHH 


RKAFIPFVL 

« Hide

References

[1]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX088688 Genomic DNA. Translation: CAI11971.1.
BC133964 mRNA. Translation: AAI33965.1.
RefSeqNP_001038404.1. NM_001044939.1.
UniGeneDr.81044.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000063577.

Proteomic databases

PRIDEQ5RIU9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000063578; ENSDARP00000063577; ENSDARG00000043307.
GeneID560717.
KEGGdre:560717.

Organism-specific databases

CTD79644.
ZFINZDB-GENE-030131-7915. srd5a3.

Phylogenomic databases

eggNOGNOG330066.
GeneTreeENSGT00500000044920.
HOGENOMHOG000018885.
HOVERGENHBG057797.
InParanoidA4FVI8.
KOK12345.
OMASSPHMFF.
OrthoDBEOG72ZCFT.
PhylomeDBQ5RIU9.
TreeFamTF315011.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ5RIU9.

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...

Other

NextBio20883585.
PROQ5RIU9.

Entry information

Entry namePORED_DANRE
AccessionPrimary (citable) accession number: Q5RIU9
Secondary accession number(s): A4FVI8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways