ID PORED_DANRE Reviewed; 309 AA. AC Q5RIU9; A4FVI8; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 03-AUG-2022, entry version 93. DE RecName: Full=Polyprenol reductase; DE EC=1.3.1.94 {ECO:0000250|UniProtKB:Q9H8P0}; DE AltName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 3; DE EC=1.3.1.22 {ECO:0000250|UniProtKB:Q9H8P0}; DE AltName: Full=Steroid 5-alpha-reductase 3; DE Short=S5AR 3; DE Short=SR type 3; GN Name=srd5a3; ORFNames=si:ch211-278f21.3; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays a key role in early steps of protein N-linked CC glycosylation by being required for the conversion of polyprenol into CC dolichol. Dolichols are required for the synthesis of dolichol-linked CC monosaccharides and the oligosaccharide precursor used for N- CC glycosylation. Acts as a polyprenol reductase that promotes the CC reduction of the alpha-isoprene unit of polyprenols into dolichols in a CC NADP-dependent mechanism. Also able to convert testosterone (T) into 5- CC alpha-dihydrotestosterone (DHT). {ECO:0000250|UniProtKB:Q9H8P0}. CC -!- CATALYTIC ACTIVITY: CC Reaction=di-trans,poly-cis-dolichol + NADP(+) = di-trans,cis-polyprenol CC + H(+) + NADPH; Xref=Rhea:RHEA:34279, Rhea:RHEA-COMP:9521, Rhea:RHEA- CC COMP:9525, ChEBI:CHEBI:15378, ChEBI:CHEBI:16091, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:67132; EC=1.3.1.94; CC Evidence={ECO:0000250|UniProtKB:Q9H8P0}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34281; CC Evidence={ECO:0000250|UniProtKB:Q9H8P0}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid + CC H(+) + NADPH; Xref=Rhea:RHEA:54384, ChEBI:CHEBI:13601, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:47909, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.3.1.22; CC Evidence={ECO:0000250|UniProtKB:Q9H8P0}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54386; CC Evidence={ECO:0000250|UniProtKB:Q9H8P0}; CC -!- CATALYTIC ACTIVITY: CC Reaction=androst-4-ene-3,17-dione + H(+) + NADPH = 5alpha-androstan- CC 3,17-dione + NADP(+); Xref=Rhea:RHEA:50816, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15994, ChEBI:CHEBI:16422, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:Q9H8P0}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50818; CC Evidence={ECO:0000250|UniProtKB:Q9H8P0}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17beta-hydroxy-5alpha-androstan-3-one + NADP(+) = H(+) + NADPH CC + testosterone; Xref=Rhea:RHEA:50820, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16330, ChEBI:CHEBI:17347, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.3.1.22; CC Evidence={ECO:0000250|UniProtKB:Q9H8P0}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822; CC Evidence={ECO:0000250|UniProtKB:Q9H8P0}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000250|UniProtKB:Q9H8P0}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q9H8P0}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q9H8P0}. CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol CC reductase subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX088688; CAI11971.1; -; Genomic_DNA. DR EMBL; BC133964; AAI33965.1; -; mRNA. DR RefSeq; NP_001038404.1; NM_001044939.1. DR AlphaFoldDB; Q5RIU9; -. DR SMR; Q5RIU9; -. DR STRING; 7955.ENSDARP00000063577; -. DR PaxDb; Q5RIU9; -. DR Ensembl; ENSDART00000063578; ENSDARP00000063577; ENSDARG00000043307. DR GeneID; 560717; -. DR KEGG; dre:560717; -. DR CTD; 79644; -. DR ZFIN; ZDB-GENE-030131-7915; srd5a3. DR eggNOG; KOG1640; Eukaryota. DR GeneTree; ENSGT00500000044920; -. DR HOGENOM; CLU_044409_2_1_1; -. DR InParanoid; Q5RIU9; -. DR OMA; SSPHMFF; -. DR OrthoDB; 1574389at2759; -. DR PhylomeDB; Q5RIU9; -. DR TreeFam; TF315011; -. DR Reactome; R-DRE-193048; Androgen biosynthesis. DR Reactome; R-DRE-446199; Synthesis of Dolichyl-phosphate. DR UniPathway; UPA00378; -. DR PRO; PR:Q5RIU9; -. DR Proteomes; UP000000437; Genome assembly. DR Proteomes; UP000814640; Chromosome 20. DR Bgee; ENSDARG00000043307; Expressed in ovary and 28 other tissues. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC. DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISS:UniProtKB. DR GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-EC. DR GO; GO:0019408; P:dolichol biosynthetic process; IBA:GO_Central. DR GO; GO:0019348; P:dolichol metabolic process; ISS:UniProtKB. DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB. DR GO; GO:0016095; P:polyprenol catabolic process; ISS:UniProtKB. DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C. DR InterPro; IPR039698; Dfg10/SRD5A3. DR PANTHER; PTHR14624; PTHR14624; 1. DR Pfam; PF02544; Steroid_dh; 1. DR PROSITE; PS50244; S5A_REDUCTASE; 1. PE 2: Evidence at transcript level; KW Endoplasmic reticulum; Lipid metabolism; Membrane; NADP; Oxidoreductase; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..309 FT /note="Polyprenol reductase" FT /id="PRO_0000398651" FT TOPO_DOM 1..3 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 4..24 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 25..67 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 68..88 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 89..114 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 115..135 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 136..150 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 151..171 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 172..185 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 186..206 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 207..255 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 256..276 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 277..309 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CONFLICT 69 FT /note="F -> S (in Ref. 2; AAI33965)" FT /evidence="ECO:0000305" SQ SEQUENCE 309 AA; 35708 MW; 89513C21F5D7FEB6 CRC64; MFHILSIVNI IWLLLALCFG AAFCLNKFSV KLPNRVEHVF QDFIRYGKTK ENIKRASWQL VFDLSKRYFY HFYVVSVMWN GLLLLFSIRS VVMSEAFPDW IIDVLGSLTG RSRGAWNEIH LSTLLLQVLL WVHTLRRLLE CLFVSVFSDG VINVVQYAFG LSYYIILGLT VLCTNDSLPQ SESVSFFNQL TWYHVVGTLL FFWASFLQHQ SLSLLAKMRT DSSGKVETLA HKMPCGGWFE LVSCPHYLAE LLIYAAMCVC CGCASLTWWM VVLYVLCNQA LAAQLCHEYY RSKFKTYPHH RKAFIPFVL //