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 19-FEB-2014, entry version 60. DE RecName: Full=Polyprenol reductase; DE EC=1.3.1.94; DE AltName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 3; DE EC=1.3.1.22; 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 Cyprinidae; 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., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA 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., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA 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., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human 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 CC into dolichol. Dolichols are required for the synthesis of CC dolichol-linked monosaccharides and the oligosaccharide precursor CC used for N-glycosylation. Acts as a polyprenol reductase that CC promotes the reduction of the alpha-isoprene unit of polyprenols CC into dolichols in a NADP-dependent mechanism. Also able to convert CC testosterone (T) into 5-alpha-dihydrotestosterone (DHT) (By CC similarity). CC -!- CATALYTIC ACTIVITY: Ditrans,polycis-dolichol + NADP(+) = CC ditrans,polycis-polyprenol + NADPH. CC -!- CATALYTIC ACTIVITY: A 3-oxo-5-alpha-steroid + NADP(+) = a 3-oxo- CC Delta(4)-steroid + NADPH. CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. CC Polyprenol reductase subfamily. 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 UniGene; Dr.81044; -. DR STRING; 7955.ENSDARP00000063577; -. DR PRIDE; 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; NOG330066; -. DR GeneTree; ENSGT00500000044920; -. DR HOGENOM; HOG000018885; -. DR HOVERGEN; HBG057797; -. DR InParanoid; A4FVI8; -. DR KO; K12345; -. DR OMA; SSPHMFF; -. DR OrthoDB; EOG72ZCFT; -. DR TreeFam; TF315011; -. DR UniPathway; UPA00378; -. DR NextBio; 20883585; -. DR PRO; PR:Q5RIU9; -. DR Bgee; Q5RIU9; -. 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: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 GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway. DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C. DR Pfam; PF02544; Steroid_dh; 1. DR PROSITE; PS50244; S5A_REDUCTASE; 1. PE 2: Evidence at transcript level; KW Complete proteome; Endoplasmic reticulum; Membrane; NADP; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 309 Polyprenol reductase. FT /FTId=PRO_0000398651. FT TOPO_DOM 1 3 Cytoplasmic (Potential). FT TRANSMEM 4 24 Helical; (Potential). FT TOPO_DOM 25 67 Lumenal (Potential). FT TRANSMEM 68 88 Helical; (Potential). FT TOPO_DOM 89 114 Cytoplasmic (Potential). FT TRANSMEM 115 135 Helical; (Potential). FT TOPO_DOM 136 150 Lumenal (Potential). FT TRANSMEM 151 171 Helical; (Potential). FT TOPO_DOM 172 185 Cytoplasmic (Potential). FT TRANSMEM 186 206 Helical; (Potential). FT TOPO_DOM 207 255 Lumenal (Potential). FT TRANSMEM 256 276 Helical; (Potential). FT TOPO_DOM 277 309 Cytoplasmic (Potential). FT CONFLICT 69 69 F -> S (in Ref. 2; AAI33965). 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 //