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 16-NOV-2011, entry version 43. DE RecName: Full=Probable polyprenol reductase; DE EC=1.3.1.-; DE AltName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 3; DE EC=1.3.99.5; 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; RG The Danio rerio sequencing project at the Sanger Institute; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. 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: Probable polyprenol reductase. Plays a key role in early CC steps of protein N-linked glycosylation by being required for the CC conversion of polyprenol into dolichol. Dolichols are required for CC the synthesis of dolichol-linked monosaccharides and the CC oligosaccharide precursor used for N-glycosylation. Probably acts CC as a polyprenol reductase that promotes the reduction of the CC alpha-isoprene unit of polyprenols into dolichols in a NADP- CC dependent mechanism. Also able to convert testosterone (T) into 5- CC alpha-dihydrotestosterone (DHT) (By similarity). CC -!- CATALYTIC ACTIVITY: A 3-oxo-5-alpha-steroid + acceptor = a 3-oxo- CC Delta(4)-steroid + reduced acceptor. 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 IPI; IPI00516108; -. DR RefSeq; NP_001038404.1; NM_001044939.1. DR UniGene; Dr.81044; -. DR STRING; Q5RIU9; -. 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 GeneTree; ENSGT00500000044920; -. DR HOVERGEN; HBG057797; -. DR InParanoid; Q5RIU9; -. DR OMA; EVPKSWF; -. DR PhylomeDB; Q5RIU9; -. DR ArrayExpress; Q5RIU9; -. DR Bgee; Q5RIU9; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; ISS:UniProtKB. 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 InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C. DR KO; K12345; -. 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 Probable 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 //