ID PORED_AILME Reviewed; 318 AA. AC D2HBV9; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 09-FEB-2010, sequence version 1. DT 24-JAN-2024, entry version 51. 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 {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=PANDA_008038; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda. OX NCBI_TaxID=9646; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B., RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J., RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A., RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B., RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W., RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M., RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G., RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C., RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D., RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W., RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J., RA Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). 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- CC androstan-3,17-dione + NADP(+); Xref=Rhea:RHEA:50816, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16422, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC 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; GL192668; EFB15787.1; -; Genomic_DNA. DR RefSeq; XP_002919412.1; XM_002919366.3. DR AlphaFoldDB; D2HBV9; -. DR SMR; D2HBV9; -. DR STRING; 9646.ENSAMEP00000019466; -. DR Ensembl; ENSAMET00000035187.1; ENSAMEP00000036180.1; ENSAMEG00000031461.1. DR GeneID; 100463734; -. DR KEGG; aml:100463734; -. DR CTD; 79644; -. DR eggNOG; KOG1640; Eukaryota. DR GeneTree; ENSGT00500000044920; -. DR HOGENOM; CLU_044409_2_1_1; -. DR InParanoid; D2HBV9; -. DR OrthoDB; 2896758at2759; -. DR UniPathway; UPA00378; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IEA:InterPro. DR GO; GO:0047751; F:3-oxo-5alpha-steroid 4-dehydrogenase (NADP+); 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:0102389; F:polyprenol reductase activity; IEA:UniProtKB-EC. 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 Gene3D; 1.20.120.1630; -; 1. DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C. DR InterPro; IPR039698; Dfg10/SRD5A3. DR PANTHER; PTHR14624; DFG10 PROTEIN; 1. DR PANTHER; PTHR14624:SF0; POLYPRENOL REDUCTASE; 1. DR Pfam; PF02544; Steroid_dh; 1. DR PROSITE; PS50244; S5A_REDUCTASE; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum; Lipid metabolism; Membrane; NADP; Oxidoreductase; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..318 FT /note="Polyprenol reductase" FT /id="PRO_0000398648" FT TOPO_DOM 1..19 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 20..40 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 41..80 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 81..101 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 102..119 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 120..140 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 141..156 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 157..177 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 178..194 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 195..215 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 216..265 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 266..286 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 287..318 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" SQ SEQUENCE 318 AA; 36775 MW; B0CD88A5D8E2667D CRC64; MAPWAAAQLW ALNPLRALWL TLAAAFLLTL LLQLVPPGLL PGCALFQDLI RYGKTKREGQ SRPAVCRVFD VPKRYFSHFY IISALWNGFL LWHLTQSVFL GVPFPNWLHG LLRILGASQF QGGELALSAF LVLVFLWLHS LRRLFECFYV SVFSNTVIHI VQYCFGLVYY VLTGLTVLSQ VPMDGRNAYV IGKNLLMQAR WFHILGMLMF IWSSVHQYKC HVILGNLRKN KAGVVIHCNH RIPFGDWFEY VSSPNYLAEL MIYISMAVTF GFHNLTWWLV VTYVFFSQAL SAFLSHKFYK SKFVSYPKHR KAFLPFLF //