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   01-OCT-2014, entry version 63.
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). {ECO:0000250}.
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
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC       Polyprenol reductase subfamily. {ECO:0000305}.
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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   PhylomeDB; Q5RIU9; -.
DR   TreeFam; TF315011; -.
DR   Reactome; REACT_175194; Synthesis of Dolichyl-phosphate.
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. {ECO:0000255}.
FT   TRANSMEM      4     24       Helical. {ECO:0000255}.
FT   TOPO_DOM     25     67       Lumenal. {ECO:0000255}.
FT   TRANSMEM     68     88       Helical. {ECO:0000255}.
FT   TOPO_DOM     89    114       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    115    135       Helical. {ECO:0000255}.
FT   TOPO_DOM    136    150       Lumenal. {ECO:0000255}.
FT   TRANSMEM    151    171       Helical. {ECO:0000255}.
FT   TOPO_DOM    172    185       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    186    206       Helical. {ECO:0000255}.
FT   TOPO_DOM    207    255       Lumenal. {ECO:0000255}.
FT   TRANSMEM    256    276       Helical. {ECO:0000255}.
FT   TOPO_DOM    277    309       Cytoplasmic. {ECO:0000255}.
FT   CONFLICT     69     69       F -> S (in Ref. 2; AAI33965).
FT                                {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
//