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-OCT-2012, entry version 50.
DE   RecName: Full=Probable polyprenol reductase;
DE            EC=1.3.1.-;
DE   AltName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 3;
DE            EC=1.3.1.30;
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: 5-alpha-pregnan-3,20-dione + NADP(+) =
CC       progesterone + 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.
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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   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; EOG47D9H9; -.
DR   UniPathway; UPA00378; -.
DR   NextBio; 20883585; -.
DR   ArrayExpress; 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 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:0050213; F:progesterone 5-alpha-reductase activity; IEA: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   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       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
//