PORED_CAEEL
ID PORED_CAEEL Reviewed; 309 AA.
AC Q17428; Q7JLP4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Polyprenol reductase;
DE EC=1.3.1.94;
GN ORFNames=B0024.13;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 (By similarity). {ECO:0000250}.
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 -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; Z71178; CAA94885.2; -; Genomic_DNA.
DR PIR; T18648; T18648.
DR RefSeq; NP_001256209.1; NM_001269280.1.
DR AlphaFoldDB; Q17428; -.
DR SMR; Q17428; -.
DR STRING; 6239.B0024.13; -.
DR EPD; Q17428; -.
DR PaxDb; Q17428; -.
DR PeptideAtlas; Q17428; -.
DR EnsemblMetazoa; B0024.13.1; B0024.13.1; WBGene00007102.
DR GeneID; 179438; -.
DR KEGG; cel:CELE_B0024.13; -.
DR UCSC; B0024.13a; c. elegans.
DR CTD; 179438; -.
DR WormBase; B0024.13; CE35376; WBGene00007102; -.
DR eggNOG; KOG1640; Eukaryota.
DR GeneTree; ENSGT00500000044920; -.
DR HOGENOM; CLU_044409_2_1_1; -.
DR InParanoid; Q17428; -.
DR OMA; KRWFRHF; -.
DR OrthoDB; 1574389at2759; -.
DR PhylomeDB; Q17428; -.
DR Reactome; R-CEL-193048; Androgen biosynthesis.
DR Reactome; R-CEL-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q17428; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00007102; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019408; P:dolichol biosynthetic process; IBA:GO_Central.
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 InterPro; IPR039698; Dfg10/SRD5A3.
DR PANTHER; PTHR14624; PTHR14624; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; NADP; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..309
FT /note="Polyprenol reductase"
FT /id="PRO_0000398653"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 309 AA; 35430 MW; 1D4F125A25B3A9EC CRC64;
MLDRLWEVRQ ALPLYLLVST LGLAISCCFT LICPHVCRLI PALTTYGKAA DQQEDNSLVE
KISVPKKWFK HFYAIGLLTL FICLHTVHSL IYNPNYLHPV VLKILATLTR SYSIPPITPS
TSILALLLIS LHVARRLYET IFVSVYSDSR MNLFHYAVGI VHYIILPISI MCETQGVASK
LPQLHVSIDD ISLTQWAGAV LFWICNWKQH QLAEQIANTR KGPRGLIRNY AYGICFGGWF
NLVSCPHFLF EICIYLSLFL VIPDAYVYRF IIMFVCINQT FAALITHSWY HKTFPKYPKS
RKALIPYVL
