ID A0A0K0DES8_ANGCA Unreviewed; 297 AA.
AC A0A0K0DES8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 28-JUN-2023, entry version 21.
DE RecName: Full=Polyprenol reductase {ECO:0000256|ARBA:ARBA00017362, ECO:0000256|RuleBase:RU367081};
DE EC=1.3.1.94 {ECO:0000256|ARBA:ARBA00012522, ECO:0000256|RuleBase:RU367081};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Metastrongyloidea; Angiostrongylidae; Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000940301-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0000940301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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. {ECO:0000256|RuleBase:RU367081}.
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:0000256|RuleBase:RU367081};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|RuleBase:RU367081}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367081}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC reductase subfamily. {ECO:0000256|ARBA:ARBA00008951,
CC ECO:0000256|RuleBase:RU367081}.
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DR AlphaFoldDB; A0A0K0DES8; -.
DR STRING; 6313.A0A0K0DES8; -.
DR WBParaSite; ACAC_0000940301-mRNA-1; ACAC_0000940301-mRNA-1; ACAC_0000940301.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000035642; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016095; P:polyprenol catabolic process; IEA:UniProtKB-UniRule.
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 {ECO:0000256|RuleBase:RU367081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367081};
KW NADP {ECO:0000256|RuleBase:RU367081};
KW Oxidoreductase {ECO:0000256|RuleBase:RU367081};
KW Reference proteome {ECO:0000313|Proteomes:UP000035642};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367081}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 137..154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 175..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 254..273
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT DOMAIN 186..263
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 297 AA; 34490 MW; 98849E9F30FEF8D9 CRC64;
MLPLLPSYLV VVTLGLSLAC TLTLFVPSCP SIVPALTTYG VSALYLRDKI KFIQVISVPK
RFVRSNYLSH LKRMDSLELN FIQQGLLQMV LAFLFGRVIL YNWSTTVLAL FLILFHVVRR
LWETLCISVY SDTTMNIFHY IVGLVHYIIL PLTIMCESQS FAEGKYSKSF SHRSLISAIS
PWQWFGTALF LICNREQHHI SRDIAALRRA PDGLVFNYCY GICYGGWFEY VSCPHFLFEI
GIYLSLWMVL WRAYAFRFLA IFVVVNQLFA GLITHRWYQR TFKAYPLNRR AVVPYIL
//