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Database: UniProt
Entry: A0A0K0DES8_ANGCA
LinkDB: A0A0K0DES8_ANGCA
Original site: A0A0K0DES8_ANGCA 
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
//
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