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Database: UniProt
Entry: A0A3Q0T216_AMPCI
LinkDB: A0A3Q0T216_AMPCI
Original site: A0A3Q0T216_AMPCI 
ID   A0A3Q0T216_AMPCI        Unreviewed;       330 AA.
AC   A0A3Q0T216;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Polyprenol reductase {ECO:0000256|ARBA:ARBA00017362, ECO:0000256|RuleBase:RU367081};
DE            EC=1.3.1.22 {ECO:0000256|ARBA:ARBA00012049, ECO:0000256|RuleBase:RU367081};
DE            EC=1.3.1.94 {ECO:0000256|ARBA:ARBA00012522, ECO:0000256|RuleBase:RU367081};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000030123.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000030123.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Also able to convert testosterone (T) into 5-alpha-
CC       dihydrotestosterone (DHT). {ECO:0000256|RuleBase:RU367081}.
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=17beta-hydroxy-5alpha-androstan-3-one + NADP(+) = H(+) + NADPH
CC         + testosterone; Xref=Rhea:RHEA:50820, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16330, ChEBI:CHEBI:17347, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.3.1.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00023677};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822;
CC         Evidence={ECO:0000256|ARBA:ARBA00023677};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid +
CC         H(+) + NADPH; Xref=Rhea:RHEA:54384, ChEBI:CHEBI:13601,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:47909, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.3.1.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00033710};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54386;
CC         Evidence={ECO:0000256|ARBA:ARBA00033710};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=androst-4-ene-3,17-dione + H(+) + NADPH = 5alpha-
CC         androstan-3,17-dione + NADP(+); Xref=Rhea:RHEA:50816,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16422,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000256|ARBA:ARBA00023719};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50818;
CC         Evidence={ECO:0000256|ARBA:ARBA00023719};
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|ARBA:ARBA00033658};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34281;
CC         Evidence={ECO:0000256|ARBA:ARBA00033658};
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; A0A3Q0T216; -.
DR   STRING; 61819.ENSACIP00000030123; -.
DR   Ensembl; ENSACIT00000030913.1; ENSACIP00000030123.1; ENSACIG00000023307.1.
DR   GeneTree; ENSGT00500000044920; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000261340; Unplaced.
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:0047751; F:3-oxo-5alpha-steroid 4-dehydrogenase (NADP+); 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   Gene3D; 1.20.120.1630; -; 1.
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   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU367081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU367081}.
FT   TRANSMEM        76..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367081"
FT   TRANSMEM        132..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367081"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367081"
FT   TRANSMEM        216..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367081"
FT   TRANSMEM        272..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367081"
FT   DOMAIN          218..299
FT                   /note="Steroid 5-alpha reductase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50244"
SQ   SEQUENCE   330 AA;  38433 MW;  AA00F45E9C7FAE17 CRC64;
     MMWSSVDFSA INALWSFLAL FFLVAFCAYK ISPLLPRRFE ACRVYILFQD LIRYGKTKQS
     LKRDDWLRVF DIPKRWFWHF YAISVGWNGL LLVLYLNFII QHQAYPLWLT GMLDILTGVP
     GNDSQGRLKE NWVLLLSLVP QLSTVLVQLL LWVHSFRRLL ECLFVSVFSY GAMHLVQYMF
     GLGYYIMLGL TVLCCDRMEK GLKSSTLLTQ LDWRQIAGFV LFIWASLLQH QSMVLLARLR
     TGKSGAVETL AHRVPKGGLF ELVSCPHYFA ELLIYVSFSF VFRGLCLTWW LVVLYVLFNQ
     ALAGQLCHDL YISKYKSYPS HRRAFIPFVL
//
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