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PORED_XENLA
ID   PORED_XENLA             Reviewed;         319 AA.
AC   Q8AVI9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Polyprenol reductase;
DE            EC=1.3.1.94 {ECO:0000250|UniProtKB:Q9H8P0};
DE   AltName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 3;
DE            EC=1.3.1.22 {ECO:0000250|UniProtKB:Q9H8P0};
DE   AltName: Full=Steroid 5-alpha-reductase 3;
DE            Short=S5AR 3;
DE            Short=SR type 3;
GN   Name=srd5a3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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. Also able to convert testosterone (T) into 5-
CC       alpha-dihydrotestosterone (DHT). {ECO:0000250|UniProtKB:Q9H8P0}.
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:0000250|UniProtKB:Q9H8P0};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34281;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
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:0000250|UniProtKB:Q9H8P0};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54386;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=androst-4-ene-3,17-dione + H(+) + NADPH = 5alpha-androstan-
CC         3,17-dione + NADP(+); Xref=Rhea:RHEA:50816, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15994, ChEBI:CHEBI:16422, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50818;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
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:0000250|UniProtKB:Q9H8P0};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9H8P0}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9H8P0}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9H8P0}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; BC042255; AAH42255.1; -; mRNA.
DR   RefSeq; NP_001079436.1; NM_001085967.1.
DR   AlphaFoldDB; Q8AVI9; -.
DR   DNASU; 379123; -.
DR   GeneID; 379123; -.
DR   KEGG; xla:379123; -.
DR   CTD; 379123; -.
DR   Xenbase; XB-GENE-985517; srd5a3.S.
DR   OrthoDB; 1574389at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 379123; Expressed in oocyte and 19 other tissues.
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 component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC.
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:0102389; F:polyprenol reductase activity; IEA:UniProtKB-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   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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..319
FT                   /note="Polyprenol reductase"
FT                   /id="PRO_0000317705"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..79
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..122
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..158
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..195
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        217..266
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..319
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   319 AA;  36591 MW;  5163DCD07643B1DB CRC64;
     MQLVQLLPPG VSLLALVWLA VDAAFLTALL LYLQRGCDSG RSLLCSVFQD LIRYGKTKSG
     LRRPSWLQWF DIPKRCFWHF YFVSLVWNGF LLWILLHLLL QSVPVPEWLQ AVLQFLCAGS
     EPQVLGGELS VVLAFSLLWL HSLRRLLECL FVSIFSNGVI HFVQYCFGLG YYILIGFTIL
     GYCPLDRRTA VSLDDLLMQG NWYHILGLTL YVWASLHQYT CHCILADLRK SASGAIINLK
     HAVPTGDWFE KVSCPHYFAE LLIYLSIAVV FGLLNTIWWL VVLYVLLSQA LAAVLCHEFY
     HEKFDSYPIH RKAFIPLIF
 
 
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