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Protein

Polyprenol reductase

Gene

srd5a3

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism. Also able to convert testosterone (T) into 5-alpha-dihydrotestosterone (DHT) (By similarity).By similarity

Catalytic activityi

Ditrans,polycis-dolichol + NADP+ = ditrans,polycis-polyprenol + NADPH.
A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta4-steroid + NADPH.

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandNADP

Enzyme and pathway databases

UniPathwayiUPA00378

Names & Taxonomyi

Protein namesi
Recommended name:
Polyprenol reductase (EC:1.3.1.94)
Alternative name(s):
3-oxo-5-alpha-steroid 4-dehydrogenase 3 (EC:1.3.1.22)
Steroid 5-alpha-reductase 3
Short name:
S5AR 3
Short name:
SR type 3
Gene namesi
Name:srd5a3
OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifieri8364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
Proteomesi
  • UP000008143 Componenti: Unassembled WGS sequence

Organism-specific databases

XenbaseiXB-GENE-985511 srd5a3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 2CytoplasmicSequence analysis2
Transmembranei3 – 23HelicalSequence analysisAdd BLAST21
Topological domaini24 – 65LumenalSequence analysisAdd BLAST42
Transmembranei66 – 86HelicalSequence analysisAdd BLAST21
Topological domaini87 – 120CytoplasmicSequence analysisAdd BLAST34
Transmembranei121 – 141HelicalSequence analysisAdd BLAST21
Topological domaini142 – 148LumenalSequence analysis7
Transmembranei149 – 169HelicalSequence analysisAdd BLAST21
Topological domaini170 – 184CytoplasmicSequence analysisAdd BLAST15
Transmembranei185 – 205HelicalSequence analysisAdd BLAST21
Topological domaini206 – 255LumenalSequence analysisAdd BLAST50
Transmembranei256 – 276HelicalSequence analysisAdd BLAST21
Topological domaini277 – 308CytoplasmicSequence analysisAdd BLAST32

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003177061 – 308Polyprenol reductaseAdd BLAST308

Proteomic databases

PaxDbiQ0P4J9

Interactioni

Protein-protein interaction databases

STRINGi8364.ENSXETP00000045522

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1640 Eukaryota
ENOG4111JQM LUCA
HOVERGENiHBG057797
InParanoidiQ0P4J9
KOiK12345
OrthoDBiEOG091G0F09

Family and domain databases

InterProiView protein in InterPro
IPR001104 3-oxo-5_a-steroid_4-DH_C
PfamiView protein in Pfam
PF02544 Steroid_dh, 1 hit
PROSITEiView protein in PROSITE
PS50244 S5A_REDUCTASE, 1 hit

Sequencei

Sequence statusi: Complete.

Q0P4J9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLLALVWLL LDATFLITLL WHLLQGCKSG HSLLCSVFQD LIRYGKTKTG
60 70 80 90 100
LQRPAWLQWF DIPKRCFWHF YCVSLIWNGC LLWILLRLLL QSVPVPEWLQ
110 120 130 140 150
LVLHFLHAGS EPQILDRELS VILALALLWL HSLRRLLECL FVSVFSNGVI
160 170 180 190 200
HLVQYCFGLG YYFLIGITVL TYCPLDRRTV STDNLLTQCH WYHILGLALY
210 220 230 240 250
IWASLHQYRC HCILAGLRKS ASGNVINLNH SVPCGDWFER VSCPHYFAEL
260 270 280 290 300
LIYVSIAVVF GLLNTIWWLV VLYVLLNQAL AALLCHEFYH EKFDTYPIHR

KAFIPFIF
Length:308
Mass (Da):35,876
Last modified:September 19, 2006 - v1
Checksum:iFFE931DCDB0D558A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC122039 mRNA Translation: AAI22040.1
RefSeqiNP_001072539.1, NM_001079071.1
UniGeneiStr.24988

Genome annotation databases

GeneIDi779994
KEGGixtr:779994

Similar proteinsi

Entry informationi

Entry nameiPORED_XENTR
AccessioniPrimary (citable) accession number: Q0P4J9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 19, 2006
Last modified: April 25, 2018
This is version 66 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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