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Protein

Polyprenol reductase

Gene

SRD5A3

Organism
Ailuropoda melanoleuca (Giant panda)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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-Delta(4)-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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

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
ORF Names:PANDA_008038
OrganismiAiluropoda melanoleuca (Giant panda)
Taxonomic identifieri9646 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaUrsidaeAiluropoda
Proteomesi
  • UP000008912 Componenti: Unassembled WGS sequence

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 19CytoplasmicSequence analysisAdd BLAST19
Transmembranei20 – 40HelicalSequence analysisAdd BLAST21
Topological domaini41 – 80LumenalSequence analysisAdd BLAST40
Transmembranei81 – 101HelicalSequence analysisAdd BLAST21
Topological domaini102 – 119CytoplasmicSequence analysisAdd BLAST18
Transmembranei120 – 140HelicalSequence analysisAdd BLAST21
Topological domaini141 – 156LumenalSequence analysisAdd BLAST16
Transmembranei157 – 177HelicalSequence analysisAdd BLAST21
Topological domaini178 – 194CytoplasmicSequence analysisAdd BLAST17
Transmembranei195 – 215HelicalSequence analysisAdd BLAST21
Topological domaini216 – 265LumenalSequence analysisAdd BLAST50
Transmembranei266 – 286HelicalSequence analysisAdd BLAST21
Topological domaini287 – 318CytoplasmicSequence analysisAdd BLAST32

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003986481 – 318Polyprenol reductaseAdd BLAST318

Interactioni

Protein-protein interaction databases

STRINGi9646.ENSAMEP00000019466.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1640. Eukaryota.
ENOG4111JQM. LUCA.
HOGENOMiHOG000018885.
InParanoidiD2HBV9.
KOiK12345.
OrthoDBiEOG091G0F09.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D2HBV9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPWAAAQLW ALNPLRALWL TLAAAFLLTL LLQLVPPGLL PGCALFQDLI
60 70 80 90 100
RYGKTKREGQ SRPAVCRVFD VPKRYFSHFY IISALWNGFL LWHLTQSVFL
110 120 130 140 150
GVPFPNWLHG LLRILGASQF QGGELALSAF LVLVFLWLHS LRRLFECFYV
160 170 180 190 200
SVFSNTVIHI VQYCFGLVYY VLTGLTVLSQ VPMDGRNAYV IGKNLLMQAR
210 220 230 240 250
WFHILGMLMF IWSSVHQYKC HVILGNLRKN KAGVVIHCNH RIPFGDWFEY
260 270 280 290 300
VSSPNYLAEL MIYISMAVTF GFHNLTWWLV VTYVFFSQAL SAFLSHKFYK
310
SKFVSYPKHR KAFLPFLF
Length:318
Mass (Da):36,775
Last modified:February 9, 2010 - v1
Checksum:iB0CD88A5D8E2667D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL192668 Genomic DNA. Translation: EFB15787.1.
RefSeqiXP_002919412.1. XM_002919366.2.

Genome annotation databases

GeneIDi100463734.
KEGGiaml:100463734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL192668 Genomic DNA. Translation: EFB15787.1.
RefSeqiXP_002919412.1. XM_002919366.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9646.ENSAMEP00000019466.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100463734.
KEGGiaml:100463734.

Organism-specific databases

CTDi79644.

Phylogenomic databases

eggNOGiKOG1640. Eukaryota.
ENOG4111JQM. LUCA.
HOGENOMiHOG000018885.
InParanoidiD2HBV9.
KOiK12345.
OrthoDBiEOG091G0F09.

Enzyme and pathway databases

UniPathwayiUPA00378.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPORED_AILME
AccessioniPrimary (citable) accession number: D2HBV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 9, 2010
Last modified: September 7, 2016
This is version 31 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.