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Protein

Polyprenol reductase

Gene

Srd5a3

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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-Delta(4)-steroid + NADPH.

Pathway:iprotein 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
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei20 – 4021HelicalSequence AnalysisAdd
BLAST
Topological domaini41 – 7434LumenalSequence AnalysisAdd
BLAST
Transmembranei75 – 9521HelicalSequence AnalysisAdd
BLAST
Topological domaini96 – 13237CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei133 – 15321HelicalSequence AnalysisAdd
BLAST
Topological domaini154 – 16815LumenalSequence AnalysisAdd
BLAST
Transmembranei169 – 18921HelicalSequence AnalysisAdd
BLAST
Topological domaini190 – 20617CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei207 – 22721HelicalSequence AnalysisAdd
BLAST
Topological domaini228 – 27750LumenalSequence AnalysisAdd
BLAST
Transmembranei278 – 29821HelicalSequence AnalysisAdd
BLAST
Topological domaini299 – 33032CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Polyprenol reductasePRO_0000398649Add
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

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.

C7T2J9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASWVGTELS ALNPLRTLWL ALAAAFLLAL LLQLAPAGLL PNCALFQDLI
60 70 80 90 100
RYGKTKLSGP RRPAVCRAFD VPKRYFSHFY VVSVLWNGFL LWFLSRSLFL
110 120 130 140 150
GAPFPNWLRA LLRTLGSTQF RALEMESKAS QMLVGELALS AFLVLVFLWV
160 170 180 190 200
HSVRRLFECF YISVFSNAVM HVVQYCFGLV YYVLVGLTVL SQVPMDDKNV
210 220 230 240 250
YMLGKNLLLP ARWFHVLGMM MFLWSSAHQY ECHVILSNLR RNKKGAIVHC
260 270 280 290 300
QHRIPFGDWF EYVSSANYLA ELMIYISMAV TFGFHNFTWW LVVAYVFFCQ
310 320 330
ALSAFFNHKF YKSTFVSYPK HRKAFLPFLF
Length:330
Mass (Da):38,164
Last modified:October 13, 2009 - v1
Checksum:i6E7990C37A6D27D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ851160 mRNA. Translation: ACV30167.1.
RefSeqiNP_001268635.1. NM_001281706.1.

Genome annotation databases

GeneIDi101843963.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ851160 mRNA. Translation: ACV30167.1.
RefSeqiNP_001268635.1. NM_001281706.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101843963.

Organism-specific databases

CTDi79644.

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...

Publicationsi

  1. "Cloning, sequence analysis and tissue distribution of the steroid 5alpha-reductase 3 (Srd5a3) full-length cDNA from Syrian hamster."
    Vilchis F., Ramos L., Chavez B.
    Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Harderian gland.

Entry informationi

Entry nameiPORED_MESAU
AccessioniPrimary (citable) accession number: C7T2J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 13, 2009
Last modified: January 7, 2015
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3

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 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.