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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-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
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeMesocricetus
Proteomesi
  • UP000189706 Componenti: Genome assembly

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 – 19CytoplasmicSequence analysisAdd BLAST19
Transmembranei20 – 40HelicalSequence analysisAdd BLAST21
Topological domaini41 – 74LumenalSequence analysisAdd BLAST34
Transmembranei75 – 95HelicalSequence analysisAdd BLAST21
Topological domaini96 – 132CytoplasmicSequence analysisAdd BLAST37
Transmembranei133 – 153HelicalSequence analysisAdd BLAST21
Topological domaini154 – 168LumenalSequence analysisAdd BLAST15
Transmembranei169 – 189HelicalSequence analysisAdd BLAST21
Topological domaini190 – 206CytoplasmicSequence analysisAdd BLAST17
Transmembranei207 – 227HelicalSequence analysisAdd BLAST21
Topological domaini228 – 277LumenalSequence analysisAdd BLAST50
Transmembranei278 – 298HelicalSequence analysisAdd BLAST21
Topological domaini299 – 330CytoplasmicSequence analysisAdd BLAST32

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003986491 – 330Polyprenol reductaseAdd BLAST330

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

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.

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.

Similar proteinsi

Entry informationi

Entry nameiPORED_MESAU
AccessioniPrimary (citable) accession number: C7T2J9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 13, 2009
Last modified: September 27, 2017
This is version 25 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