Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5RIU9

- PORED_DANRE

UniProt

Q5RIU9 - PORED_DANRE

Protein

Polyprenol reductase

Gene

srd5a3

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    GO - Molecular functioni

    1. 3-oxo-5-alpha-steroid 4-dehydrogenase activity Source: UniProtKB
    2. cholestenone 5-alpha-reductase activity Source: UniProtKB-EC
    3. oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Source: UniProtKB

    GO - Biological processi

    1. dolichol-linked oligosaccharide biosynthetic process Source: UniProtKB
    2. dolichol metabolic process Source: UniProtKB
    3. polyprenol catabolic process Source: UniProtKB
    4. protein glycosylation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    ReactomeiREACT_175194. Synthesis of Dolichyl-phosphate.
    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:si:ch211-278f21.3
    OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
    Taxonomic identifieri7955 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
    ProteomesiUP000000437: Chromosome 20

    Organism-specific databases

    ZFINiZDB-GENE-030131-7915. srd5a3.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309Polyprenol reductasePRO_0000398651Add
    BLAST

    Proteomic databases

    PRIDEiQ5RIU9.

    Expressioni

    Gene expression databases

    BgeeiQ5RIU9.

    Interactioni

    Protein-protein interaction databases

    STRINGi7955.ENSDARP00000063577.

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 33CytoplasmicSequence Analysis
    Topological domaini25 – 6743LumenalSequence AnalysisAdd
    BLAST
    Topological domaini89 – 11426CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini136 – 15015LumenalSequence AnalysisAdd
    BLAST
    Topological domaini172 – 18514CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini207 – 25549LumenalSequence AnalysisAdd
    BLAST
    Topological domaini277 – 30933CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4 – 2421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei68 – 8821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei115 – 13521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei151 – 17121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei186 – 20621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei256 – 27621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG330066.
    GeneTreeiENSGT00500000044920.
    HOGENOMiHOG000018885.
    HOVERGENiHBG057797.
    InParanoidiA4FVI8.
    KOiK12345.
    OMAiSSPHMFF.
    OrthoDBiEOG72ZCFT.
    PhylomeDBiQ5RIU9.
    TreeFamiTF315011.

    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.

    Q5RIU9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFHILSIVNI IWLLLALCFG AAFCLNKFSV KLPNRVEHVF QDFIRYGKTK    50
    ENIKRASWQL VFDLSKRYFY HFYVVSVMWN GLLLLFSIRS VVMSEAFPDW 100
    IIDVLGSLTG RSRGAWNEIH LSTLLLQVLL WVHTLRRLLE CLFVSVFSDG 150
    VINVVQYAFG LSYYIILGLT VLCTNDSLPQ SESVSFFNQL TWYHVVGTLL 200
    FFWASFLQHQ SLSLLAKMRT DSSGKVETLA HKMPCGGWFE LVSCPHYLAE 250
    LLIYAAMCVC CGCASLTWWM VVLYVLCNQA LAAQLCHEYY RSKFKTYPHH 300
    RKAFIPFVL 309
    Length:309
    Mass (Da):35,708
    Last modified:December 21, 2004 - v1
    Checksum:i89513C21F5D7FEB6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691F → S in AAI33965. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX088688 Genomic DNA. Translation: CAI11971.1.
    BC133964 mRNA. Translation: AAI33965.1.
    RefSeqiNP_001038404.1. NM_001044939.1.
    UniGeneiDr.81044.

    Genome annotation databases

    EnsembliENSDART00000063578; ENSDARP00000063577; ENSDARG00000043307.
    GeneIDi560717.
    KEGGidre:560717.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX088688 Genomic DNA. Translation: CAI11971.1 .
    BC133964 mRNA. Translation: AAI33965.1 .
    RefSeqi NP_001038404.1. NM_001044939.1.
    UniGenei Dr.81044.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7955.ENSDARP00000063577.

    Proteomic databases

    PRIDEi Q5RIU9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSDART00000063578 ; ENSDARP00000063577 ; ENSDARG00000043307 .
    GeneIDi 560717.
    KEGGi dre:560717.

    Organism-specific databases

    CTDi 79644.
    ZFINi ZDB-GENE-030131-7915. srd5a3.

    Phylogenomic databases

    eggNOGi NOG330066.
    GeneTreei ENSGT00500000044920.
    HOGENOMi HOG000018885.
    HOVERGENi HBG057797.
    InParanoidi A4FVI8.
    KOi K12345.
    OMAi SSPHMFF.
    OrthoDBi EOG72ZCFT.
    PhylomeDBi Q5RIU9.
    TreeFami TF315011.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_175194. Synthesis of Dolichyl-phosphate.

    Miscellaneous databases

    NextBioi 20883585.
    PROi Q5RIU9.

    Gene expression databases

    Bgeei Q5RIU9.

    Family and domain databases

    InterProi IPR001104. 3-oxo-5_a-steroid_4-DH_C.
    [Graphical view ]
    Pfami PF02544. Steroid_dh. 1 hit.
    [Graphical view ]
    PROSITEi PS50244. S5A_REDUCTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The zebrafish reference genome sequence and its relationship to the human genome."
      Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
      , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
      Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Tuebingen.
    2. NIH - Zebrafish Gene Collection (ZGC) project
      Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.

    Entry informationi

    Entry nameiPORED_DANRE
    AccessioniPrimary (citable) accession number: Q5RIU9
    Secondary accession number(s): A4FVI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 63 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

    External Data

    Dasty 3