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Q5RJM1

- PORED_RAT

UniProt

Q5RJM1 - PORED_RAT

Protein

Polyprenol reductase

Gene

Srd5a3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    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).1 Publication

    Catalytic activityi

    Ditrans,polycis-dolichol + NADP+ = ditrans,polycis-polyprenol + NADPH.1 Publication
    A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta(4)-steroid + NADPH.1 Publication

    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_195792. 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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 14

    Organism-specific databases

    RGDi1308828. Srd5a3.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    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 – 330330Polyprenol reductasePRO_0000398650Add
    BLAST

    Proteomic databases

    PRIDEiQ5RJM1.

    Expressioni

    Tissue specificityi

    Expressed in the 2 tissues tested i.e. testis and liver.1 Publication

    Gene expression databases

    GenevestigatoriQ5RJM1.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000003021.

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini38 – 8952LumenalSequence AnalysisAdd
    BLAST
    Topological domaini111 – 13626CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini158 – 16912LumenalSequence AnalysisAdd
    BLAST
    Topological domaini191 – 20616CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini228 – 27750LumenalSequence AnalysisAdd
    BLAST
    Topological domaini299 – 33032CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei17 – 3721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei90 – 11021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei137 – 15721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei170 – 19021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei207 – 22721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei278 – 29821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG330066.
    GeneTreeiENSGT00500000044920.
    HOGENOMiHOG000018885.
    HOVERGENiHBG057797.
    KOiK12345.
    OMAiGMESKAS.
    OrthoDBiEOG72ZCFT.
    PhylomeDBiQ5RJM1.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5RJM1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGWAGAELS VLNPLRALWL LLAAAFLLAL LLQLAPARLL PSCALFQDLI    50
    RYGKTKQSGS RRPAVCRAFD VPKRYFSHFY VVSVLWNGSL LWFLSQSLFL 100
    GAPFPSWLWA LLRTLGVTQF QALGMESKAS RIQGKKLALS TFLVLVFLWV 150
    HSLRRLFECF YVSVFSNTAI HVVQYCFGLV YYVLVGLTVL SQVPMNDKNV 200
    YALGKNLLLQ ARWFHILGMM MFFWSSAHQY KCHVILSNLR RNKKGVVIHC 250
    QHRIPFGDWF EYVSSANYLA ELMIYISMAV TFGLHNVTWW LVVTYVFFSQ 300
    ALSAFFNHRF YKSTFVSYPK HRKAFLPFLF 330
    Length:330
    Mass (Da):38,092
    Last modified:October 5, 2010 - v2
    Checksum:iEC97594D66A76543
    GO
    Isoform 2 (identifier: Q5RJM1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         262-330: YVSSANYLAE...HRKAFLPFLF → LYGEERSPGDRFPSSRR

    Note: No experimental confirmation available.

    Show »
    Length:278
    Mass (Da):31,886
    Checksum:iD1548EFDF67DD528
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti134 – 1363GKK → AGE in AAH86584. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei262 – 33069YVSSA…LPFLF → LYGEERSPGDRFPSSRR in isoform 2. 1 PublicationVSP_039791Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC086584 mRNA. Translation: AAH86584.1.
    RefSeqiNP_001014012.1. NM_001013990.1.
    UniGeneiRn.819.

    Genome annotation databases

    EnsembliENSRNOT00000003021; ENSRNOP00000003021; ENSRNOG00000002216.
    ENSRNOT00000059763; ENSRNOP00000056514; ENSRNOG00000002216. [Q5RJM1-2]
    GeneIDi305291.
    KEGGirno:305291.
    UCSCiRGD:1308828. rat. [Q5RJM1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC086584 mRNA. Translation: AAH86584.1 .
    RefSeqi NP_001014012.1. NM_001013990.1.
    UniGenei Rn.819.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000003021.

    Proteomic databases

    PRIDEi Q5RJM1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000003021 ; ENSRNOP00000003021 ; ENSRNOG00000002216 .
    ENSRNOT00000059763 ; ENSRNOP00000056514 ; ENSRNOG00000002216 . [Q5RJM1-2 ]
    GeneIDi 305291.
    KEGGi rno:305291.
    UCSCi RGD:1308828. rat. [Q5RJM1-1 ]

    Organism-specific databases

    CTDi 79644.
    RGDi 1308828. Srd5a3.

    Phylogenomic databases

    eggNOGi NOG330066.
    GeneTreei ENSGT00500000044920.
    HOGENOMi HOG000018885.
    HOVERGENi HBG057797.
    KOi K12345.
    OMAi GMESKAS.
    OrthoDBi EOG72ZCFT.
    PhylomeDBi Q5RJM1.
    TreeFami TF315011.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_195792. Synthesis of Dolichyl-phosphate.

    Miscellaneous databases

    NextBioi 654334.
    PROi Q5RJM1.

    Gene expression databases

    Genevestigatori Q5RJM1.

    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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Ovary.
    3. "Formation of dolichol from dehydrodolichol is catalyzed by NADPH-dependent reductase localized in microsomes of rat liver."
      Sagami H., Kurisaki A., Ogura K.
      J. Biol. Chem. 268:10109-10113(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Liver.

    Entry informationi

    Entry nameiPORED_RAT
    AccessioniPrimary (citable) accession number: Q5RJM1
    Secondary accession number(s): D3ZUS5, D4A5U7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 59 of the entry and version 2 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