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Q8VCH6

- DHC24_MOUSE

UniProt

Q8VCH6 - DHC24_MOUSE

Protein

Delta(24)-sterol reductase

Gene

Dhcr24

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the reduction of the delta-24 double bond of sterol intermediates.By similarity

    Catalytic activityi

    5-alpha-cholest-7-en-3-beta-ol + NADP+ = 5-alpha-cholesta-7,24-dien-3-beta-ol + NADPH.

    Cofactori

    FAD.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei122 – 1232Cleavage; by caspaseSequence Analysis
    Sitei383 – 3842Cleavage; by caspaseSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi163 – 17513FADSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. delta24-sterol reductase activity Source: UniProtKB-EC
    2. enzyme binding Source: UniProtKB
    3. flavin adenine dinucleotide binding Source: InterPro
    4. oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Source: MGI
    5. peptide antigen binding Source: UniProtKB
    6. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro

    GO - Biological processi

    1. amyloid precursor protein catabolic process Source: MGI
    2. cholesterol biosynthetic process Source: UniProtKB
    3. cholesterol metabolic process Source: MGI
    4. male genitalia development Source: MGI
    5. membrane organization Source: MGI
    6. negative regulation of apoptotic process Source: UniProtKB
    7. negative regulation of cell proliferation Source: Ensembl
    8. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    9. plasminogen activation Source: MGI
    10. protein localization Source: MGI
    11. Ras protein signal transduction Source: Ensembl
    12. response to hormone Source: Ensembl
    13. response to oxidative stress Source: UniProtKB
    14. skin development Source: UniProtKB
    15. sterol metabolic process Source: MGI
    16. tissue development Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    ReactomeiREACT_208531. Cholesterol biosynthesis.
    UniPathwayiUPA00063.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta(24)-sterol reductase (EC:1.3.1.72)
    Alternative name(s):
    24-dehydrocholesterol reductase
    3-beta-hydroxysterol delta-24-reductase
    Gene namesi
    Name:Dhcr24
    Synonyms:Kiaa0018
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1922004. Dhcr24.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoskeleton Source: Ensembl
    2. cytosol Source: Ensembl
    3. endoplasmic reticulum Source: UniProtKB
    4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    5. Golgi membrane Source: UniProtKB-SubCell
    6. integral component of membrane Source: UniProtKB-KW
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 516494Delta(24)-sterol reductasePRO_0000320300Add
    BLAST

    Proteomic databases

    MaxQBiQ8VCH6.
    PaxDbiQ8VCH6.
    PRIDEiQ8VCH6.

    PTM databases

    PhosphoSiteiQ8VCH6.

    Expressioni

    Gene expression databases

    BgeeiQ8VCH6.
    CleanExiMM_DHCR24.
    GenevestigatoriQ8VCH6.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-1858806.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VCH6.
    SMRiQ8VCH6. Positions 115-286.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 319LumenalSequence Analysis
    Topological domaini53 – 516464CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei32 – 5221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 234177FAD-binding PCMH-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0277.
    GeneTreeiENSGT00390000008338.
    HOGENOMiHOG000243421.
    HOVERGENiHBG051349.
    InParanoidiQ8VCH6.
    KOiK09828.
    OMAiLPNNPGM.
    OrthoDBiEOG7H7920.
    PhylomeDBiQ8VCH6.
    TreeFamiTF313170.

    Family and domain databases

    Gene3Di3.30.465.10. 1 hit.
    InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR006094. Oxid_FAD_bind_N.
    [Graphical view]
    PfamiPF01565. FAD_binding_4. 1 hit.
    [Graphical view]
    SUPFAMiSSF56176. SSF56176. 1 hit.
    PROSITEiPS51387. FAD_PCMH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8VCH6-1 [UniParc]FASTAAdd to Basket

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    MEPAVSLAVC ALLFLLWVRV KGLEFVLIHQ RWVFVCLFLL PLSLIFDIYY    50
    YVRAWVVFKL SSAPRLHEQR VRDIQKQVRE WKEQGSKTFM CTGRPGWLTV 100
    SLRVGKYKKT HKNIMINLMD ILEVDTKKQI VRVEPLVSMG QVTALLNSIG 150
    WTLPVLPELD DLTVGGLIMG TGIESSSHKY GLFQHICTAY ELILADGSFV 200
    RCTPSENSDL FYAVPWSCGT LGFLVAAEIR IIPAKKYVKL RFEPVRGLEA 250
    ICEKFTRESQ RLENHFVEGL LYSLDEAVIM TGVMTDDVEP SKLNSIGSYY 300
    KPWFFKHVEN YLKTNREGLE YIPLRHYYHR HTRSIFWELQ DIIPFGNNPI 350
    FRYLFGWMVP PKISLLKLTQ GETLRKLYEQ HHVVQDMLVP MKCMSQALHT 400
    FQNDIHVYPI WLCPFILPSQ PGLVHPKGDE AELYVDIGAY GEPRVKHFEA 450
    RSCMRQLEKF VRSVHGFQML YADCYMNREE FWEMFDGSLY HKLRKQLGCQ 500
    DAFPEVYDKI CKAARH 516
    Length:516
    Mass (Da):60,112
    Last modified:March 1, 2002 - v1
    Checksum:i7F41D598539E86E4
    GO

    Sequence cautioni

    The sequence BAC97846.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 622SS → TN in BAB31012. (PubMed:16141072)Curated
    Sequence conflicti68 – 714EQRV → NXPL in BAB31012. (PubMed:16141072)Curated
    Sequence conflicti94 – 941R → P in BAB31012. (PubMed:16141072)Curated
    Sequence conflicti278 – 2781V → VAV in AAK72106. (PubMed:11519011)Curated
    Sequence conflicti290 – 2901P → S in AAK72106. (PubMed:11519011)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY039762 mRNA. Translation: AAK72106.1.
    AK129036 mRNA. Translation: BAC97846.1. Different initiation.
    AL929585, BX511043 Genomic DNA. Translation: CAM27475.1.
    BC019797 mRNA. Translation: AAH19797.1.
    AK017937 mRNA. Translation: BAB31012.1.
    CCDSiCCDS18420.1.
    RefSeqiNP_444502.2. NM_053272.2.
    UniGeneiMm.133370.

    Genome annotation databases

    EnsembliENSMUST00000047973; ENSMUSP00000038063; ENSMUSG00000034926.
    GeneIDi74754.
    KEGGimmu:74754.
    UCSCiuc008tyl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY039762 mRNA. Translation: AAK72106.1 .
    AK129036 mRNA. Translation: BAC97846.1 . Different initiation.
    AL929585 , BX511043 Genomic DNA. Translation: CAM27475.1 .
    BC019797 mRNA. Translation: AAH19797.1 .
    AK017937 mRNA. Translation: BAB31012.1 .
    CCDSi CCDS18420.1.
    RefSeqi NP_444502.2. NM_053272.2.
    UniGenei Mm.133370.

    3D structure databases

    ProteinModelPortali Q8VCH6.
    SMRi Q8VCH6. Positions 115-286.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1858806.

    PTM databases

    PhosphoSitei Q8VCH6.

    Proteomic databases

    MaxQBi Q8VCH6.
    PaxDbi Q8VCH6.
    PRIDEi Q8VCH6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000047973 ; ENSMUSP00000038063 ; ENSMUSG00000034926 .
    GeneIDi 74754.
    KEGGi mmu:74754.
    UCSCi uc008tyl.1. mouse.

    Organism-specific databases

    CTDi 1718.
    MGIi MGI:1922004. Dhcr24.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0277.
    GeneTreei ENSGT00390000008338.
    HOGENOMi HOG000243421.
    HOVERGENi HBG051349.
    InParanoidi Q8VCH6.
    KOi K09828.
    OMAi LPNNPGM.
    OrthoDBi EOG7H7920.
    PhylomeDBi Q8VCH6.
    TreeFami TF313170.

    Enzyme and pathway databases

    UniPathwayi UPA00063 .
    Reactomei REACT_208531. Cholesterol biosynthesis.

    Miscellaneous databases

    ChiTaRSi DHCR24. mouse.
    NextBioi 341564.
    PROi Q8VCH6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8VCH6.
    CleanExi MM_DHCR24.
    Genevestigatori Q8VCH6.

    Family and domain databases

    Gene3Di 3.30.465.10. 1 hit.
    InterProi IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR006094. Oxid_FAD_bind_N.
    [Graphical view ]
    Pfami PF01565. FAD_binding_4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56176. SSF56176. 1 hit.
    PROSITEi PS51387. FAD_PCMH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mutations in the 3beta-hydroxysterol delta24-reductase gene cause desmosterolosis, an autosomal recessive disorder of cholesterol biosynthesis."
      Waterham H.R., Koster J., Romeijn G.J., Hennekam R.C.M., Vreken P., Andersson H.C., FitzPatrick D.R., Kelley R.I., Wanders R.J.A.
      Am. J. Hum. Genet. 69:685-694(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Fetal brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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].
      Strain: FVB/N.
      Tissue: Liver.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-516.
      Strain: C57BL/6J.
      Tissue: Thymus.

    Entry informationi

    Entry nameiDHC24_MOUSE
    AccessioniPrimary (citable) accession number: Q8VCH6
    Secondary accession number(s): Q6ZQK9, Q91ZD0, Q9CU63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 92 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3