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O88822

- SC5D_MOUSE

UniProt

O88822 - SC5D_MOUSE

Protein

Lathosterol oxidase

Gene

Sc5d

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (18 Sep 2013)
      Previous versions | rss
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    Functioni

    Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol.

    Catalytic activityi

    5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O2 = cholesta-5,7-dien-3-beta-ol + NAD(P)+ + 2 H2O.

    Cofactori

    Iron.By similarity

    GO - Molecular functioni

    1. C-5 sterol desaturase activity Source: Ensembl
    2. iron ion binding Source: InterPro
    3. lathosterol oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cholesterol biosynthetic process via lathosterol Source: Ensembl
    2. fatty acid biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    Iron, NAD, NADP

    Enzyme and pathway databases

    BRENDAi1.14.21.6. 3474.
    ReactomeiREACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_208531. Cholesterol biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lathosterol oxidase (EC:1.14.21.6)
    Alternative name(s):
    C-5 sterol desaturase
    Delta(7)-sterol 5-desaturase
    Lathosterol 5-desaturase
    Sterol-C5-desaturase
    Gene namesi
    Name:Sc5d
    Synonyms:Sc5dl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1353611. Sc5d.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 299299Lathosterol oxidasePRO_0000117029Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei253 – 2531PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiO88822.

    PTM databases

    PhosphoSiteiO88822.

    Expressioni

    Gene expression databases

    GenevestigatoriO88822.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000057354.

    Structurei

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei32 – 5221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei79 – 9921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei117 – 13721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei186 – 20621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi138 – 1436Histidine box-1
    Motifi151 – 1555Histidine box-2
    Motifi228 – 2336Histidine box-3

    Domaini

    The histidine box domains may contain the active site and/or be involved in metal ion binding.

    Sequence similaritiesi

    Belongs to the sterol desaturase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3000.
    GeneTreeiENSGT00550000075101.
    HOGENOMiHOG000200579.
    HOVERGENiHBG012628.
    InParanoidiO88822.
    KOiK00227.
    OMAiFFCATLS.
    OrthoDBiEOG7NSB2T.
    TreeFamiTF300797.

    Family and domain databases

    InterProiIPR006694. Fatty_acid_hydroxylase.
    [Graphical view]
    PfamiPF04116. FA_hydroxylase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O88822-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLVLSAADY YFFTPYVYPA TWPEDNIIRQ TISLLIVTNL GAYILYFFCA    50
    TLSYYFVYDH SLMKHPQFLK NQVSREIVFT VKSLPWISIP TVSLFLLELR 100
    GYSKLYDDIG DFPNGWIHLM VSVVSFLFFT DMLIYWIHRG LHHRLVYKRI 150
    HKPHHIWKIP TPFASHAFHP VDGFLQSLPY HIYPFVFPLH KVVYLGLYVL 200
    VNVWTISIHD GDFRVPQILR PFINGSAHHT DHHMFFDYNY GQYFTLWDRI 250
    GGSFKHPSSF EGKGPHSYVK NMTEKESNSF AENGCKGKKV GNGEFTKNK 299
    Length:299
    Mass (Da):35,062
    Last modified:September 18, 2013 - v2
    Checksum:i96F3AFF61F7ED707
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361W → R in BAA33730. (PubMed:10786622)Curated
    Sequence conflicti291 – 2911G → S in BAA33730. (PubMed:10786622)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB016248 mRNA. Translation: BAA33730.1.
    AK043825 mRNA. Translation: BAC31666.1.
    AK077670 mRNA. Translation: BAC36944.1.
    AC160051 Genomic DNA. No translation available.
    CCDSiCCDS23086.1.
    RefSeqiNP_766357.1. NM_172769.2.
    XP_006510316.1. XM_006510253.1.
    UniGeneiMm.32700.
    Mm.392107.
    Mm.470142.

    Genome annotation databases

    EnsembliENSMUST00000052725; ENSMUSP00000057354; ENSMUSG00000032018.
    ENSMUST00000169609; ENSMUSP00000130438; ENSMUSG00000032018.
    GeneIDi235293.
    KEGGimmu:235293.
    UCSCiuc009par.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB016248 mRNA. Translation: BAA33730.1 .
    AK043825 mRNA. Translation: BAC31666.1 .
    AK077670 mRNA. Translation: BAC36944.1 .
    AC160051 Genomic DNA. No translation available.
    CCDSi CCDS23086.1.
    RefSeqi NP_766357.1. NM_172769.2.
    XP_006510316.1. XM_006510253.1.
    UniGenei Mm.32700.
    Mm.392107.
    Mm.470142.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000057354.

    PTM databases

    PhosphoSitei O88822.

    Proteomic databases

    PRIDEi O88822.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000052725 ; ENSMUSP00000057354 ; ENSMUSG00000032018 .
    ENSMUST00000169609 ; ENSMUSP00000130438 ; ENSMUSG00000032018 .
    GeneIDi 235293.
    KEGGi mmu:235293.
    UCSCi uc009par.1. mouse.

    Organism-specific databases

    CTDi 6309.
    MGIi MGI:1353611. Sc5d.

    Phylogenomic databases

    eggNOGi COG3000.
    GeneTreei ENSGT00550000075101.
    HOGENOMi HOG000200579.
    HOVERGENi HBG012628.
    InParanoidi O88822.
    KOi K00227.
    OMAi FFCATLS.
    OrthoDBi EOG7NSB2T.
    TreeFami TF300797.

    Enzyme and pathway databases

    BRENDAi 1.14.21.6. 3474.
    Reactomei REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_208531. Cholesterol biosynthesis.

    Miscellaneous databases

    NextBioi 382567.
    PROi O88822.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori O88822.

    Family and domain databases

    InterProi IPR006694. Fatty_acid_hydroxylase.
    [Graphical view ]
    Pfami PF04116. FA_hydroxylase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant."
      Nishi S., Nishino H., Ishibashi T.
      Biochim. Biophys. Acta 1490:106-108(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    2. "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].
      Strain: C57BL/6J.
      Tissue: Brain cortex.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.

    Entry informationi

    Entry nameiSC5D_MOUSE
    AccessioniPrimary (citable) accession number: O88822
    Secondary accession number(s): Q8BGI0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: September 18, 2013
    Last modified: October 1, 2014
    This is version 103 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3