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Protein

Lathosterol oxidase

Gene

Sc5d

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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

Fe cationBy 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
Complete GO annotation...

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_303828. Activation of gene expression by SREBF (SREBP).
REACT_345006. 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 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1353611. Sc5d.

Subcellular locationi

Topology

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

GO - Cellular componenti

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

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.

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.
OMAiIEDSAYG.
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

        10         20         30         40         50
MDLVLSAADY YFFTPYVYPA TWPEDNIIRQ TISLLIVTNL GAYILYFFCA
60 70 80 90 100
TLSYYFVYDH SLMKHPQFLK NQVSREIVFT VKSLPWISIP TVSLFLLELR
110 120 130 140 150
GYSKLYDDIG DFPNGWIHLM VSVVSFLFFT DMLIYWIHRG LHHRLVYKRI
160 170 180 190 200
HKPHHIWKIP TPFASHAFHP VDGFLQSLPY HIYPFVFPLH KVVYLGLYVL
210 220 230 240 250
VNVWTISIHD GDFRVPQILR PFINGSAHHT DHHMFFDYNY GQYFTLWDRI
260 270 280 290
GGSFKHPSSF EGKGPHSYVK NMTEKESNSF AENGCKGKKV GNGEFTKNK
Length:299
Mass (Da):35,062
Last modified:September 17, 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:
EMBLi
GenBanki
DDBJi
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_006510253.2.
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:
EMBLi
GenBanki
DDBJi
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_006510253.2.
UniGeneiMm.32700.
Mm.392107.
Mm.470142.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000057354.

PTM databases

PhosphoSiteiO88822.

Proteomic databases

PRIDEiO88822.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6309.
MGIiMGI:1353611. Sc5d.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi1.14.21.6. 3474.
ReactomeiREACT_303828. Activation of gene expression by SREBF (SREBP).
REACT_345006. Cholesterol biosynthesis.

Miscellaneous databases

NextBioi382567.
PROiO88822.
SOURCEiSearch...

Gene expression databases

GenevestigatoriO88822.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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(1999) [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(2004) [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 14, 1999
Last sequence update: September 17, 2013
Last modified: March 31, 2015
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.