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Protein

Lathosterol oxidase

Gene

Sc5d

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol.1 Publication

Catalytic activityi

A Delta(7)-sterol + 2 ferrocytochrome b5 + O2 + 2 H+ = a Delta(5,7)-sterol + 2 ferricytochrome b5 + 2 H2O.2 Publications

Cofactori

Fe cationBy similarity

GO - Molecular functioni

  • C-5 sterol desaturase activity Source: RGD
  • iron ion binding Source: InterPro
  • lathosterol oxidase activity Source: RGD

GO - Biological processi

  • cholesterol biosynthetic process via lathosterol Source: RGD
  • fatty acid biosynthetic process Source: InterPro
  • fatty acid metabolic process Source: RGD
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

ReactomeiR-RNO-2426168. Activation of gene expression by SREBF (SREBP).
R-RNO-6807047. Cholesterol biosynthesis via desmosterol.
R-RNO-6807062. Cholesterol biosynthesis via lathosterol.

Names & Taxonomyi

Protein namesi
Recommended name:
Lathosterol oxidase (EC:1.14.19.20)
Alternative name(s):
C-5 sterol desaturase
Delta(7)-sterol 5-desaturase
Delta(7)-sterol C5(6)-desaturase
Lathosterol 5-desaturase
Sterol-C5-desaturaseImported
Gene namesi
Name:Sc5dImported
Synonyms:C5dImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi620775. Sc5d.

Subcellular locationi

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

Topology

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Lathosterol oxidasePRO_0000434558Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9EQS5.

Expressioni

Gene expression databases

GenevisibleiQ9EQS5. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011284.

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

eggNOGiKOG0872. Eukaryota.
COG3000. LUCA.
GeneTreeiENSGT00550000075101.
HOGENOMiHOG000200579.
HOVERGENiHBG012628.
KOiK00227.
OMAiDHALMKH.
OrthoDBiEOG7NSB2T.
PhylomeDBiQ9EQS5.
TreeFamiTF300797.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9EQS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLVLSAADY YFFTPYVYPA TWPEDNIIRQ TVSLLVVTNL GAYILYFFCA
60 70 80 90 100
TLSYYFVYDH SLMKHPQFLK NQVSREIMFT VKSLPWISIP TVSLFLLELR
110 120 130 140 150
GYSKLYDDIG DFPNGWIHLI MSVISFLFFT DMLIYWIHRG LHHRLLYKHI
160 170 180 190 200
HKPHHIWKIP TPFASHAFHP VDGFLQSLPY HIYPFVFPLH KVVYLGLYVL
210 220 230 240 250
VNVWTISIHD GDFRVPQIFR PFINGSAHHT DHHMLFDYNY GQYFTLWDRI
260 270 280 290
GGSFKHPSSF EGKGPHSYVK NMTEKESNSL AENGCKSKKL CNGEFTKNE
Length:299
Mass (Da):35,147
Last modified:March 1, 2001 - v1
Checksum:iAE2D03FF486A46A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052846 mRNA. Translation: BAB19798.1.
AC133265 Genomic DNA. No translation available.
CH473975 Genomic DNA. Translation: EDL95251.1.
BC081704 mRNA. Translation: AAH81704.1.
RefSeqiNP_446094.1. NM_053642.2.
UniGeneiRn.17462.
Rn.18741.

Genome annotation databases

EnsembliENSRNOT00000011284; ENSRNOP00000011284; ENSRNOG00000008305.
GeneIDi114100.
KEGGirno:114100.
UCSCiRGD:620775. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052846 mRNA. Translation: BAB19798.1.
AC133265 Genomic DNA. No translation available.
CH473975 Genomic DNA. Translation: EDL95251.1.
BC081704 mRNA. Translation: AAH81704.1.
RefSeqiNP_446094.1. NM_053642.2.
UniGeneiRn.17462.
Rn.18741.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011284.

Proteomic databases

PaxDbiQ9EQS5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011284; ENSRNOP00000011284; ENSRNOG00000008305.
GeneIDi114100.
KEGGirno:114100.
UCSCiRGD:620775. rat.

Organism-specific databases

CTDi6309.
RGDi620775. Sc5d.

Phylogenomic databases

eggNOGiKOG0872. Eukaryota.
COG3000. LUCA.
GeneTreeiENSGT00550000075101.
HOGENOMiHOG000200579.
HOVERGENiHBG012628.
KOiK00227.
OMAiDHALMKH.
OrthoDBiEOG7NSB2T.
PhylomeDBiQ9EQS5.
TreeFamiTF300797.

Enzyme and pathway databases

ReactomeiR-RNO-2426168. Activation of gene expression by SREBF (SREBP).
R-RNO-6807047. Cholesterol biosynthesis via desmosterol.
R-RNO-6807062. Cholesterol biosynthesis via lathosterol.

Miscellaneous databases

PROiQ9EQS5.

Gene expression databases

GenevisibleiQ9EQS5. RN.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and site-directed mutagenesis of the mammalian sterol C5-desaturase."
    Nishino H., Hozumi K., Moromi M., Nam S., Ishibashi T.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "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.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: TestisImported.
  5. "Partial purification and characterization of lathosterol 5-desaturase from rat liver microsomes."
    Honjo K., Ishibashi T., Imai Y.
    J. Biochem. 97:955-959(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
  6. "Temperature-induced differential kinetic properties between an initial burst and the following steady state in membrane-bound enzymes: studies on lathosterol 5-desaturase."
    Nishino H., Nakaya J., Nishi S., Kurosawa T., Ishibashi T.
    Arch. Biochem. Biophys. 339:298-304(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.

Entry informationi

Entry nameiSC5D_RAT
AccessioniPrimary (citable) accession number: Q9EQS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2015
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 101 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.