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Protein

Cholesterol 25-hydroxylase

Gene

Ch25h

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

Functioni

Catalyzes the formation of 25-hydroxycholesterol from cholesterol, leading to repress cholesterol biosynthetic enzymes. May play an important role in regulating lipid metabolism by synthesizing a corepressor that blocks sterol regulatory element binding protein (SREBP) processing. In testis, production of 25-hydroxycholesterol by macrophages may play a role in Leydig cell differentiation.1 Publication

Catalytic activityi

Cholesterol + AH2 + O2 = 25-hydroxycholesterol + A + H2O.1 Publication

Cofactori

Fe cation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.99.38. 3474.
ReactomeiR-MMU-192105. Synthesis of bile acids and bile salts.

Chemistry

SwissLipidsiSLP:000001484.

Names & Taxonomyi

Protein namesi
Recommended name:
Cholesterol 25-hydroxylase (EC:1.14.99.38)
Alternative name(s):
Cholesterol 25-monooxygenase
Short name:
m25OH
Gene namesi
Name:Ch25h
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1333869. Ch25h.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei38 – 5821HelicalSequence analysisAdd
BLAST
Transmembranei88 – 10821HelicalSequence analysisAdd
BLAST
Transmembranei124 – 14421HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice do not display any apparent alteration in bile acid synthesis and cholesterol metabolism.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi242 – 2432HH → EE: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 298298Cholesterol 25-hydroxylasePRO_0000226802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi5 – 51N-linked (GlcNAc...)Sequence analysis
Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9Z0F5.
PRIDEiQ9Z0F5.

Expressioni

Tissue specificityi

Widely expressed at low level and at higher level in the lung. Weakly expressed in the heart, lung and kidney.1 Publication

Gene expression databases

BgeeiQ9Z0F5.
CleanExiMM_CH25H.
GenevisibleiQ9Z0F5. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000049683.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi142 – 1465Histidine box-1
Motifi157 – 1615Histidine box-2
Motifi238 – 2447Histidine box-3

Sequence similaritiesi

Belongs to the sterol desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0873. Eukaryota.
COG3000. LUCA.
GeneTreeiENSGT00530000063017.
HOGENOMiHOG000015767.
HOVERGENiHBG080944.
InParanoidiQ9Z0F5.
KOiK10223.
OMAiYFLWHLL.
OrthoDBiEOG7288S0.
PhylomeDBiQ9Z0F5.
TreeFamiTF353265.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9Z0F5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCYNGSELQ DLGCSSQLLL QPLWDTIRTR EAFTRSPIFP VTFSIITYVG
60 70 80 90 100
FCLPFVVLDV LYPWVPILRR YKIHPDFSPS VKQLLPCLGL TLYQHLVFVF
110 120 130 140 150
PVTLLHWVRS PALLPQEAPE LVQLLSHVLI CLLLFDTEIF AWHLLHHKVP
160 170 180 190 200
WLYRTFHKVH HQNSSSFALA TQYMSFWELL SLTFFDVLNV AVLRCHPLTI
210 220 230 240 250
FTFHVINIWL SVEDHSGYDF PWSTHRLVPF GWYGGVAHHD MHHSQFNCNF
260 270 280 290
APYFTHWDKM LGTLRSAPLP ESLCACGERC VNSRERCAVH LIQKKKQT
Length:298
Mass (Da):34,672
Last modified:May 1, 1999 - v1
Checksum:iBBCE4A97A20284C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221V → A in AAH39919 (PubMed:15489334).Curated
Sequence conflicti199 – 1991T → S in BAE35945 (PubMed:16141072).Curated
Sequence conflicti282 – 2821N → D in AAH39919 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059211 Genomic DNA. Translation: AAC97480.1.
AF059213 mRNA. Translation: AAC97482.1.
AK140360 mRNA. Translation: BAE24352.1.
AK152770 mRNA. Translation: BAE31482.1.
AK160657 mRNA. Translation: BAE35945.1.
BC039919 mRNA. Translation: AAH39919.1.
CCDSiCCDS29759.1.
RefSeqiNP_034020.1. NM_009890.1.
UniGeneiMm.30824.

Genome annotation databases

EnsembliENSMUST00000050562; ENSMUSP00000049683; ENSMUSG00000050370.
GeneIDi12642.
KEGGimmu:12642.
UCSCiuc008hgj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059211 Genomic DNA. Translation: AAC97480.1.
AF059213 mRNA. Translation: AAC97482.1.
AK140360 mRNA. Translation: BAE24352.1.
AK152770 mRNA. Translation: BAE31482.1.
AK160657 mRNA. Translation: BAE35945.1.
BC039919 mRNA. Translation: AAH39919.1.
CCDSiCCDS29759.1.
RefSeqiNP_034020.1. NM_009890.1.
UniGeneiMm.30824.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000049683.

Chemistry

SwissLipidsiSLP:000001484.

Proteomic databases

PaxDbiQ9Z0F5.
PRIDEiQ9Z0F5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000050562; ENSMUSP00000049683; ENSMUSG00000050370.
GeneIDi12642.
KEGGimmu:12642.
UCSCiuc008hgj.1. mouse.

Organism-specific databases

CTDi9023.
MGIiMGI:1333869. Ch25h.

Phylogenomic databases

eggNOGiKOG0873. Eukaryota.
COG3000. LUCA.
GeneTreeiENSGT00530000063017.
HOGENOMiHOG000015767.
HOVERGENiHBG080944.
InParanoidiQ9Z0F5.
KOiK10223.
OMAiYFLWHLL.
OrthoDBiEOG7288S0.
PhylomeDBiQ9Z0F5.
TreeFamiTF353265.

Enzyme and pathway databases

BRENDAi1.14.99.38. 3474.
ReactomeiR-MMU-192105. Synthesis of bile acids and bile salts.

Miscellaneous databases

PROiQ9Z0F5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z0F5.
CleanExiMM_CH25H.
GenevisibleiQ9Z0F5. MM.

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 mouse and human cholesterol 25-hydroxylases, polytopic membrane proteins that synthesize a potent oxysterol regulator of lipid metabolism."
    Lund E.G., Kerr T.A., Sakai J., Li W.-P., Russell D.W.
    J. Biol. Chem. 273:34316-34327(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, ENZYME ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF 242-HIS-HIS-243.
    Strain: 129/SvEv and C57BL/6.
  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: Adipose tissue and Bone marrow.
  3. "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: Mammary tumor.
  4. "The enzymes, regulation, and genetics of bile acid synthesis."
    Russell D.W.
    Annu. Rev. Biochem. 72:137-174(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCH25H_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0F5
Secondary accession number(s): Q3TUM6, Q8CHQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 102 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. 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.