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Protein

Cholesterol 25-hydroxylase

Gene

Ch25h

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Catalyzes the formation of 25-hydroxycholesterol from cholesterol, leading to repress cholesterol biosynthetic enzymes. Plays a key role in cell positioning and movement in lymphoid tissues: 25-hydroxycholesterol is an intermediate in biosynthesis of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC), an oxysterol that acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells. 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.By similarity

Catalytic activityi

Cholesterol + AH2 + O2 = 25-hydroxycholesterol + A + H2O.By similarity

Cofactori

Fe cationBy similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processLipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandIron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.99.38 5301
ReactomeiR-RNO-192105 Synthesis of bile acids and bile salts

Names & Taxonomyi

Protein namesi
Recommended name:
Cholesterol 25-hydroxylase (EC:1.14.99.38)
Alternative name(s):
Cholesterol 25-monooxygenase
Gene namesi
Name:Ch25h
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1310575 Ch25h

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei38 – 58HelicalSequence analysisAdd BLAST21
Transmembranei84 – 104HelicalSequence analysisAdd BLAST21
Transmembranei124 – 144HelicalSequence analysisAdd BLAST21
Transmembranei167 – 187HelicalSequence analysisAdd BLAST21
Transmembranei190 – 210HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002268041 – 298Cholesterol 25-hydroxylaseAdd BLAST298

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi5N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi163N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ4QQV7

Expressioni

Tissue specificityi

Expressed in testicular macrophages at all stages, with the highest level in 10 day old animals.2 Publications

Inductioni

Down-regulated by testosterone.1 Publication

Gene expression databases

BgeeiENSRNOG00000019141
GenevisibleiQ4QQV7 RN

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025856

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi142 – 146Histidine box-15
Motifi157 – 161Histidine box-25
Motifi238 – 244Histidine box-37

Sequence similaritiesi

Belongs to the sterol desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0873 Eukaryota
COG3000 LUCA
GeneTreeiENSGT00530000063017
HOGENOMiHOG000015767
HOVERGENiHBG080944
InParanoidiQ4QQV7
KOiK10223
OMAiQFNCNFA
OrthoDBiEOG091G0CY4
PhylomeDBiQ4QQV7
TreeFamiTF353265

Family and domain databases

InterProiView protein in InterPro
IPR006694 Fatty_acid_hydroxylase
PfamiView protein in Pfam
PF04116 FA_hydroxylase, 1 hit

Sequencei

Sequence statusi: Complete.

Q4QQV7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACHNVSELQ DLGCSNQLLL QPLWDSIRTG EASARSPFFP VIFSIFTYLG
60 70 80 90 100
FCLPFVVLDV LCPWVPILRR YKIHPDFSPS VRQLLPCLGL TLYQHLVFVF
110 120 130 140 150
PVTLMHWARS PALLPREAPE LSQLLSHVLI CLLLFDTEIF AWHLLHHKVP
160 170 180 190 200
WLYRTFHKVH HQNSSSFALA TQYMSVWELL SLTFFDVLNV AMLQCHPLTI
210 220 230 240 250
LVFHVVNIWL SVEDHSGYDF PWSTHRLVPF GWYGGVAHHD LHHSQFNCNF
260 270 280 290
APYFTHWDKM LGTLRCAPHS KRLCAGSESC LDSGEQCTVH LNQKKKQT
Length:298
Mass (Da):34,414
Last modified:July 19, 2005 - v1
Checksum:i25BC9E1DDAC4AF3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC097964 mRNA Translation: AAH97964.1
RefSeqiNP_001020586.1, NM_001025415.1
XP_006231353.1, XM_006231291.3
UniGeneiRn.155971

Genome annotation databases

EnsembliENSRNOT00000025856; ENSRNOP00000025856; ENSRNOG00000019141
GeneIDi309527
KEGGirno:309527
UCSCiRGD:1310575 rat

Similar proteinsi

Entry informationi

Entry nameiCH25H_RAT
AccessioniPrimary (citable) accession number: Q4QQV7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: July 19, 2005
Last modified: May 23, 2018
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health