CH25H_DANRE
ID CH25H_DANRE Reviewed; 251 AA.
AC Q5PRC0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cholesterol 25-hydroxylase-like protein;
DE EC=1.14.99.38 {ECO:0000250|UniProtKB:Q9Z0F5};
GN Name=ch25h; ORFNames=zgc:101688;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of 25-hydroxycholesterol from
CC cholesterol, leading to repress cholesterol biosynthetic enzymes. Plays
CC a key role in cell positioning and movement in lymphoid tissues: 25-
CC hydroxycholesterol is an intermediate in biosynthesis of 7-alpha,25-
CC dihydroxycholesterol (7-alpha,25-OHC), an oxysterol that acts as a
CC ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic
CC receptor for a number of lymphoid cells. May play an important role in
CC regulating lipid metabolism by synthesizing a corepressor that blocks
CC sterol regulatory element binding protein (SREBP) processing. In
CC testis, production of 25-hydroxycholesterol by macrophages may play a
CC role in Leydig cell differentiation. {ECO:0000250|UniProtKB:Q9Z0F5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + cholesterol + O2 = 25-hydroxycholesterol + A + H2O;
CC Xref=Rhea:RHEA:21104, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:42977; EC=1.14.99.38;
CC Evidence={ECO:0000250|UniProtKB:Q9Z0F5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21105;
CC Evidence={ECO:0000250|UniProtKB:Q9Z0F5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + H(+) + NADPH + O2 = 25-hydroxycholesterol + H2O
CC + NADP(+); Xref=Rhea:RHEA:46132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:42977, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:Q9Z0F5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46133;
CC Evidence={ECO:0000250|UniProtKB:Q9Z0F5};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q9Z0F5};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Z0F5}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Z0F5}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC086721; AAH86721.1; -; mRNA.
DR RefSeq; NP_001008652.1; NM_001008652.1.
DR AlphaFoldDB; Q5PRC0; -.
DR STRING; 7955.ENSDARP00000066438; -.
DR PaxDb; Q5PRC0; -.
DR Ensembl; ENSDART00000066439; ENSDARP00000066438; ENSDARG00000045190.
DR GeneID; 494109; -.
DR KEGG; dre:494109; -.
DR CTD; 9023; -.
DR ZFIN; ZDB-GENE-041212-81; ch25h.
DR eggNOG; KOG0873; Eukaryota.
DR GeneTree; ENSGT00940000162142; -.
DR HOGENOM; CLU_047036_5_1_1; -.
DR InParanoid; Q5PRC0; -.
DR OMA; YKYHKAT; -.
DR OrthoDB; 1493916at2759; -.
DR PhylomeDB; Q5PRC0; -.
DR TreeFam; TF314256; -.
DR Reactome; R-DRE-192105; Synthesis of bile acids and bile salts.
DR PRO; PR:Q5PRC0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000045190; Expressed in spleen and 14 other tissues.
DR ExpressionAtlas; Q5PRC0; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000254; F:C-4 methylsterol oxidase activity; IBA:GO_Central.
DR GO; GO:0001567; F:cholesterol 25-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0035754; P:B cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IDA:ZFIN.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..251
FT /note="Cholesterol 25-hydroxylase-like protein"
FT /id="PRO_0000226805"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 113..247
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 126..130
FT /note="Histidine box-1"
FT MOTIF 141..145
FT /note="Histidine box-2"
FT MOTIF 222..228
FT /note="Histidine box-3"
SQ SEQUENCE 251 AA; 29735 MW; 15315B70C824E279 CRC64;
MFGLQHIWDC ILQYEAQLRS PFFPVLFSIT VYLSFCLPFV LLDALSPKVE LIRRYKIQQK
ASVSWTMMWS CLALSLYNHV VYIFPLSVLH WYWRPVSYLA EAPGVLRVVW DLAACLLLFD
FQYFVWHLLH HKVPWLYRTF HKVHHKYTST FALATEYSGA WETLSLGFFA AVNPMLLGVH
PMTEMLFHML NMWLSVEDHC GYDLPWATHR LMPFGLYGGA PHHDVHHQKF KSNYAPYFTH
WDKLFGTLHF E
