ID   C25HL_CAEBR             Reviewed;         300 AA.
AC   Q618G2; A8XKF3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Cholesterol 25-hydroxylase-like protein;
DE            EC=1.14.99.-;
GN   ORFNames=CBG14675;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Probable sterol desaturase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR   EMBL; HE600983; CAP33127.1; -; Genomic_DNA.
DR   RefSeq; XP_002644688.1; XM_002644642.1.
DR   AlphaFoldDB; Q618G2; -.
DR   STRING; 6238.CBG14675; -.
DR   EnsemblMetazoa; CBG14675.1; CBG14675.1; WBGene00035097.
DR   GeneID; 8586684; -.
DR   KEGG; cbr:CBG_14675; -.
DR   CTD; 8586684; -.
DR   WormBase; CBG14675; CBP03614; WBGene00035097; -.
DR   eggNOG; KOG0873; Eukaryota.
DR   HOGENOM; CLU_047036_5_1_1; -.
DR   InParanoid; Q618G2; -.
DR   OMA; TTWGFMV; -.
DR   OrthoDB; 1493916at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
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:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR006694; Fatty_acid_hydroxylase.
DR   Pfam; PF04116; FA_hydroxylase; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Iron; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Metal-binding; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..300
FT                   /note="Cholesterol 25-hydroxylase-like protein"
FT                   /id="PRO_0000226807"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          135..266
FT                   /note="Fatty acid hydroxylase"
FT                   /evidence="ECO:0000255"
FT   MOTIF           148..152
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           163..167
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000250"
FT   MOTIF           242..248
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        9
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   300 AA;  36271 MW;  54B4747880118F53 CRC64;
     MLDLYPVHNF TVEQLEYEKN TRVLQPVWDW IKNGNEHILS SPLFPPFYAL SIDYTWVAVF
     TFIDLFLYDV PFFKNAKIQK DRVVTWDLMK KSLKLQGWNQ LLWIYPMALV QLIWVPDTEL
     PILAPTVFEM VSQLAIFFLA FDFTYFWFHY FNHKIKWLYR WCHSVHHMYS SPFAASAQHL
     HPFELFFVAT FITTVPWIFP THCLTYWLWF FVAQSVSYEV HIGYDFPFAL HRIFWFYSGA
     PAHDMHHLRP LTCFQPWFNY LDRLMGYHIT YEDLKKMTEA KFKKFGLYSV EDEKGLIKIN