ID   C25L1_DANRE             Reviewed;         282 AA.
AC   Q567X1; Q1LX56;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cholesterol 25-hydroxylase-like protein 1, member 1;
DE            EC=1.14.99.-;
GN   Name=ch25hl1.1; ORFNames=si:dkey-24l11.8, zgc:110696;
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 GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May catalyze the formation of 25-hydroxycholesterol from
CC       cholesterol. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR   EMBL; BX470164; CAK10821.1; -; Genomic_DNA.
DR   EMBL; BC092984; AAH92984.1; -; mRNA.
DR   RefSeq; NP_001017865.1; NM_001017865.1.
DR   AlphaFoldDB; Q567X1; -.
DR   STRING; 7955.ENSDARP00000057552; -.
DR   PaxDb; Q567X1; -.
DR   Ensembl; ENSDART00000057553; ENSDARP00000057552; ENSDARG00000039381.
DR   Ensembl; ENSDART00000181825; ENSDARP00000147438; ENSDARG00000113169.
DR   Ensembl; ENSDART00000187833; ENSDARP00000145701; ENSDARG00000109469.
DR   GeneID; 336673; -.
DR   KEGG; dre:336673; -.
DR   CTD; 336673; -.
DR   ZFIN; ZDB-GENE-030131-8617; ch25hl1.1.
DR   eggNOG; KOG0873; Eukaryota.
DR   GeneTree; ENSGT00940000163793; -.
DR   HOGENOM; CLU_047036_5_1_1; -.
DR   InParanoid; Q567X1; -.
DR   OMA; QLYRWIH; -.
DR   OrthoDB; 1493916at2759; -.
DR   PhylomeDB; Q567X1; -.
DR   TreeFam; TF353265; -.
DR   PRO; PR:Q567X1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 18.
DR   Bgee; ENSDARG00000039381; Expressed in zone of skin and 11 other tissues.
DR   ExpressionAtlas; Q567X1; baseline.
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:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR   GO; GO:0008203; P:cholesterol metabolic process; 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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW   Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..282
FT                   /note="Cholesterol 25-hydroxylase-like protein 1, member 1"
FT                   /id="PRO_0000226806"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          133..265
FT                   /note="Fatty acid hydroxylase"
FT                   /evidence="ECO:0000255"
FT   MOTIF           144..148
FT                   /note="Histidine box-1"
FT   MOTIF           159..163
FT                   /note="Histidine box-2"
FT   MOTIF           240..246
FT                   /note="Histidine box-3"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        20
FT                   /note="V -> L (in Ref. 2; AAH92984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79
FT                   /note="R -> S (in Ref. 2; AAH92984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109
FT                   /note="V -> M (in Ref. 2; AAH92984)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   282 AA;  32343 MW;  903ADC0DB02FB33C CRC64;
     MWNISEVVFQ LPTSSASDRV LQPLWDYLLL RHYTLISSPF FPVLLAFSSY IIFSVPFAVL
     DVLGEKAPLF KYKIQKDRRP TVGMMLRTLW TAVYNHLVFV LPAVLITNVV MPMPPLPTVA
     PTVWEMFSGG LGALLVFDTQ YFLWHMVHHK NPHLYRWVHA IHHDYISPFS WSTQHLSGVE
     LMTVGFWSNI DPILLKCHPL TVWTLTVYSI WMSVEDHIGY DLPFSPGHLV PFGLLGGAMA
     HDMHHQKPSS NFAPFFSHWD KIFGTAITVK LTQKSEKEKQ VA