C25HL_CAEEL
ID C25HL_CAEEL Reviewed; 300 AA.
AC Q20027;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cholesterol 25-hydroxylase-like protein;
DE EC=1.14.99.-;
GN ORFNames=F35C8.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
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; FO080312; CCD62784.1; -; Genomic_DNA.
DR PIR; T16255; T16255.
DR RefSeq; NP_508912.1; NM_076511.1.
DR AlphaFoldDB; Q20027; -.
DR BioGRID; 50045; 2.
DR DIP; DIP-27397N; -.
DR IntAct; Q20027; 1.
DR STRING; 6239.F35C8.5; -.
DR iPTMnet; Q20027; -.
DR EPD; Q20027; -.
DR PaxDb; Q20027; -.
DR PeptideAtlas; Q20027; -.
DR EnsemblMetazoa; F35C8.5.1; F35C8.5.1; WBGene00018036.
DR GeneID; 185268; -.
DR KEGG; cel:CELE_F35C8.5; -.
DR UCSC; F35C8.5; c. elegans.
DR CTD; 185268; -.
DR WormBase; F35C8.5; CE04497; WBGene00018036; -.
DR eggNOG; KOG0873; Eukaryota.
DR GeneTree; ENSGT00940000162142; -.
DR HOGENOM; CLU_047036_5_1_1; -.
DR InParanoid; Q20027; -.
DR OMA; TTWGFMV; -.
DR OrthoDB; 1493916at2759; -.
DR PhylomeDB; Q20027; -.
DR Reactome; R-CEL-192105; Synthesis of bile acids and bile salts.
DR PRO; PR:Q20027; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00018036; Expressed in larva and 2 other tissues.
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 1: Evidence at protein level;
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_0000226808"
FT TRANSMEM 54..73
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 192..212
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 MOTIF 163..167
FT /note="Histidine box-2"
FT MOTIF 242..248
FT /note="Histidine box-3"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
SQ SEQUENCE 300 AA; 36065 MW; 5FC8B659A4FD2B3F CRC64;
MLDLYPVQNL TVDQLEYEKN TRFLQPAWDW IKNGNEHILS SPLFPPFYAL SIDYTWVAVF
TFIDVFLCNV PFFKDAKIQK DRKVTWDLIK KSLKLQGWNQ LLWIYPMALV QLIWVPDTEL
PILAPTVFEM LSQLAIFFLA FDFTYFWFHY INHKVKWLYR WCHSVHHMYS SPFAASAQHL
HPFELFFVGT FITTIPWIFP THCLTYWIWF FIAQSVSYEV HIGYDFPFAL HRIFWFYSGA
PAHDMHHLRP LTCFQPWFNY LDRLMGYHIT YADLKKMTEA KFKKFGLYSA EDEKGLIKIN
