SC5D_MOUSE
ID SC5D_MOUSE Reviewed; 299 AA.
AC O88822; Q8BGI0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Lathosterol oxidase;
DE EC=1.14.19.20;
DE AltName: Full=C-5 sterol desaturase;
DE AltName: Full=Delta(7)-sterol 5-desaturase;
DE AltName: Full=Delta(7)-sterol C5(6)-desaturase;
DE AltName: Full=Lathosterol 5-desaturase;
DE AltName: Full=Sterol-C5-desaturase;
GN Name=Sc5d; Synonyms=Sc5dl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=10786622; DOI=10.1016/s0167-4781(99)00248-1;
RA Nishi S., Nishino H., Ishibashi T.;
RT "cDNA cloning of the mammalian sterol C5-desaturase and the expression in
RT yeast mutant.";
RL Biochim. Biophys. Acta 1490:106-108(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Catalyzes a dehydrogenation to introduce C5-6 double bond
CC into lathosterol in cholesterol biosynthesis.
CC {ECO:0000250|UniProtKB:O75845}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a Delta(7)-sterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a
CC Delta(5),Delta(7)-sterol + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:54320, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:138130,
CC ChEBI:CHEBI:138131; EC=1.14.19.20;
CC Evidence={ECO:0000250|UniProtKB:Q9EQS5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54321;
CC Evidence={ECO:0000250|UniProtKB:Q9EQS5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + lathosterol + O2 = 7-
CC dehydrocholesterol + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46556, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17168, ChEBI:CHEBI:17759, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=1.14.19.20;
CC Evidence={ECO:0000250|UniProtKB:O75845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46557;
CC Evidence={ECO:0000250|UniProtKB:O75845};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; AB016248; BAA33730.1; -; mRNA.
DR EMBL; AK043825; BAC31666.1; -; mRNA.
DR EMBL; AK077670; BAC36944.1; -; mRNA.
DR EMBL; AC160051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23086.1; -.
DR RefSeq; NP_766357.1; NM_172769.2.
DR RefSeq; XP_006510316.1; XM_006510253.2.
DR AlphaFoldDB; O88822; -.
DR BioGRID; 231634; 3.
DR STRING; 10090.ENSMUSP00000057354; -.
DR iPTMnet; O88822; -.
DR PhosphoSitePlus; O88822; -.
DR EPD; O88822; -.
DR PaxDb; O88822; -.
DR PeptideAtlas; O88822; -.
DR PRIDE; O88822; -.
DR ProteomicsDB; 253403; -.
DR Antibodypedia; 45921; 34 antibodies from 14 providers.
DR DNASU; 235293; -.
DR Ensembl; ENSMUST00000052725; ENSMUSP00000057354; ENSMUSG00000032018.
DR Ensembl; ENSMUST00000169609; ENSMUSP00000130438; ENSMUSG00000032018.
DR GeneID; 235293; -.
DR KEGG; mmu:235293; -.
DR UCSC; uc009par.1; mouse.
DR CTD; 6309; -.
DR MGI; MGI:1353611; Sc5d.
DR VEuPathDB; HostDB:ENSMUSG00000032018; -.
DR eggNOG; KOG0872; Eukaryota.
DR GeneTree; ENSGT00550000075101; -.
DR HOGENOM; CLU_047036_2_2_1; -.
DR InParanoid; O88822; -.
DR OMA; HTLHHMY; -.
DR OrthoDB; 1249774at2759; -.
DR PhylomeDB; O88822; -.
DR TreeFam; TF300797; -.
DR BRENDA; 1.14.19.20; 3474.
DR Reactome; R-MMU-6807047; Cholesterol biosynthesis via desmosterol.
DR Reactome; R-MMU-6807062; Cholesterol biosynthesis via lathosterol.
DR BioGRID-ORCS; 235293; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Sc5d; mouse.
DR PRO; PR:O88822; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O88822; protein.
DR Bgee; ENSMUSG00000032018; Expressed in left lobe of liver and 259 other tissues.
DR ExpressionAtlas; O88822; baseline and differential.
DR Genevisible; O88822; MM.
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:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000248; F:C-5 sterol desaturase activity; ISO:MGI.
DR GO; GO:0050046; F:delta7-sterol 5(6)-desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0033490; P:cholesterol biosynthetic process via lathosterol; ISO:MGI.
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; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..299
FT /note="Lathosterol oxidase"
FT /id="PRO_0000117029"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 124..252
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT REGION 280..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 138..143
FT /note="Histidine box-1"
FT MOTIF 151..155
FT /note="Histidine box-2"
FT MOTIF 228..233
FT /note="Histidine box-3"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75845"
FT CONFLICT 136
FT /note="W -> R (in Ref. 1; BAA33730)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="G -> S (in Ref. 1; BAA33730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 35062 MW; 96F3AFF61F7ED707 CRC64;
MDLVLSAADY YFFTPYVYPA TWPEDNIIRQ TISLLIVTNL GAYILYFFCA TLSYYFVYDH
SLMKHPQFLK NQVSREIVFT VKSLPWISIP TVSLFLLELR GYSKLYDDIG DFPNGWIHLM
VSVVSFLFFT DMLIYWIHRG LHHRLVYKRI HKPHHIWKIP TPFASHAFHP VDGFLQSLPY
HIYPFVFPLH KVVYLGLYVL VNVWTISIHD GDFRVPQILR PFINGSAHHT DHHMFFDYNY
GQYFTLWDRI GGSFKHPSSF EGKGPHSYVK NMTEKESNSF AENGCKGKKV GNGEFTKNK
