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Lathosterol oxidase (EC 1.14.19.20) (C-5 sterol desaturase) (Delta(7)-sterol 5-desaturase) (Delta(7)-sterol C5(6)-desaturase) (Lathosterol 5-desaturase) (Sterol-C5-desaturase)

 SC5D_HUMAN              Reviewed;         299 AA.
O75845; O00119; Q6GTM5; Q9UK15;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-JUN-2018, entry version 158.
RecName: Full=Lathosterol oxidase;
EC=1.14.19.20;
AltName: Full=C-5 sterol desaturase;
AltName: Full=Delta(7)-sterol 5-desaturase;
AltName: Full=Delta(7)-sterol C5(6)-desaturase;
AltName: Full=Lathosterol 5-desaturase;
AltName: Full=Sterol-C5-desaturase;
Name=SC5D; Synonyms=SC5DL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8976377;
Matsushima M., Inazawa J., Takahashi E., Suzumori K., Nakamura Y.;
"Molecular cloning and mapping of a human cDNA(SC5DL) encoding a
protein homologous to fungal sterol-C5-desaturase.";
Cytogenet. Cell Genet. 74:252-254(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=B-cell;
PubMed=10344195; DOI=10.1023/A:1006113919172;
Husselstein T., Schaller H., Gachotte D., Benveniste P.;
"Delta7-sterol-C5-desaturase: molecular characterization and
functional expression of wild-type and mutant alleles.";
Plant Mol. Biol. 39:891-906(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=10786622; DOI=10.1016/S0167-4781(99)00248-1;
Nishi S., Nishino H., Ishibashi T.;
"cDNA cloning of the mammalian sterol C5-desaturase and the expression
in yeast mutant.";
Biochim. Biophys. Acta 1490:106-108(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Sugawara T.;
"Human sterol C5 desaturase promoter.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Kidney;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[10]
VARIANTS LATHST GLN-29 AND ASP-211.
PubMed=12189593; DOI=10.1086/342668;
Brunetti-Pierri N., Corso G., Rossi M., Ferrari P., Balli F.,
Rivasi F., Annunziata I., Ballabio A., Dello Russo A., Andria G.,
Parenti G.;
"Lathosterolosis, a novel multiple-malformation/mental retardation
syndrome due to deficiency of 3beta-hydroxysteroid-delta5-
desaturase.";
Am. J. Hum. Genet. 71:952-958(2002).
[11]
VARIANT LATHST SER-46.
PubMed=12812989; DOI=10.1093/hmg/ddg172;
Krakowiak P.A., Wassif C.A., Kratz L., Cozma D., Kovarova M.,
Harris G., Grinberg A., Yang Y., Hunter A.G.W., Tsokos M.,
Kelley R.I., Porter F.D.;
"Lathosterolosis: an inborn error of human and murine cholesterol
synthesis due to lathosterol 5-desaturase deficiency.";
Hum. Mol. Genet. 12:1631-1641(2003).
-!- FUNCTION: Catalyzes a dehydrogenation to introduce C5-6 double
bond into lathosterol.
-!- CATALYTIC ACTIVITY: A Delta(7)-sterol + 2 ferrocytochrome b5 +
O(2) + 2 H(+) = a Delta(5,7)-sterol + 2 ferricytochrome b5 + 2
H(2)O. {ECO:0000250|UniProtKB:Q9EQS5}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- DOMAIN: The histidine box domains may contain the active site
and/or be involved in metal ion binding.
-!- DISEASE: Lathosterolosis (LATHST) [MIM:607330]: Autosomal
recessive disorder characterized by a complex phenotype, including
multiple congenital anomalies, mental retardation, and liver
disease. {ECO:0000269|PubMed:12189593,
ECO:0000269|PubMed:12812989}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the sterol desaturase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D85181; BAA18970.1; -; mRNA.
EMBL; AF187981; AAF00544.1; -; mRNA.
EMBL; AB016247; BAA33729.1; -; mRNA.
EMBL; AB057650; BAB68218.1; -; Genomic_DNA.
EMBL; AK312634; BAG35518.1; -; mRNA.
EMBL; AK222686; BAD96406.1; -; mRNA.
EMBL; AK223141; BAD96861.1; -; mRNA.
EMBL; CH471065; EAW67520.1; -; Genomic_DNA.
EMBL; BC012333; AAH12333.1; -; mRNA.
EMBL; BC050427; AAH50427.1; -; mRNA.
CCDS; CCDS8435.1; -.
RefSeq; NP_001020127.1; NM_001024956.2.
RefSeq; NP_008849.2; NM_006918.4.
UniGene; Hs.287749; -.
ProteinModelPortal; O75845; -.
BioGrid; 112216; 16.
STRING; 9606.ENSP00000264027; -.
ChEMBL; CHEMBL3509588; -.
SwissLipids; SLP:000001259; -.
iPTMnet; O75845; -.
PhosphoSitePlus; O75845; -.
BioMuta; SC5D; -.
EPD; O75845; -.
PaxDb; O75845; -.
PeptideAtlas; O75845; -.
PRIDE; O75845; -.
ProteomicsDB; 50227; -.
TopDownProteomics; O75845; -.
DNASU; 6309; -.
Ensembl; ENST00000264027; ENSP00000264027; ENSG00000109929.
Ensembl; ENST00000392789; ENSP00000376539; ENSG00000109929.
GeneID; 6309; -.
KEGG; hsa:6309; -.
UCSC; uc001pxu.4; human.
CTD; 6309; -.
DisGeNET; 6309; -.
EuPathDB; HostDB:ENSG00000109929.9; -.
GeneCards; SC5D; -.
HGNC; HGNC:10547; SC5D.
HPA; HPA066283; -.
HPA; HPA070248; -.
MalaCards; SC5D; -.
MIM; 602286; gene.
MIM; 607330; phenotype.
neXtProt; NX_O75845; -.
OpenTargets; ENSG00000109929; -.
Orphanet; 46059; Lathosterolosis.
PharmGKB; PA34957; -.
eggNOG; KOG0872; Eukaryota.
eggNOG; COG3000; LUCA.
GeneTree; ENSGT00550000075101; -.
HOGENOM; HOG000200579; -.
HOVERGEN; HBG012628; -.
InParanoid; O75845; -.
KO; K00227; -.
OMA; FINGSAH; -.
OrthoDB; EOG091G0C85; -.
PhylomeDB; O75845; -.
TreeFam; TF300797; -.
BioCyc; MetaCyc:HS03271-MONOMER; -.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-6807047; Cholesterol biosynthesis via desmosterol.
Reactome; R-HSA-6807062; Cholesterol biosynthesis via lathosterol.
ChiTaRS; SC5D; human.
GeneWiki; Sterol-C5-desaturase-like; -.
GenomeRNAi; 6309; -.
PRO; PR:O75845; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000109929; -.
CleanEx; HS_SC5DL; -.
ExpressionAtlas; O75845; baseline and differential.
Genevisible; O75845; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0000248; F:C-5 sterol desaturase activity; EXP:Reactome.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0050046; F:lathosterol oxidase activity; IBA:GO_Central.
GO; GO:0033489; P:cholesterol biosynthetic process via desmosterol; TAS:Reactome.
GO; GO:0033490; P:cholesterol biosynthetic process via lathosterol; IBA:GO_Central.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; TAS:Reactome.
InterPro; IPR006694; Fatty_acid_hydroxylase.
Pfam; PF04116; FA_hydroxylase; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Endoplasmic reticulum; Iron;
Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
Phosphoprotein; Reference proteome; Steroid biosynthesis;
Steroid metabolism; Sterol biosynthesis; Sterol metabolism;
Transmembrane; Transmembrane helix.
CHAIN 1 299 Lathosterol oxidase.
/FTId=PRO_0000117028.
TRANSMEM 32 52 Helical. {ECO:0000255}.
TRANSMEM 79 99 Helical. {ECO:0000255}.
TRANSMEM 117 137 Helical. {ECO:0000255}.
TRANSMEM 186 206 Helical. {ECO:0000255}.
MOTIF 138 143 Histidine box-1.
MOTIF 151 155 Histidine box-2.
MOTIF 228 233 Histidine box-3.
MOD_RES 253 253 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
VARIANT 29 29 R -> Q (in LATHST; dbSNP:rs104894295).
{ECO:0000269|PubMed:12189593}.
/FTId=VAR_014423.
VARIANT 46 46 Y -> S (in LATHST; dbSNP:rs104894297).
{ECO:0000269|PubMed:12812989}.
/FTId=VAR_020829.
VARIANT 211 211 G -> D (in LATHST; dbSNP:rs104894296).
{ECO:0000269|PubMed:12189593}.
/FTId=VAR_014424.
CONFLICT 216 299 PQILQPFINGSAHHTDHHMFFDYNYGQYFTLWDRIGGSFKN
PSSFEGKGPLSYVKEMTEGKRSSHSGNGCKNEKLFNGEFTK
TE -> RMKNYSMESLQRLNRLLPSYS (in Ref. 1;
BAA18970). {ECO:0000305}.
CONFLICT 280 280 H -> P (in Ref. 3; BAA33729 and 4;
BAB68218). {ECO:0000305}.
SEQUENCE 299 AA; 35301 MW; 9EF8B20D522FAA56 CRC64;
MDLVLRVADY YFFTPYVYPA TWPEDDIFRQ AISLLIVTNV GAYILYFFCA TLSYYFVFDH
ALMKHPQFLK NQVRREIKFT VQALPWISIL TVALFLLEIR GYSKLHDDLG EFPYGLFELV
VSIISFLFFT DMFIYWIHRG LHHRLVYKRL HKPHHIWKIP TPFASHAFHP IDGFLQSLPY
HIYPFIFPLH KVVYLSLYIL VNIWTISIHD GDFRVPQILQ PFINGSAHHT DHHMFFDYNY
GQYFTLWDRI GGSFKNPSSF EGKGPLSYVK EMTEGKRSSH SGNGCKNEKL FNGEFTKTE


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