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O75845

- SC5D_HUMAN

UniProt

O75845 - SC5D_HUMAN

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Protein

Lathosterol oxidase

Gene

SC5D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol.

Catalytic activityi

5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O2 = cholesta-5,7-dien-3-beta-ol + NAD(P)+ + 2 H2O.

Cofactori

Iron.By similarity

GO - Molecular functioni

  1. C-5 sterol desaturase activity Source: ProtInc
  2. iron ion binding Source: InterPro
  3. lathosterol oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cholesterol biosynthetic process Source: Reactome
  2. cholesterol biosynthetic process via lathosterol Source: Ensembl
  3. fatty acid biosynthetic process Source: InterPro
  4. lipid metabolic process Source: ProtInc
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

Iron, NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS03271-MONOMER.
ReactomeiREACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Lathosterol oxidase (EC:1.14.21.6)
Alternative name(s):
C-5 sterol desaturase
Delta(7)-sterol 5-desaturase
Lathosterol 5-desaturase
Sterol-C5-desaturase
Gene namesi
Name:SC5D
Synonyms:SC5DL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:10547. SC5D.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Lathosterolosis (LATHST) [MIM:607330]: Autosomal recessive disorder characterized by a complex phenotype, including multiple congenital anomalies, mental retardation, and liver disease.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291R → Q in LATHST. 1 Publication
VAR_014423
Natural varianti46 – 461Y → S in LATHST. 1 Publication
VAR_020829
Natural varianti211 – 2111G → D in LATHST. 1 Publication
VAR_014424

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi607330. phenotype.
Orphaneti46059. Lathosterolosis.
PharmGKBiPA34957.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Lathosterol oxidasePRO_0000117028Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei253 – 2531Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO75845.
PRIDEiO75845.

PTM databases

PhosphoSiteiO75845.

Expressioni

Gene expression databases

BgeeiO75845.
CleanExiHS_SC5DL.
ExpressionAtlasiO75845. baseline and differential.
GenevestigatoriO75845.

Interactioni

Protein-protein interaction databases

BioGridi112216. 5 interactions.
STRINGi9606.ENSP00000264027.

Structurei

3D structure databases

ProteinModelPortaliO75845.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei32 – 5221HelicalSequence AnalysisAdd
BLAST
Transmembranei79 – 9921HelicalSequence AnalysisAdd
BLAST
Transmembranei117 – 13721HelicalSequence AnalysisAdd
BLAST
Transmembranei186 – 20621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi138 – 1436Histidine box-1
Motifi151 – 1555Histidine box-2
Motifi228 – 2336Histidine box-3

Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similaritiesi

Belongs to the sterol desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3000.
GeneTreeiENSGT00550000075101.
HOGENOMiHOG000200579.
HOVERGENiHBG012628.
InParanoidiO75845.
KOiK00227.
OMAiFFCATLS.
OrthoDBiEOG7NSB2T.
PhylomeDBiO75845.
TreeFamiTF300797.

Family and domain databases

InterProiIPR006694. Fatty_acid_hydroxylase.
[Graphical view]
PfamiPF04116. FA_hydroxylase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75845-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDLVLRVADY YFFTPYVYPA TWPEDDIFRQ AISLLIVTNV GAYILYFFCA
60 70 80 90 100
TLSYYFVFDH ALMKHPQFLK NQVRREIKFT VQALPWISIL TVALFLLEIR
110 120 130 140 150
GYSKLHDDLG EFPYGLFELV VSIISFLFFT DMFIYWIHRG LHHRLVYKRL
160 170 180 190 200
HKPHHIWKIP TPFASHAFHP IDGFLQSLPY HIYPFIFPLH KVVYLSLYIL
210 220 230 240 250
VNIWTISIHD GDFRVPQILQ PFINGSAHHT DHHMFFDYNY GQYFTLWDRI
260 270 280 290
GGSFKNPSSF EGKGPLSYVK EMTEGKRSSH SGNGCKNEKL FNGEFTKTE
Length:299
Mass (Da):35,301
Last modified:January 23, 2007 - v2
Checksum:i9EF8B20D522FAA56
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 29984PQILQ…FTKTE → RMKNYSMESLQRLNRLLPSY S in BAA18970. (PubMed:8976377)CuratedAdd
BLAST
Sequence conflicti280 – 2801H → P in BAA33729. (PubMed:10786622)Curated
Sequence conflicti280 – 2801H → P in BAB68218. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291R → Q in LATHST. 1 Publication
VAR_014423
Natural varianti46 – 461Y → S in LATHST. 1 Publication
VAR_020829
Natural varianti211 – 2111G → D in LATHST. 1 Publication
VAR_014424

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D85181 mRNA. Translation: BAA18970.1.
AF187981 mRNA. Translation: AAF00544.1.
AB016247 mRNA. Translation: BAA33729.1.
AB057650 Genomic DNA. Translation: BAB68218.1.
AK312634 mRNA. Translation: BAG35518.1.
AK222686 mRNA. Translation: BAD96406.1.
AK223141 mRNA. Translation: BAD96861.1.
CH471065 Genomic DNA. Translation: EAW67520.1.
BC012333 mRNA. Translation: AAH12333.1.
BC050427 mRNA. Translation: AAH50427.1.
CCDSiCCDS8435.1.
RefSeqiNP_001020127.1. NM_001024956.2.
NP_008849.2. NM_006918.4.
UniGeneiHs.287749.

Genome annotation databases

EnsembliENST00000264027; ENSP00000264027; ENSG00000109929.
ENST00000392789; ENSP00000376539; ENSG00000109929.
GeneIDi6309.
KEGGihsa:6309.
UCSCiuc001pxu.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D85181 mRNA. Translation: BAA18970.1 .
AF187981 mRNA. Translation: AAF00544.1 .
AB016247 mRNA. Translation: BAA33729.1 .
AB057650 Genomic DNA. Translation: BAB68218.1 .
AK312634 mRNA. Translation: BAG35518.1 .
AK222686 mRNA. Translation: BAD96406.1 .
AK223141 mRNA. Translation: BAD96861.1 .
CH471065 Genomic DNA. Translation: EAW67520.1 .
BC012333 mRNA. Translation: AAH12333.1 .
BC050427 mRNA. Translation: AAH50427.1 .
CCDSi CCDS8435.1.
RefSeqi NP_001020127.1. NM_001024956.2.
NP_008849.2. NM_006918.4.
UniGenei Hs.287749.

3D structure databases

ProteinModelPortali O75845.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112216. 5 interactions.
STRINGi 9606.ENSP00000264027.

PTM databases

PhosphoSitei O75845.

Proteomic databases

PaxDbi O75845.
PRIDEi O75845.

Protocols and materials databases

DNASUi 6309.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264027 ; ENSP00000264027 ; ENSG00000109929 .
ENST00000392789 ; ENSP00000376539 ; ENSG00000109929 .
GeneIDi 6309.
KEGGi hsa:6309.
UCSCi uc001pxu.3. human.

Organism-specific databases

CTDi 6309.
GeneCardsi GC11P121163.
HGNCi HGNC:10547. SC5D.
MIMi 602286. gene.
607330. phenotype.
neXtProti NX_O75845.
Orphaneti 46059. Lathosterolosis.
PharmGKBi PA34957.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3000.
GeneTreei ENSGT00550000075101.
HOGENOMi HOG000200579.
HOVERGENi HBG012628.
InParanoidi O75845.
KOi K00227.
OMAi FFCATLS.
OrthoDBi EOG7NSB2T.
PhylomeDBi O75845.
TreeFami TF300797.

Enzyme and pathway databases

BioCyci MetaCyc:HS03271-MONOMER.
Reactomei REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.

Miscellaneous databases

ChiTaRSi SC5DL. human.
GeneWikii Sterol-C5-desaturase-like.
GenomeRNAii 6309.
NextBioi 24491.
PROi O75845.
SOURCEi Search...

Gene expression databases

Bgeei O75845.
CleanExi HS_SC5DL.
ExpressionAtlasi O75845. baseline and differential.
Genevestigatori O75845.

Family and domain databases

InterProi IPR006694. Fatty_acid_hydroxylase.
[Graphical view ]
Pfami PF04116. FA_hydroxylase. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and mapping of a human cDNA(SC5DL) encoding a protein homologous to fungal sterol-C5-desaturase."
    Matsushima M., Inazawa J., Takahashi E., Suzumori K., Nakamura Y.
    Cytogenet. Cell Genet. 74:252-254(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Delta7-sterol-C5-desaturase: molecular characterization and functional expression of wild-type and mutant alleles."
    Husselstein T., Schaller H., Gachotte D., Benveniste P.
    Plant Mol. Biol. 39:891-906(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: B-cell.
  3. "cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant."
    Nishi S., Nishino H., Ishibashi T.
    Biochim. Biophys. Acta 1490:106-108(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  4. "Human sterol C5 desaturase promoter."
    Sugawara T.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. 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
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Kidney.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Lathosterolosis, a novel multiple-malformation/mental retardation syndrome due to deficiency of 3beta-hydroxysteroid-delta5-desaturase."
    Brunetti-Pierri N., Corso G., Rossi M., Ferrari P., Balli F., Rivasi F., Annunziata I., Ballabio A., Dello Russo A., Andria G., Parenti G.
    Am. J. Hum. Genet. 71:952-958(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LATHST GLN-29 AND ASP-211.
  11. "Lathosterolosis: an inborn error of human and murine cholesterol synthesis due to lathosterol 5-desaturase deficiency."
    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.
    Hum. Mol. Genet. 12:1631-1641(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LATHST SER-46.

Entry informationi

Entry nameiSC5D_HUMAN
AccessioniPrimary (citable) accession number: O75845
Secondary accession number(s): O00119, Q6GTM5, Q9UK15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3