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Protein

Acyl-CoA desaturase

Gene

SCD

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

Functioni

Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O2 and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA.

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.

Cofactori

GO - Molecular functioni

  • iron ion binding Source: InterPro
  • stearoyl-CoA 9-desaturase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Iron

Enzyme and pathway databases

BRENDAi1.14.19.1. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase (EC:1.14.19.1)
Alternative name(s):
Delta(9)-desaturase
Short name:
Delta-9 desaturase
Fatty acid desaturase
Stearoyl-CoA desaturase
Gene namesi
Name:SCD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:10571. SCD.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7171CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei72 – 9322HelicalSequence AnalysisAdd
BLAST
Topological domaini94 – 1029LumenalSequence Analysis
Transmembranei103 – 11917HelicalSequence AnalysisAdd
BLAST
Topological domaini120 – 21697CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei217 – 23519HelicalSequence AnalysisAdd
BLAST
Topological domaini236 – 25015LumenalSequence AnalysisAdd
BLAST
Transmembranei251 – 27323HelicalSequence AnalysisAdd
BLAST
Topological domaini274 – 35986CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34984.

Polymorphism and mutation databases

BioMutaiSCD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Acyl-CoA desaturasePRO_0000185395Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00767.
PaxDbiO00767.
PRIDEiO00767.

PTM databases

PhosphoSiteiO00767.

Expressioni

Gene expression databases

BgeeiO00767.
GenevestigatoriO00767.

Organism-specific databases

HPAiHPA012107.

Interactioni

Protein-protein interaction databases

BioGridi112225. 6 interactions.
IntActiO00767. 2 interactions.
MINTiMINT-2997962.

Structurei

3D structure databases

ProteinModelPortaliO00767.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi120 – 1256Histidine box-1
Motifi157 – 1615Histidine box-2
Motifi298 – 3025Histidine 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 fatty acid desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1398.
GeneTreeiENSGT00530000063158.
HOVERGENiHBG003367.
InParanoidiO00767.
KOiK00507.
OMAiNKESECK.
OrthoDBiEOG7ZPNKS.
PhylomeDBiO00767.
TreeFamiTF313251.

Family and domain databases

InterProiIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00767-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAHLLQDDI SSSYTTTTTI TAPPSRVLQN GGDKLETMPL YLEDDIRPDI
60 70 80 90 100
KDDIYDPTYK DKEGPSPKVE YVWRNIILMS LLHLGALYGI TLIPTCKFYT
110 120 130 140 150
WLWGVFYYFV SALGITAGAH RLWSHRSYKA RLPLRLFLII ANTMAFQNDV
160 170 180 190 200
YEWARDHRAH HKFSETHADP HNSRRGFFFS HVGWLLVRKH PAVKEKGSTL
210 220 230 240 250
DLSDLEAEKL VMFQRRYYKP GLLMMCFILP TLVPWYFWGE TFQNSVFVAT
260 270 280 290 300
FLRYAVVLNA TWLVNSAAHL FGYRPYDKNI SPRENILVSL GAVGEGFHNY
310 320 330 340 350
HHSFPYDYSA SEYRWHINFT TFFIDCMAAL GLAYDRKKVS KAAILARIKR

TGDGNYKSG
Length:359
Mass (Da):41,523
Last modified:June 6, 2002 - v2
Checksum:iED56A63DBD850F05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51L → M in AAB30631 (PubMed:7909540).Curated
Sequence conflicti8 – 81D → E in AAB30631 (PubMed:7909540).Curated
Sequence conflicti25 – 262SR → PG in CAA73998 (Ref. 1) Curated
Sequence conflicti25 – 262SR → PG in AAB30631 (PubMed:7909540).Curated
Sequence conflicti237 – 2371F → C in AAB30631 (PubMed:7909540).Curated
Sequence conflicti269 – 2691H → L in BAD96582 (Ref. 5) Curated
Sequence conflicti320 – 3201T → N in CAA73998 (Ref. 1) Curated
Sequence conflicti326 – 3261C → W in CAA73998 (Ref. 1) Curated
Sequence conflicti333 – 3331A → T in CAA73998 (Ref. 1) Curated
Sequence conflicti356 – 3594Missing in AAH05807 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241M → L.4 Publications
Corresponds to variant rs2234970 [ dbSNP | Ensembl ].
VAR_025994

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13647 mRNA. Translation: CAA73998.1.
AF097514 mRNA. Translation: AAD29870.1.
AB032261 mRNA. Translation: BAA93510.1.
AK312312 mRNA. Translation: BAG35237.1.
AK222862 mRNA. Translation: BAD96582.1.
AL139819 Genomic DNA. Translation: CAH72823.1.
AL139819 Genomic DNA. Translation: CAH72824.1.
CH471066 Genomic DNA. Translation: EAW49829.1.
CH471066 Genomic DNA. Translation: EAW49830.1.
BC005807 mRNA. Translation: AAH05807.1.
BC062303 mRNA. Translation: AAH62303.1.
AF320307 Genomic DNA. Translation: AAK54510.1.
S70284 mRNA. Translation: AAB30631.1.
CCDSiCCDS7493.1.
PIRiI54779.
RefSeqiNP_005054.3. NM_005063.4.
UniGeneiHs.558396.

Genome annotation databases

EnsembliENST00000370355; ENSP00000359380; ENSG00000099194.
GeneIDi6319.
KEGGihsa:6319.
UCSCiuc001kqy.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13647 mRNA. Translation: CAA73998.1.
AF097514 mRNA. Translation: AAD29870.1.
AB032261 mRNA. Translation: BAA93510.1.
AK312312 mRNA. Translation: BAG35237.1.
AK222862 mRNA. Translation: BAD96582.1.
AL139819 Genomic DNA. Translation: CAH72823.1.
AL139819 Genomic DNA. Translation: CAH72824.1.
CH471066 Genomic DNA. Translation: EAW49829.1.
CH471066 Genomic DNA. Translation: EAW49830.1.
BC005807 mRNA. Translation: AAH05807.1.
BC062303 mRNA. Translation: AAH62303.1.
AF320307 Genomic DNA. Translation: AAK54510.1.
S70284 mRNA. Translation: AAB30631.1.
CCDSiCCDS7493.1.
PIRiI54779.
RefSeqiNP_005054.3. NM_005063.4.
UniGeneiHs.558396.

3D structure databases

ProteinModelPortaliO00767.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112225. 6 interactions.
IntActiO00767. 2 interactions.
MINTiMINT-2997962.

Chemistry

BindingDBiO00767.
ChEMBLiCHEMBL5555.

PTM databases

PhosphoSiteiO00767.

Polymorphism and mutation databases

BioMutaiSCD.

Proteomic databases

MaxQBiO00767.
PaxDbiO00767.
PRIDEiO00767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370355; ENSP00000359380; ENSG00000099194.
GeneIDi6319.
KEGGihsa:6319.
UCSCiuc001kqy.3. human.

Organism-specific databases

CTDi6319.
GeneCardsiGC10P102096.
H-InvDBHIX0009123.
HGNCiHGNC:10571. SCD.
HPAiHPA012107.
MIMi604031. gene.
neXtProtiNX_O00767.
PharmGKBiPA34984.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1398.
GeneTreeiENSGT00530000063158.
HOVERGENiHBG003367.
InParanoidiO00767.
KOiK00507.
OMAiNKESECK.
OrthoDBiEOG7ZPNKS.
PhylomeDBiO00767.
TreeFamiTF313251.

Enzyme and pathway databases

BRENDAi1.14.19.1. 2681.

Miscellaneous databases

ChiTaRSiSCD. human.
GeneWikiiStearoyl-CoA_desaturase-1.
GenomeRNAii6319.
NextBioi24520.
PROiO00767.
SOURCEiSearch...

Gene expression databases

BgeeiO00767.
GenevestigatoriO00767.

Family and domain databases

InterProiIPR005804. Fatty_acid_desaturase-1.
IPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PfamiPF00487. FA_desaturase. 1 hit.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and expression of a stearoyl CoA desaturase from human liver."
    Al-Jeryan L., McCord A., Pierotti A.R., Craft J.A.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Human stearoyl-CoA desaturase: alternative transcripts generated from a single gene by usage of tandem polyadenylation sites."
    Zhang L., Ge L., Parimoo S., Stenn K., Prouty S.M.
    Biochem. J. 340:255-264(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-224.
    Tissue: Brain, Liver and Skin.
  3. "Cloning, sequencing and expression of human stearoyl-CoA desaturase."
    Hoshino T., Ohtsu K.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-224.
  4. "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].
    Tissue: Cerebellum.
  5. 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: Liver.
  6. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-224.
  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], VARIANT LEU-224.
    Tissue: Mammary gland and Placenta.
  9. "Isolation and characterization of the human stearoyl-CoA desaturase gene promoter: requirement of a conserved CCAAT cis-element."
    Zhang L., Ge L., Tran T., Stenn K., Prouty S.M.
    Biochem. J. 357:183-193(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
  10. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
    Xu G., Shin S.B., Jaffrey S.R.
    Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-27.
    Tissue: Leukemic T-cell.
  11. "Partial characterization of a cDNA for human stearoyl-CoA desaturase and changes in its mRNA expression in some normal and malignant tissues."
    Li J., Ding S.-F., Habib N.A., Fermor B.F., Wood C.B., Gilmour R.S.
    Int. J. Cancer 57:348-352(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-239.
    Tissue: Adipose tissue.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACOD_HUMAN
AccessioniPrimary (citable) accession number: O00767
Secondary accession number(s): B2R5U0
, D3DR68, Q16150, Q53GR9, Q5W037, Q5W038, Q6GSS4, Q96KF6, Q9BS07, Q9Y695
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 6, 2002
Last modified: April 29, 2015
This is version 148 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.