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Protein

Acyl-CoA desaturase

Gene

SCD

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

Functioni

Stearyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:15907797, PubMed:18765284). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:15907797, PubMed:18765284). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:15610069). Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity).By similarity3 Publications

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.3 Publications

Cofactori

Fe2+1 Publication1 PublicationNote: Expected to bind 2 Fe2+ ions per subunit, instead of the Zn2+ ions seen in the 3D-structure.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei75Substrate1 Publication1
Metal bindingi120Iron 11 Publication1
Metal bindingi125Iron 11 Publication1
Binding sitei148Substrate1 Publication1
Binding sitei155Substrate1 Publication1
Binding sitei156Substrate1 Publication1
Metal bindingi157Iron 11 Publication1
Metal bindingi160Iron 21 Publication1
Metal bindingi161Iron 11 Publication1
Binding sitei188Substrate1 Publication1
Binding sitei189Substrate1 Publication1
Binding sitei262Substrate1 Publication1
Metal bindingi269Iron 21 Publication1
Metal bindingi298Iron 21 Publication1
Metal bindingi301Iron 11 Publication1
Metal bindingi302Iron 21 Publication1

GO - Molecular functioni

  • iron ion binding Source: UniProtKB
  • oxidoreductase activity Source: UniProtKB
  • stearoyl-CoA 9-desaturase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandIron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.19.1 2681
ReactomeiR-HSA-2426168 Activation of gene expression by SREBF (SREBP)
R-HSA-75105 Fatty acyl-CoA biosynthesis
SIGNORiO00767

Chemistry databases

SwissLipidsiSLP:000000465

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase (EC:1.14.19.13 Publications)
Alternative name(s):
Delta(9)-desaturase
Short name:
Delta-9 desaturase
Fatty acid desaturase
Stearoyl-CoA desaturase1 Publication
Short name:
hSCD11 Publication
Gene namesi
Name:SCD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000099194.5
HGNCiHGNC:10571 SCD
MIMi604031 gene
neXtProtiNX_O00767

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 72Cytoplasmic1 PublicationAdd BLAST72
Transmembranei73 – 93Helical1 PublicationAdd BLAST21
Topological domaini94 – 97Lumenal1 Publication4
Transmembranei98 – 118Helical1 PublicationAdd BLAST21
Topological domaini119 – 217Cytoplasmic1 PublicationAdd BLAST99
Transmembranei218 – 237Helical1 PublicationAdd BLAST20
Topological domaini238 – 241Lumenal1 Publication4
Transmembranei242 – 263Helical1 PublicationAdd BLAST22
Topological domaini264 – 359Cytoplasmic1 PublicationAdd BLAST96

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi6319
OpenTargetsiENSG00000099194
PharmGKBiPA34984

Chemistry databases

ChEMBLiCHEMBL5555

Polymorphism and mutation databases

BioMutaiSCD

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001853951 – 359Acyl-CoA desaturaseAdd BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei198PhosphoserineCombined sources1
Modified residuei203PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO00767
MaxQBiO00767
PaxDbiO00767
PeptideAtlasiO00767
PRIDEiO00767
ProteomicsDBi48027
TopDownProteomicsiO00767

PTM databases

iPTMnetiO00767
PhosphoSitePlusiO00767
SwissPalmiO00767

Expressioni

Tissue specificityi

Detected in fetal liver, lung and brain. Highly expressed in adult adipose tissue, and at lower levels in adult brain and lung.1 Publication

Gene expression databases

BgeeiENSG00000099194
GenevisibleiO00767 HS

Organism-specific databases

HPAiHPA012107
HPA063921

Interactioni

Subunit structurei

May self-associate and form homodimers.1 Publication

Protein-protein interaction databases

BioGridi112225, 21 interactors
IntActiO00767, 43 interactors
MINTiO00767
STRINGi9606.ENSP00000359380

Chemistry databases

BindingDBiO00767

Structurei

Secondary structure

1359
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi57 – 59Combined sources3
Beta strandi63 – 65Combined sources3
Helixi73 – 91Combined sources19
Turni92 – 95Combined sources4
Helixi98 – 115Combined sources18
Helixi116 – 124Combined sources9
Helixi132 – 144Combined sources13
Helixi150 – 162Combined sources13
Turni163 – 165Combined sources3
Helixi173 – 175Combined sources3
Helixi177 – 181Combined sources5
Helixi183 – 185Combined sources3
Helixi192 – 196Combined sources5
Helixi203 – 206Combined sources4
Helixi209 – 216Combined sources8
Helixi218 – 226Combined sources9
Helixi228 – 237Combined sources10
Helixi242 – 247Combined sources6
Turni248 – 250Combined sources3
Helixi251 – 262Combined sources12
Turni263 – 266Combined sources4
Helixi267 – 269Combined sources3
Beta strandi271 – 273Combined sources3
Beta strandi278 – 280Combined sources3
Helixi286 – 291Combined sources6
Beta strandi292 – 294Combined sources3
Helixi298 – 303Combined sources6
Beta strandi308 – 313Combined sources6
Helixi319 – 329Combined sources11
Helixi341 – 346Combined sources6

3D structure databases

ProteinModelPortaliO00767
SMRiO00767
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi120 – 125Histidine box-1Curated6
Motifi157 – 161Histidine box-2Curated5
Motifi298 – 302Histidine box-3Curated5

Domaini

The histidine box domains are involved in binding the catalytic metal ions.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1600 Eukaryota
COG1398 LUCA
GeneTreeiENSGT00530000063158
HOVERGENiHBG003367
InParanoidiO00767
KOiK00507
OMAiHRRHHEC
OrthoDBiEOG091G0B5S
PhylomeDBiO00767
TreeFamiTF313251

Family and domain databases

CDDicd03505 Delta9-FADS-like, 1 hit
InterProiView protein in InterPro
IPR015876 Acyl-CoA_DS
IPR001522 FADS-1_CS
PANTHERiPTHR11351 PTHR11351, 1 hit
PRINTSiPR00075 FACDDSATRASE
PROSITEiView protein in PROSITE
PS00476 FATTY_ACID_DESATUR_1, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti5L → M in AAB30631 (PubMed:7909540).Curated1
Sequence conflicti8D → E in AAB30631 (PubMed:7909540).Curated1
Sequence conflicti25 – 26SR → PG in CAA73998 (Ref. 1) Curated2
Sequence conflicti25 – 26SR → PG in AAB30631 (PubMed:7909540).Curated2
Sequence conflicti237F → C in AAB30631 (PubMed:7909540).Curated1
Sequence conflicti269H → L in BAD96582 (Ref. 5) Curated1
Sequence conflicti320T → N in CAA73998 (Ref. 1) Curated1
Sequence conflicti326C → W in CAA73998 (Ref. 1) Curated1
Sequence conflicti333A → T in CAA73998 (Ref. 1) Curated1
Sequence conflicti356 – 359Missing in AAH05807 (PubMed:15489334).Curated4

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025994224M → L4 PublicationsCorresponds to variant dbSNP:rs2234970Ensembl.1

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 No translation available.
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.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

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 historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 6, 2002
Last modified: July 18, 2018
This is version 176 of the entry and version 2 of the sequence. See 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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