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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

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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS01878-MONOMER.
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

HGNCiHGNC:10571. SCD.

Subcellular locationi

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

GO - Cellular componenti

  • endoplasmic reticulum Source: HPA
  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi6319.
MalaCardsiSCD.
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.
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. 16 interactors.
IntActiO00767. 8 interactors.
MINTiMINT-2997962.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZYOX-ray3.25A45-359[»]
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.
OMAiLIPTCKF.
OrthoDBiEOG091G0B5S.
PhylomeDBiO00767.
TreeFamiTF313251.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiIPR015876. Acyl-CoA_DS.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
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)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 → L.4 PublicationsCorresponds to variant rs2234970dbSNPEnsembl.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. 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.4. 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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZYOX-ray3.25A45-359[»]
ProteinModelPortaliO00767.
SMRiO00767.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112225. 16 interactors.
IntActiO00767. 8 interactors.
MINTiMINT-2997962.
STRINGi9606.ENSP00000359380.

Chemistry databases

BindingDBiO00767.
ChEMBLiCHEMBL5555.
SwissLipidsiSLP:000000465.

PTM databases

iPTMnetiO00767.
PhosphoSitePlusiO00767.
SwissPalmiO00767.

Polymorphism and mutation databases

BioMutaiSCD.

Proteomic databases

EPDiO00767.
MaxQBiO00767.
PaxDbiO00767.
PeptideAtlasiO00767.
PRIDEiO00767.
TopDownProteomicsiO00767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370355; ENSP00000359380; ENSG00000099194.
GeneIDi6319.
KEGGihsa:6319.
UCSCiuc001kqy.4. human.

Organism-specific databases

CTDi6319.
DisGeNETi6319.
GeneCardsiSCD.
H-InvDBHIX0009123.
HGNCiHGNC:10571. SCD.
HPAiHPA012107.
HPA063921.
MalaCardsiSCD.
MIMi604031. gene.
neXtProtiNX_O00767.
OpenTargetsiENSG00000099194.
PharmGKBiPA34984.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
GeneTreeiENSGT00530000063158.
HOVERGENiHBG003367.
InParanoidiO00767.
KOiK00507.
OMAiLIPTCKF.
OrthoDBiEOG091G0B5S.
PhylomeDBiO00767.
TreeFamiTF313251.

Enzyme and pathway databases

BioCyciZFISH:HS01878-MONOMER.
BRENDAi1.14.19.1. 2681.
ReactomeiR-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-75105. Fatty Acyl-CoA Biosynthesis.
SIGNORiO00767.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000099194.
GenevisibleiO00767. HS.

Family and domain databases

CDDicd03505. Delta9-FADS-like. 1 hit.
InterProiIPR015876. Acyl-CoA_DS.
IPR001522. FADS-1_CS.
[Graphical view]
PANTHERiPTHR11351. PTHR11351. 1 hit.
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 164 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

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

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 one 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.