Scd1

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:2892838, PubMed:7947684). 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:2892838, PubMed:7947684). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. 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 (PubMed:7947684). Required for normal development of sebaceous glands. Required for the biosynthesis of normal levels of Delta-9 unsaturated fatty acids and 1-alkyl-2,3-diacylglycerol in the Harderian gland. Required for normal production of meibum, an oily material that prevents drying of the cornea (By similarity).By similarity2 Publications

Miscellaneous

Desaturase has a half-life of only 4 hours.

Catalytic activityⁱ

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

Cofactorⁱ

Fe²⁺2 PublicationsNote: Expected to bind 2 Fe²⁺ ions per subunit.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	74	SubstrateBy similarity	1
Metal bindingⁱ	119	Iron 1By similarity	1
Metal bindingⁱ	124	Iron 1By similarity	1
Binding siteⁱ	147	SubstrateBy similarity	1
Binding siteⁱ	154	SubstrateBy similarity	1
Binding siteⁱ	155	SubstrateBy similarity	1
Metal bindingⁱ	156	Iron 1By similarity	1
Metal bindingⁱ	159	Iron 2By similarity	1
Metal bindingⁱ	160	Iron 1By similarity	1
Binding siteⁱ	187	SubstrateBy similarity	1
Binding siteⁱ	188	SubstrateBy similarity	1
Binding siteⁱ	261	SubstrateBy similarity	1
Metal bindingⁱ	268	Iron 2By similarity	1
Metal bindingⁱ	297	Iron 2By similarity	1
Metal bindingⁱ	300	Iron 1By similarity	1
Metal bindingⁱ	301	Iron 2By similarity	1

GO - Molecular functionⁱ

iron ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 2892838
oxidoreductase activity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 7947684
palmitoyl-CoA 9-desaturase activity Source: Ensembl
stearoyl-CoA 9-desaturase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 2892838

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

brown fat cell differentiation Source: Ensembl
cholesterol esterification Source: Ensembl
defense response to Gram-positive bacterium Source: Ensembl
fatty acid biosynthetic process
Source: RGD
Traceable author statementⁱ
- 12896875
lipid biosynthetic process
Source: RGD
Inferred from expression patternⁱ
- 12896875
monounsaturated fatty acid biosynthetic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
negative regulation of growth of symbiont in host Source: Ensembl
positive regulation of cold-induced thermogenesis
Source: YuBioLab
Inferred from sequence or structural similarityⁱ
- 15210843
- 19429677
regulation of water loss via skin Source: Ensembl
response to fatty acid
Source: UniProtKB
Inferred from direct assayⁱ
- 1982442
tarsal gland development Source: Ensembl
triglyceride metabolic process Source: Ensembl
unsaturated fatty acid biosynthetic process
Source: UniProtKB
Inferred from direct assayⁱ
- 2892838
white fat cell differentiation Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
Ligand	Iron, Metal-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-14123
BRENDAⁱ	1.14.19.1 5301
Reactomeⁱ	R-RNO-75105 Fatty acyl-CoA biosynthesis

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Acyl-CoA desaturase 1 (EC:1.14.19.12 Publications) Alternative name(s): Delta(9)-desaturase 1Curated Short name: Delta-9 desaturase 1Curated Fatty acid desaturase 1 Stearoyl-CoA desaturase 11 Publication
Gene namesⁱ	Name:Scd1 Synonyms:Scd
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 1

Organism-specific databases

Rat genome database More...RGDⁱ	621176 Scd1

RGDⁱ

621176 Scd1

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 71	CytoplasmicBy similarityAdd BLAST	71
Transmembraneⁱ	72 – 92	HelicalBy similarityAdd BLAST	21
Topological domainⁱ	93 – 96	LumenalBy similarity	4
Transmembraneⁱ	97 – 117	HelicalBy similarityAdd BLAST	21
Topological domainⁱ	118 – 216	CytoplasmicBy similarityAdd BLAST	99
Transmembraneⁱ	217 – 236	HelicalBy similarityAdd BLAST	20
Topological domainⁱ	237 – 240	LumenalBy similarity	4
Transmembraneⁱ	241 – 262	HelicalBy similarityAdd BLAST	22
Topological domainⁱ	263 – 358	CytoplasmicBy similarityAdd BLAST	96

Keywords - Cellular componentⁱ

Endoplasmic reticulum, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	119	H → A: Abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	124	H → A: Abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	156	H → A: Abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	157	R → N: No effect on enzyme activity. 1 Publication	1
Mutagenesisⁱ	159	H → A: Abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	160	H → A: Abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	166	H → A: No effect on enzyme activity. 1 Publication	1
Mutagenesisⁱ	170	H → A: No effect on enzyme activity; when associated with H-173. 1 Publication	1
Mutagenesisⁱ	173	R → H: No effect on enzyme activity; when associated with A-170. 1 Publication	1
Mutagenesisⁱ	297	H → A: Abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	300	H → A: Abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	301	H → A: Abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	315	H → A: No effect on enzyme activity. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL5424

ChEMBLⁱ

CHEMBL5424

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000185400	1 – 358	Acyl-CoA desaturase 1Add BLAST		358

Proteomic databases

PaxDbⁱ	P07308
PeptideAtlas More...PeptideAtlasⁱ	P07308
PRIDEⁱ	P07308

PTM databases

iPTMnetⁱ	P07308
PhosphoSitePlusⁱ	P07308

Expressionⁱ

Tissue specificityⁱ

Detected in liver (at protein level) (PubMed:2892838). Detected in adipose tissue. Detected in liver when rats are kept on a fat-free diet, but not when their food contains unsaturated fatty acids.1 Publication

Inductionⁱ

Up-regulated in liver in the absence of dietary unsaturated fatty acids(PubMed:1982442). Expression in adipose tissue seems to be constitutive (PubMed:1982442).1 Publication

Gene expression databases

Bgeeⁱ	ENSRNOG00000013552 Expressed in 10 organ(s), highest expression level in liver
Genevisibleⁱ	P07308 RN

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	251497, 1 interactor
STRINGⁱ	10116.ENSRNOP00000018447

Chemistry databases

BindingDBⁱ

P07308

Structureⁱ

3D structure databases

SMRⁱ	P07308
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Motif

Feature key	Position(s)	DescriptionActions	Length
Motifⁱ	119 – 124	Histidine box-1Curated	6
Motifⁱ	156 – 160	Histidine box-2Curated	5
Motifⁱ	297 – 301	Histidine box-3Curated	5

Domainⁱ

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

Sequence similaritiesⁱ

Belongs to the fatty acid desaturase type 1 family.Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG1600 Eukaryota COG1398 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063158
HOGENOMⁱ	HOG000270352
HOVERGENⁱ	HBG003367
InParanoidⁱ	P07308
KEGG Orthology (KO) More...KOⁱ	K00507
OMAⁱ	RNCWWVA
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0B5S

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd03505 Delta9-FADS-like, 1 hit
InterProⁱ	View protein in InterPro IPR015876 Acyl-CoA_DS IPR005804 FA_desaturase_dom IPR001522 FADS-1_CS
PANTHERⁱ	PTHR11351 PTHR11351, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00487 FA_desaturase, 1 hit
PRINTSⁱ	PR00075 FACDDSATRASE
PROSITEⁱ	View protein in PROSITE PS00476 FATTY_ACID_DESATUR_1, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P07308-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MPAHMLQEIS SSYTTTTTIT EPPSGNLQNG REKMKKVPLY LEEDIRPEMR 
        60         70         80         90        100
EDIHDPSYQD EEGPPPKLEY VWRNIILMAL LHVGALYGIT LIPSSKVYTL 
       110        120        130        140        150
LWGIFYYLIS ALGITAGAHR LWSHRTYKAR LPLRIFLIIA NTMAFQNDVY 
       160        170        180        190        200
EWARDHRAHH KFSETHADPH NSRRGFFFSH VGWLLVRKHP AVKEKGGKLD 
       210        220        230        240        250
MSDLKAEKLV MFQRRYYKPG LLLMCFILPT LVPWYCWGET FLHSLFVSTF 
       260        270        280        290        300
LRYTLVLNAT WLVNSAAHLY GYRPYDKNIQ SRENILVSLG AVGEGFHNYH 
       310        320        330        340        350
HAFPYDYSAS EYRWHINFTT FFIDCMAALG LAYDRKKVSK AAVLARIKRT 

GDGSHKSS

Length:358

Mass (Da):41,467

Last modified:November 23, 2004 - v2

Checksum:ⁱB4C960A969B63774

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	291	A → S in AAA42116 (PubMed:2428815).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J02585 mRNA Translation: AAA42116.1 AF509568 mRNA Translation: AAM34745.1 AF509569 mRNA Translation: AAM34746.1
PIRⁱ	A24699
NCBI Reference Sequences More...RefSeqⁱ	NP_631931.2, NM_139192.2 XP_006231495.1, XM_006231433.2
UniGeneⁱ	Rn.1023

Genome annotation databases

Ensemblⁱ	ENSRNOT00000018447; ENSRNOP00000018447; ENSRNOG00000013552
GeneIDⁱ	246074
KEGGⁱ	rno:246074

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P07308	Acyl-CoA desaturase 1	)	MOUSE		355	UniRef90_P13516
Stearoyl-CoA desaturase 1		MESAU		358
Uncharacterized protein		NEOLE		358
UPI00042AD430		PERMB		358
UPI000A3173FE		MUSCR		358
+5

Protein	Similar proteins		Species	Score	Length	Source
P07308	Acyl-CoA desaturase 1	)	MOUSE		355	UniRef50_P13516
Acyl-CoA desaturase (Fragment)		PIG		334
Uncharacterized protein		NEOLE		358
Stearoyl-CoA desaturase 1		MESAU		358
Stearoyl-CoA desaturase 1		ANSCY		357
+93

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J02585 mRNA Translation: AAA42116.1 AF509568 mRNA Translation: AAM34745.1 AF509569 mRNA Translation: AAM34746.1
PIRⁱ	A24699
RefSeqⁱ	NP_631931.2, NM_139192.2 XP_006231495.1, XM_006231433.2
UniGeneⁱ	Rn.1023

3D structure databases

SMRⁱ	P07308
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	251497, 1 interactor
STRINGⁱ	10116.ENSRNOP00000018447

Chemistry databases

BindingDBⁱ	P07308
ChEMBLⁱ	CHEMBL5424

PTM databases

iPTMnetⁱ	P07308
PhosphoSitePlusⁱ	P07308

Proteomic databases

PaxDbⁱ	P07308
PeptideAtlasⁱ	P07308
PRIDEⁱ	P07308

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSRNOT00000018447; ENSRNOP00000018447; ENSRNOG00000013552
GeneIDⁱ	246074
KEGGⁱ	rno:246074

Organism-specific databases

CTDⁱ	6319
RGDⁱ	621176 Scd1

Phylogenomic databases

eggNOGⁱ	KOG1600 Eukaryota COG1398 LUCA
GeneTreeⁱ	ENSGT00530000063158
HOGENOMⁱ	HOG000270352
HOVERGENⁱ	HBG003367
InParanoidⁱ	P07308
KOⁱ	K00507
OMAⁱ	RNCWWVA
OrthoDBⁱ	EOG091G0B5S

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-14123
BRENDAⁱ	1.14.19.1 5301
Reactomeⁱ	R-RNO-75105 Fatty acyl-CoA biosynthesis

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P07308

PROⁱ

PR:P07308

Gene expression databases

Bgeeⁱ	ENSRNOG00000013552 Expressed in 10 organ(s), highest expression level in liver
Genevisibleⁱ	P07308 RN

Family and domain databases

CDDⁱ	cd03505 Delta9-FADS-like, 1 hit
InterProⁱ	View protein in InterPro IPR015876 Acyl-CoA_DS IPR005804 FA_desaturase_dom IPR001522 FADS-1_CS
PANTHERⁱ	PTHR11351 PTHR11351, 1 hit
Pfamⁱ	View protein in Pfam PF00487 FA_desaturase, 1 hit
PRINTSⁱ	PR00075 FACDDSATRASE
PROSITEⁱ	View protein in PROSITE PS00476 FATTY_ACID_DESATUR_1, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ACOD1_RAT
Accessionⁱ	P07308Primary (citable) accession number: P07308 Secondary accession number(s): Q8JZL5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
	Last sequence update:	November 23, 2004
	Last modified:	November 7, 2018
	This is version 156 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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UniProtKB - P07308 (ACOD1_RAT)

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Acyl-CoA desaturase 1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Endoplasmic reticulum

Other locations

Endoplasmic reticulum

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ