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UniProtKB - P07308 (ACOD1_RAT)

Entry version 170 (23 Feb 2022)
Sequence version 2 (23 Nov 2004)
Previous versions | rss
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Protein

Acyl-CoA desaturase 1

Gene

Scd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Stearoyl-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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei74SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi119Iron 1By similarity1
Metal bindingi124Iron 1By similarity1
Binding sitei147SubstrateBy similarity1
Binding sitei154SubstrateBy similarity1
Binding sitei155SubstrateBy similarity1
Metal bindingi156Iron 1By similarity1
Metal bindingi159Iron 2By similarity1
Metal bindingi160Iron 1By similarity1
Binding sitei187SubstrateBy similarity1
Binding sitei188SubstrateBy similarity1
Binding sitei261SubstrateBy similarity1
Metal bindingi268Iron 2By similarity1
Metal bindingi297Iron 2By similarity1
Metal bindingi300Iron 1By similarity1
Metal bindingi301Iron 2By similarity1

<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

  • iron ion binding Source: UniProtKB
  • metal ion binding Source: RGD
  • oxidoreductase activity Source: UniProtKB
  • palmitoyl-CoA 9-desaturase activity Source: RGD
  • stearoyl-CoA 9-desaturase activity Source: UniProtKB
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.14.19.1, 5301

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Scd1
Synonyms:Scd
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Rat genome database

More...RGDi		621176, Scd1

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 71CytoplasmicBy similarityAdd BLAST71
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei72 – 92HelicalBy similarityAdd BLAST21
Topological domaini93 – 96LumenalBy similarity4
Transmembranei97 – 117HelicalBy similarityAdd BLAST21
Topological domaini118 – 216CytoplasmicBy similarityAdd BLAST99
Transmembranei217 – 236HelicalBy similarityAdd BLAST20
Topological domaini237 – 240LumenalBy similarity4
Transmembranei241 – 262HelicalBy similarityAdd BLAST22
Topological domaini263 – 358CytoplasmicBy similarityAdd BLAST96

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi119H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi124H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi156H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi157R → N: No effect on enzyme activity. 1 Publication1
Mutagenesisi159H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi160H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi166H → A: No effect on enzyme activity. 1 Publication1
Mutagenesisi170H → A: No effect on enzyme activity; when associated with H-173. 1 Publication1
Mutagenesisi173R → H: No effect on enzyme activity; when associated with A-170. 1 Publication1
Mutagenesisi297H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi300H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi301H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi315H → A: No effect on enzyme activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5424

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001854001 – 358Acyl-CoA desaturase 1Add BLAST358

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P07308

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P07308

PeptideAtlas

More...PeptideAtlasi		P07308

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P07308

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P07308

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000013552, Expressed in liver and 22 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P07308, RN

<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

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		251497, 1 interactor

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000018447

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P07308

<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

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P07308

Database of comparative protein structure models

More...ModBasei		Search...

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni8 – 33DisorderedSequence analysisAdd BLAST26

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi119 – 124Histidine box-1Curated6
Motifi156 – 160Histidine box-2Curated5
Motifi297 – 301Histidine box-3Curated5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi8 – 27Polar residuesSequence analysisAdd BLAST20

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<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

Belongs to the fatty acid desaturase type 1 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1600, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000162971

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_027359_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07308

Identification of Orthologs from Complete Genome Data

More...OMAi		QGFRWWE

Database of Orthologous Groups

More...OrthoDBi		971318at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd03505, Delta9-FADS-like, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR015876, Acyl-CoA_DS
IPR005804, FA_desaturase_dom
IPR001522, FADS-1_CS

The PANTHER Classification System

More...PANTHERi		PTHR11351, PTHR11351, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00487, FA_desaturase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00075, FACDDSATRASE

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00476, FATTY_ACID_DESATUR_1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P07308-1 [UniParc]FASTAAdd 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB4C960A969B63774
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti291A → S in AAA42116 (PubMed:2428815).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
J02585 mRNA Translation: AAA42116.1
AF509568 mRNA Translation: AAM34745.1
AF509569 mRNA Translation: AAM34746.1

Protein sequence database of the Protein Information Resource

More...PIRi		A24699

NCBI Reference Sequences

More...RefSeqi		NP_631931.2, NM_139192.2
XP_006231495.1, XM_006231433.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000018447; ENSRNOP00000018447; ENSRNOG00000013552

Database of genes from NCBI RefSeq genomes

More...GeneIDi		246074

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:246074

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02585 mRNA Translation: AAA42116.1
AF509568 mRNA Translation: AAM34745.1
AF509569 mRNA Translation: AAM34746.1
PIRiA24699
RefSeqiNP_631931.2, NM_139192.2
XP_006231495.1, XM_006231433.2

3D structure databases

SMRiP07308
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi251497, 1 interactor
STRINGi10116.ENSRNOP00000018447

Chemistry databases

BindingDBiP07308
ChEMBLiCHEMBL5424

PTM databases

iPTMnetiP07308
PhosphoSitePlusiP07308

Proteomic databases

jPOSTiP07308
PaxDbiP07308
PeptideAtlasiP07308

Genome annotation databases

EnsembliENSRNOT00000018447; ENSRNOP00000018447; ENSRNOG00000013552
GeneIDi246074
KEGGirno:246074

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6319
RGDi621176, Scd1

Phylogenomic databases

eggNOGiKOG1600, Eukaryota
GeneTreeiENSGT00940000162971
HOGENOMiCLU_027359_0_0_1
InParanoidiP07308
OMAiQGFRWWE
OrthoDBi971318at2759

Enzyme and pathway databases

BRENDAi1.14.19.1, 5301

Miscellaneous databases

Protein Ontology

More...PROi		PR:P07308

Gene expression databases

BgeeiENSRNOG00000013552, Expressed in liver and 22 other tissues
GenevisibleiP07308, RN

Family and domain databases

CDDicd03505, Delta9-FADS-like, 1 hit
InterProiView protein in InterPro
IPR015876, Acyl-CoA_DS
IPR005804, FA_desaturase_dom
IPR001522, FADS-1_CS
PANTHERiPTHR11351, PTHR11351, 1 hit
PfamiView protein in Pfam
PF00487, FA_desaturase, 1 hit
PRINTSiPR00075, FACDDSATRASE
PROSITEiView protein in PROSITE
PS00476, FATTY_ACID_DESATUR_1, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACOD1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07308
Secondary accession number(s): Q8JZL5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 23, 2004
Last modified: February 23, 2022
This is version 170 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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