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Entry version 198 (07 Apr 2021)
Sequence version 3 (01 Nov 1997)
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Protein

Fatty acid synthase

Gene

Fasn

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

Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain.1 Publication4 Publications

<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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Cerulenin, a potent non-competitive pharmacological inhibitor of FAS, binds covalently to the active site of the condensing enzyme region, inactivating a key enzyme step in fatty acid synthesis (PubMed:16969344). Another inhibitor, though less efficient, is C75, a member of the alpha-methylene-gamma-butyrolactone chemical class, also proposed as an antitumour and anti-obesity agent (PubMed:15715522).2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

    1. Vmax=300 nmol/min/mg enzyme for the overall fatty acid synthase reaction1 Publication
    2. Vmax=900 nmol/min/mg enzyme for the beta-ketoacyl reductase reaction of acetoacetyl-CoA1 Publication
    3. Vmax=25 nmol/min/mg enzyme for the enoyl reductase reaction1 Publication
    4. Vmax=25 nmol/min/mg enzyme for the thioesterase reaction1 Publication
    5. Vmax=3 nmol/min/mg enzyme for the beta-ketoacyl synthase reaction2 Publications
    6. Vmax=16 nmol/min/µg enzyme for the transferase reaction using malonyl-CoA as donor1 Publication
    7. Vmax=1.6 nmol/min/µg enzyme for the beta-ketoacyl reductase reaction of acetoacetyl-CoA1 Publication
    8. Vmax=2.5 nmol/min/µg enzyme for the fatty acid synthase reaction1 Publication
    9. Vmax=0.72 nmol/min/µg enzyme for the thioesterase reaction1 Publication
    10. Vmax=1.9 nmol/min/µg enzyme for the enoyl reductase reaction1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid biosynthesis

    This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.3 Publications
    View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei161For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
    Active sitei581For malonyltransferase activityPROSITE-ProRule annotation1
    <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 sitei671Acyl-CoABy similarity1
    Binding sitei773Acyl-CoABy similarity1
    Active sitei878For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation1
    Active sitei2302For thioesterase activityPROSITE-ProRule annotation1
    Active sitei2475For thioesterase activityPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1665 – 1682NADP; for enoyl reductase activityAdd BLAST18
    Nucleotide bindingi1765 – 1780NADP; for ketoreductase activityAdd BLAST16

    <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

    <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 functionHydrolase, Lyase, Multifunctional enzyme, Oxidoreductase, Transferase
    Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
    LigandNAD, NADP, Pyridoxal phosphate

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-RNO-163765, ChREBP activates metabolic gene expression
    R-RNO-199220, Vitamin B5 (pantothenate) metabolism
    R-RNO-75105, Fatty acyl-CoA biosynthesis

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P12785

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00094

    Protein family/group databases

    ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

    More...
    ESTHERi
    ratno-fas, Thioesterase

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000001864

    <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:
    Fatty acid synthase (EC:2.3.1.853 Publications)
    Alternative name(s):
    Type I FAS1 Publication
    Including the following 7 domains:
    [Acyl-carrier-protein] S-acetyltransferase (EC:2.3.1.383 Publications)
    [Acyl-carrier-protein] S-malonyltransferase (EC:2.3.1.391 Publication)
    3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.413 Publications)
    3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.1003 Publications)
    3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.592 Publications)
    Enoyl-[acyl-carrier-protein] reductase (EC:1.3.1.393 Publications)
    Acyl-[acyl-carrier-protein] hydrolase (EC:3.1.2.14)
    <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:Fasn
    <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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
    <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 10

    Organism-specific databases

    Rat genome database

    More...
    RGDi
    620665, Fasn

    <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

    Keywords - Cellular componenti

    Cytoplasm

    <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

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3783

    <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_00001802791 – 2505Fatty acid synthaseAdd BLAST2505

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineBy similarity1
    Modified residuei59N6-acetyllysineBy similarity1
    Modified residuei63PhosphoserineBy similarity1
    Modified residuei70N6-acetyllysineBy similarity1
    Modified residuei207PhosphoserineBy similarity1
    Modified residuei298N6-acetyllysineBy similarity1
    Modified residuei528N6-acetyllysineBy similarity1
    Modified residuei673N6-acetyllysineBy similarity1
    Modified residuei725PhosphoserineCombined sources1
    Modified residuei790N6-acetyllysineBy similarity1
    Modified residuei993N6-acetyllysineBy similarity1
    Modified residuei1276N6-acetyllysineBy similarity1
    Modified residuei1464S-nitrosocysteineBy similarity1
    Modified residuei1578PhosphoserineCombined sources1
    Modified residuei1588PhosphoserineBy similarity1
    Modified residuei1698N6-(pyridoxal phosphate)lysine; alternateBy similarity1
    Modified residuei1698N6-acetyllysine; alternateBy similarity1
    Modified residuei1765N6-acetyllysineBy similarity1
    Modified residuei1841N6-acetyllysineBy similarity1
    Modified residuei1989N6-acetyllysineBy similarity1
    Modified residuei2085S-nitrosocysteineBy similarity1
    Modified residuei2151O-(pantetheine 4'-phosphoryl)serine; alternatePROSITE-ProRule annotation1
    Modified residuei2151Phosphoserine; alternateCombined sources1
    Modified residuei2191PhosphoserineCombined sources1
    Modified residuei2230PhosphoserineBy similarity1
    Modified residuei2385N6-acetyllysineBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki2443Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    S-nitrosylation of Fatty acid synthase at cysteine residues Cys-1464 or Cys-2085 is important for the enzyme dimerization. In adipocytes, S-nitrosylation of Fatty acid synthase occurs under physiological conditions and gradually increases during adipogenesis.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphopantetheine, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P12785

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

    More...
    PaxDbi
    P12785

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P12785

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P12785

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P12785

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

    More...
    PhosphoSitePlusi
    P12785

    <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 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 livers of rats fed on a high carbohydrate diet.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSRNOG00000045636, Expressed in liver and 21 other tissues

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P12785, 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

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer which is arranged in a head to tail fashion (By similarity).

    Interacts with CEACAM1; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (PubMed:16054098).

    By similarity1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    P12785
    With#Exp.IntAct
    itself9EBI-493558,EBI-493558

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    248415, 3 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-33893N

    Protein interaction database and analysis system

    More...
    IntActi
    P12785, 2 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    10116.ENSRNOP00000064445

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P12785

    <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

    Secondary structure

    12505
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Biological Magnetic Resonance Data Bank

    More...
    BMRBi
    P12785

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

    More...
    SMRi
    P12785

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P12785

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2113 – 2193CarrierPROSITE-ProRule annotationAdd BLAST81

    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>Regioni1 – 413Beta-ketoacyl synthaseAdd BLAST413
    Regioni429 – 817Acyl and malonyl transferasesAdd BLAST389
    Regioni647 – 648Acyl-CoA bindingBy similarity2
    Regioni1629 – 1857Enoyl reductaseAdd BLAST229
    Regioni1858 – 2113Beta-ketoacyl reductaseAdd BLAST256
    Regioni2202 – 2505ThioesteraseAdd BLAST304

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1202, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000157276

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_000022_31_7_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P12785

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    CKVYYAS

    Database of Orthologous Groups

    More...
    OrthoDBi
    19161at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P12785

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.1200.10, 1 hit
    1.10.1470.20, 1 hit
    3.10.129.110, 1 hit
    3.40.366.10, 1 hit
    3.40.47.10, 1 hit
    3.40.50.1820, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029058, AB_hydrolase
    IPR001227, Ac_transferase_dom_sf
    IPR036736, ACP-like_sf
    IPR014043, Acyl_transferase
    IPR016035, Acyl_Trfase/lysoPLipase
    IPR013149, ADH_C
    IPR023102, Fatty_acid_synthase_dom_2
    IPR011032, GroES-like_sf
    IPR018201, Ketoacyl_synth_AS
    IPR014031, Ketoacyl_synth_C
    IPR014030, Ketoacyl_synth_N
    IPR016036, Malonyl_transacylase_ACP-bd
    IPR013217, Methyltransf_12
    IPR036291, NAD(P)-bd_dom_sf
    IPR032821, PKS_assoc
    IPR020841, PKS_Beta-ketoAc_synthase_dom
    IPR020807, PKS_dehydratase
    IPR042104, PKS_dehydratase_sf
    IPR020843, PKS_ER
    IPR013968, PKS_KR
    IPR020806, PKS_PP-bd
    IPR009081, PP-bd_ACP
    IPR006162, Ppantetheine_attach_site
    IPR029063, SAM-dependent_MTases
    IPR001031, Thioesterase
    IPR016039, Thiolase-like

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00698, Acyl_transf_1, 1 hit
    PF00107, ADH_zinc_N, 1 hit
    PF16197, KAsynt_C_assoc, 1 hit
    PF00109, ketoacyl-synt, 1 hit
    PF02801, Ketoacyl-synt_C, 1 hit
    PF08659, KR, 1 hit
    PF08242, Methyltransf_12, 1 hit
    PF00550, PP-binding, 1 hit
    PF14765, PS-DH, 1 hit
    PF00975, Thioesterase, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00827, PKS_AT, 1 hit
    SM00826, PKS_DH, 1 hit
    SM00829, PKS_ER, 1 hit
    SM00825, PKS_KS, 1 hit
    SM00823, PKS_PP, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF47336, SSF47336, 1 hit
    SSF50129, SSF50129, 1 hit
    SSF51735, SSF51735, 2 hits
    SSF52151, SSF52151, 1 hit
    SSF53335, SSF53335, 1 hit
    SSF53474, SSF53474, 1 hit
    SSF53901, SSF53901, 1 hit
    SSF55048, SSF55048, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00606, B_KETOACYL_SYNTHASE, 1 hit
    PS50075, CARRIER, 1 hit
    PS00012, PHOSPHOPANTETHEINE, 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.

    P12785-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR
    60 70 80 90 100
    SGKLKDLSKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL
    110 120 130 140 150
    RGTNTGVWVG VSGSEASEAL SRDPETLLGY SMVGCQRAMM ANRLSFFFDF
    160 170 180 190 200
    KGPSIALDTA CSSSLLALQN AYQAIRSGEC PAAIVGGINL LLKPNTSVQF
    210 220 230 240 250
    MKLGMLSPDG TCRSFDDSGN GYCRAEAVVA VLLTKKSLAR RVYATILNAG
    260 270 280 290 300
    TNTDGCKEQG VTFPSGEAQE QLIRSLYQPG GVAPESLEYI EAHGTGTKVG
    310 320 330 340 350
    DPQELNGITR SLCAFRQSPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEN
    360 370 380 390 400
    GVWAPNLHFH NPNPEIPALL DGRLQVVDRP LPVRGGIVGI NSFGFGGANV
    410 420 430 440 450
    HVILQPNTQQ APAPAPHAAL PHLLHASGRT MEAVQGLLEQ GRQHSQDLAF
    460 470 480 490 500
    VSMLNDIAAT PTAAMPFRGY TVLGVEGHVQ EVQQVPASQR PLWFICSGMG
    510 520 530 540 550
    TQWRGMGLSL MRLDSFRESI LRSDEALKPL GVKVSDLLLS TDEHTFDDIV
    560 570 580 590 600
    HSFVSLTAIQ IALIDLLTSM GLKPDGIIGH SLGEVACGYA DGCLSQREAV
    610 620 630 640 650
    LAAYWRGQCI KDANLPAGSM AAVGLSWEEC KQRCPPGVVP ACHNSEDTVT
    660 670 680 690 700
    ISGPQAAVNE FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK
    710 720 730 740 750
    VIREPRPRSA RWLSTSIPEA QWQSSLARTS SAEYNVNNLV SPVLFQEALW
    760 770 780 790 800
    HVPEHAVVLE IAPHALLQAV LKRGVKPSCT IIPLMKRDHK DNLEFFLTNL
    810 820 830 840 850
    GKVHLTGIDI NPNALFPPVE FPVPRGTPLI SPHIKWDHSQ TWDIPVAEDF
    860 870 880 890 900
    PNGSSSSSAT VYNIDASSES SDHYLVDHCI DGRVLFPGTG YLYLVWKTLA
    910 920 930 940 950
    RSLSLSLEET PVVFENVTFH QATILPRTGT VPLEVRLLEA SHAFEVSDSG
    960 970 980 990 1000
    NLIVSGKVYQ WEDPDSKLFD HPEVPIPAES ESVSRLTQGE VYKELRLRGY
    1010 1020 1030 1040 1050
    DYGPHFQGVY EATLEGEQGK LLWKDNWVTF MDTMLQISIL GFSKQSLQLP
    1060 1070 1080 1090 1100
    TRVTAIYIDP ATHLQKVYML EGDTQVADVT TSRCLGVTVS GGVYISRLQT
    1110 1120 1130 1140 1150
    TATSRRQQEQ LVPTLEKFVF TPHVEPECLS ESAILQKELQ LCKGLAKALQ
    1160 1170 1180 1190 1200
    TKATQQGLKM TVPGLEDLPQ HGLPRLLAAA CQLQLNGNLQ LELGEVLARE
    1210 1220 1230 1240 1250
    RLLLPEDPLI SGLLNSQALK ACIDTALENL STLKMKVVEV LAGEGHLYSH
    1260 1270 1280 1290 1300
    ISALLNTQPM LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWDPSGPAPT
    1310 1320 1330 1340 1350
    NLGALDLVVC NCALATLGDP ALALDNMVAA LKDGGFLLMH TVLKGHALGE
    1360 1370 1380 1390 1400
    TLACLPSEVQ PGPSFLSQEE WESLFSRKAL HLVGLKKSFY GTALFLCRRL
    1410 1420 1430 1440 1450
    SPQDKPIFLP VEDTSFQWVD SLKSILATSS SQPVWLTAMN CPTSGVVGLV
    1460 1470 1480 1490 1500
    NCLRKEPGGH RIRCILLSNL SSTSHVPKLD PGSSELQKVL ESDLVMNVYR
    1510 1520 1530 1540 1550
    DGAWGAFRHF QLEQDKPEEQ TAHAFVNVLT RGDLASIRWV SSPLKHMQPP
    1560 1570 1580 1590 1600
    SSSGAQLCTV YYASLNFRDI MLATGKLSPD AIPGKWASRD CMLGMEFSGR
    1610 1620 1630 1640 1650
    DKCGRRVMGL VPAEGLATSV LLSPDFLWDV PSSWTLEEAA SVPVVYTTAY
    1660 1670 1680 1690 1700
    YSLVVRGRIQ HGETVLIHSG SGGVGQAAIS IALSLGCRVF TTVGSAEKRA
    1710 1720 1730 1740 1750
    YLQARFPQLD DTSFANSRDT SFEQHVLLHT GGKGVDLVLN SLAEEKLQAS
    1760 1770 1780 1790 1800
    VRCLAQHGRF LEIGKFDLSN NHPLGMAIFL KNVTFHGILL DALFEGANDS
    1810 1820 1830 1840 1850
    WREVAELLKA GIRDGVVKPL KCTVFPKAQV EDAFRYMAQG KHIGKVLVQV
    1860 1870 1880 1890 1900
    REEEPEAMLP GAQPTLISAI SKTFCPEHKS YIITGGLGGF GLELARWLVL
    1910 1920 1930 1940 1950
    RGAQRLVLTS RSGIRTGYQA KHVREWRRQG IHVLVSTSNV SSLEGARALI
    1960 1970 1980 1990 2000
    AEATKLGPVG GVFNLAMVLR DAMLENQTPE LFQDVNKPKY NGTLNLDRAT
    2010 2020 2030 2040 2050
    REACPELDYF VAFSSVSCGR GNAGQSNYGF ANSTMERICE QRRHDGLPGL
    2060 2070 2080 2090 2100
    AVQWGAIGDV GIILEAMGTN DTVVGGTLPQ RISSCMEVLD LFLNQPHAVL
    2110 2120 2130 2140 2150
    SSFVLAEKKA VAHGDGEAQR DLVKAVAHIL GIRDLAGINL DSSLADLGLD
    2160 2170 2180 2190 2200
    SLMGVEVRQI LEREHDLVLP IREVRQLTLR KLQEMSSKAG SDTELAAPKS
    2210 2220 2230 2240 2250
    KNDTSLKQAQ LNLSILLVNP EGPTLTRLNS VQSSERPLFL VHPIEGSITV
    2260 2270 2280 2290 2300
    FHSLAAKLSV PTYGLQCTQA APLDSIPNLA AYYIDCIKQV QPEGPYRVAG
    2310 2320 2330 2340 2350
    YSFGACVAFE MCSQLQAQQG PAPAHNNLFL FDGSHTYVLA YTQSYRAKLT
    2360 2370 2380 2390 2400
    PGCEAEAEAE AICFFIKQFV DAEHSKVLEA LLPLKSLEDR VAAAVDLITR
    2410 2420 2430 2440 2450
    SHQSLDRRDL SFAAVSFYYK LRAADQYKPK AKYHGNVILL RAKTGGTYGE
    2460 2470 2480 2490 2500
    DLGADYNLSQ VCDGKVSVHI IEGDHRTLLE GRGLESIINI IHSSLAEPRV

    SVREG
    Length:2,505
    Mass (Da):272,650
    Last modified:November 1, 1997 - v3
    <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:i5810EC13D37F3114
    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 conflicti184I → T in AAA41145 (PubMed:1736293).Curated1
    Sequence conflicti871S → P in CAA31780 (PubMed:2915923).Curated1
    Sequence conflicti2085C → P in AAA41144 (PubMed:2891707).Curated1
    Sequence conflicti2106A → V in AAA57219 (PubMed:2717611).Curated1
    Sequence conflicti2106A → V in AAA41145 (PubMed:1736293).Curated1
    Sequence conflicti2106A → V in CAA31882 (PubMed:3109907).Curated1
    Sequence conflicti2296Y → H in AAA57219 (PubMed:2717611).Curated1
    Sequence conflicti2296Y → H in CAA31882 (PubMed:3109907).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
    M76767 mRNA Translation: AAA57219.1
    X62888 mRNA Translation: CAA44679.1
    X62889 Genomic DNA Translation: CAA44680.1
    M84761 Genomic DNA Translation: AAA41145.1
    X13415 mRNA Translation: CAA31780.1
    X13527 mRNA Translation: CAA31882.1
    J03514 mRNA Translation: AAA41144.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A30313, XYRTFA

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_059028.1, NM_017332.1

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSRNOT00000073321; ENSRNOP00000064445; ENSRNOG00000045636

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    50671

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    rno:50671

    <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
    M76767 mRNA Translation: AAA57219.1
    X62888 mRNA Translation: CAA44679.1
    X62889 Genomic DNA Translation: CAA44680.1
    M84761 Genomic DNA Translation: AAA41145.1
    X13415 mRNA Translation: CAA31780.1
    X13527 mRNA Translation: CAA31882.1
    J03514 mRNA Translation: AAA41144.1
    PIRiA30313, XYRTFA
    RefSeqiNP_059028.1, NM_017332.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2PNGNMR-A2114-2202[»]
    BMRBiP12785
    SMRiP12785
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi248415, 3 interactors
    DIPiDIP-33893N
    IntActiP12785, 2 interactors
    STRINGi10116.ENSRNOP00000064445

    Chemistry databases

    BindingDBiP12785
    ChEMBLiCHEMBL3783
    SwissLipidsiSLP:000001864

    Protein family/group databases

    ESTHERiratno-fas, Thioesterase

    PTM databases

    CarbonylDBiP12785
    iPTMnetiP12785
    PhosphoSitePlusiP12785

    Proteomic databases

    jPOSTiP12785
    PaxDbiP12785
    PRIDEiP12785

    Genome annotation databases

    EnsembliENSRNOT00000073321; ENSRNOP00000064445; ENSRNOG00000045636
    GeneIDi50671
    KEGGirno:50671

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    2194
    RGDi620665, Fasn

    Phylogenomic databases

    eggNOGiKOG1202, Eukaryota
    GeneTreeiENSGT00940000157276
    HOGENOMiCLU_000022_31_7_1
    InParanoidiP12785
    OMAiCKVYYAS
    OrthoDBi19161at2759
    PhylomeDBiP12785

    Enzyme and pathway databases

    UniPathwayiUPA00094
    ReactomeiR-RNO-163765, ChREBP activates metabolic gene expression
    R-RNO-199220, Vitamin B5 (pantothenate) metabolism
    R-RNO-75105, Fatty acyl-CoA biosynthesis
    SABIO-RKiP12785

    Miscellaneous databases

    EvolutionaryTraceiP12785

    Protein Ontology

    More...
    PROi
    PR:P12785

    Gene expression databases

    BgeeiENSRNOG00000045636, Expressed in liver and 21 other tissues
    GenevisibleiP12785, RN

    Family and domain databases

    Gene3Di1.10.1200.10, 1 hit
    1.10.1470.20, 1 hit
    3.10.129.110, 1 hit
    3.40.366.10, 1 hit
    3.40.47.10, 1 hit
    3.40.50.1820, 1 hit
    InterProiView protein in InterPro
    IPR029058, AB_hydrolase
    IPR001227, Ac_transferase_dom_sf
    IPR036736, ACP-like_sf
    IPR014043, Acyl_transferase
    IPR016035, Acyl_Trfase/lysoPLipase
    IPR013149, ADH_C
    IPR023102, Fatty_acid_synthase_dom_2
    IPR011032, GroES-like_sf
    IPR018201, Ketoacyl_synth_AS
    IPR014031, Ketoacyl_synth_C
    IPR014030, Ketoacyl_synth_N
    IPR016036, Malonyl_transacylase_ACP-bd
    IPR013217, Methyltransf_12
    IPR036291, NAD(P)-bd_dom_sf
    IPR032821, PKS_assoc
    IPR020841, PKS_Beta-ketoAc_synthase_dom
    IPR020807, PKS_dehydratase
    IPR042104, PKS_dehydratase_sf
    IPR020843, PKS_ER
    IPR013968, PKS_KR
    IPR020806, PKS_PP-bd
    IPR009081, PP-bd_ACP
    IPR006162, Ppantetheine_attach_site
    IPR029063, SAM-dependent_MTases
    IPR001031, Thioesterase
    IPR016039, Thiolase-like
    PfamiView protein in Pfam
    PF00698, Acyl_transf_1, 1 hit
    PF00107, ADH_zinc_N, 1 hit
    PF16197, KAsynt_C_assoc, 1 hit
    PF00109, ketoacyl-synt, 1 hit
    PF02801, Ketoacyl-synt_C, 1 hit
    PF08659, KR, 1 hit
    PF08242, Methyltransf_12, 1 hit
    PF00550, PP-binding, 1 hit
    PF14765, PS-DH, 1 hit
    PF00975, Thioesterase, 1 hit
    SMARTiView protein in SMART
    SM00827, PKS_AT, 1 hit
    SM00826, PKS_DH, 1 hit
    SM00829, PKS_ER, 1 hit
    SM00825, PKS_KS, 1 hit
    SM00823, PKS_PP, 1 hit
    SUPFAMiSSF47336, SSF47336, 1 hit
    SSF50129, SSF50129, 1 hit
    SSF51735, SSF51735, 2 hits
    SSF52151, SSF52151, 1 hit
    SSF53335, SSF53335, 1 hit
    SSF53474, SSF53474, 1 hit
    SSF53901, SSF53901, 1 hit
    SSF55048, SSF55048, 1 hit
    PROSITEiView protein in PROSITE
    PS00606, B_KETOACYL_SYNTHASE, 1 hit
    PS50075, CARRIER, 1 hit
    PS00012, PHOSPHOPANTETHEINE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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 nameiFAS_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: P12785
    Secondary accession number(s): O09187
    , O09190, Q63577, Q64717
    <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: October 1, 1989
    Last sequence update: November 1, 1997
    Last modified: April 7, 2021
    This is version 198 of the entry and version 3 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

    3D-structure, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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