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UniProtKB - P12785 (FAS_RAT)

Entry version 198 (07 Apr 2021)
Sequence version 3 (01 Nov 1997)
Previous versions | rss
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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

    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 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 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 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

    Complete GO annotation on QuickGO ...

    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
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            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
    UniProt is an ELIXIR core data resource
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